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(cis)-Pro in microtubule associated protein tau
(trans)-Pro in microtubule associated protein tau
-
-
-
?
(cis)-Pro residue in HIF-1alpha
(trans)-Pro residue in HIF-1alpha
-
-
-
r
(cis)-Pro residue in nuclease Nuc
(trans)-Pro residue in nuclease Nuc
(cis)-Pro residue in phosphorylated protein PERIOD
(trans)-Pro residue in phosphorylated protein PERIOD
phosphorylated isoforms of PERIOD serve as Dod substrates, leading to Dod-mediated conformational changes of PERIOD
-
-
r
(cis)-Pro residue in protein FOXO3
(trans)-Pro residue in protein FOXO3
-
-
-
r
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
acetyl-Ala-Ala-(cis)-Pro-Ala-Lys-NH2
acetyl-Ala-Ala-(trans)-Pro-Ala-Lys-NH2
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
Ala-Ala-(cis)-Pro-Ala
Ala-Ala-(trans)-Pro-Ala
-
-
-
?
Ala-Ala-(trans)-Pro-Phe
Ala-Ala-(cis)-Pro-Phe
-
-
-
r
Ala-Ala-Ala-(trans)-Pro-Phe
Ala-Ala-Ala-(cis)-Pro-Phe
-
-
-
r
Ala-Gln-(cis)-Pro-Phe
Ala-Gln-(trans)-Pro-Phe
Ala-Glu-(cis)-Pro-Phe
Ala-Glu-(trans)-Pro-Phe
Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
Ala-Gly-PSI[CS-N]-Pro-Phe-4-nitroanilide
?
-
-
-
-
?
Ala-Ile-(cis)-Pro-Phe
Ala-Ile-(trans)-Pro-Phe
Ala-Leu-(cis)-Pro-Phe
Ala-Leu-(trans)-Pro-Phe
Ala-Nle-(cis)-Pro-Phe
Ala-Nle-(trans)-Pro-Phe
Ala-Ser(PO3H2)-(cis)-Pro
Ala-Ser(PO3H2)-(trans)-Pro
-
-
-
?
Ala-Ser(PO3H2)-(cis)-Pro-Arg
Ala-Ser(PO3H2)-(trans)-Pro-Arg
-
-
-
?
Ala-Val-(cis)-Pro-Phe
Ala-Val-(trans)-Pro-Phe
-
-
?
amyloidbeta precursor protein
?
-
interaction with Thr688
-
-
?
barstar C40A/C82A/P27A
?
-
the mutant of barstar lacks complications arising from oxidation of Cys in wild-type or isomerization affecting the peptidyl-Pro27 bond. Refolding is comprised by several kinetically detectable folding phases. The slowest phase in refolding, the trans to cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state
-
?
cis-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
trans-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
GFPRALPAWARPDYNPPLVE
?
-
a synthetic peptide, named PepD2, corresponding to residues 304-323 of NS5A
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Pro-(cis)-Phe 4-nitroanilide
Glutaryl-Ala-Pro-(trans)-Phe 4-nitroanilide
-
-
-
?
hepatitis C virus NS5A protein
?
interleukin-2 tyrosine kinase
?
-
catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
?
N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
100% activity, Par45 shows a strong preference for a substrate with the basic Arg residue preceding Pro
-
-
?
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
7.6% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
Phe-Phe-L-pSer-Pro-Arg-pNA
?
-
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
protein tau
?
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
reduced carboxymethylated bovine alpha-lactalbumin
reduced carboxymethylated bovine alpha-lactalbumin
-
-
-
?
RNase A S-protein
RNase A S-protein
partially folded
action of enzyme greatly reduces the population of aggregated oligomeric species
-
?
Ser(PO3H2)-(cis)-Pro-Arg
Ser(PO3H2)-(trans)-Pro-Arg
-
-
-
?
Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
?
serine/threonine protein kinase B
?
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Ala-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
suc-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
suc-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-Pro-Phe-4-nitroanilide
?
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
Suc-Ala-Leu-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Leu-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
succinyl-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Arg-p-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Arg-p-nitroanilide
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
50% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Gln-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gln-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Gln-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gln-(trans)-Pro-Phe-4-nitroanilide
65% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Gln-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Gln-(trans)-Pro-Phe-p-nitroanilide
-
27% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
-
13% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-7-amido-4-methylcoumarin
succinyl-Ala-Glu-(cis)-Pro-Phe-7-amido-4-methylcoumarin
-
-
-
r
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Gly-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Gly-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-p-nitroanilide
-
37% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
succinyl-Ala-Leu-Pro(omega180)-Phe-4-nitroanilide
succinyl-Ala-Leu-Pro(omega0)-Phe-4-nitroanilide
the substrate binds to PvFKBD35 in a cis conformation involving residues D55, H67, V73, and I74
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Lys-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Lys-(trans)-Pro-Phe-4-nitroanilide
83% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Lys-Pro-Phe-4-nitroanilide
?
succinyl-Ala-Nle-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Nle-(trans)-Pro-Phe-4-nitroanilide
194% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-Pro-Phe-4-nitroanilide
?
-
-
-
-
?
succinyl-Ala-Ser-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ser-(trans)-Pro-Phe-4-nitroanilide
23% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Val-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Val-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Val-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Val-(trans)-Pro-Phe-4-nitroanilide
18% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Val-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Val-(trans)-Pro-Phe-p-nitroanilide
-
76% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Arg-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Arg-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Leu-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Leu-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Phe-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Phe-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ser-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ser-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide
?
-
-
-
-
?
Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide
Trp-Phe-Tyr-Ser(PO3H2)-(trans)-Pro-Arg-4-nitroanilide
-
-
-
-
?
TRYWNAKMK-(cis)-PFIFGA
TRYWNAKMK-(trans)-PFIFGA
VYKS-(cis)-PVVSGDTS-(cis)-PRHL
VYKS-(trans)-PVVSGDTS-(trans)-PRHL
interconversion occurs at both P5 and P13
-
-
?
additional information
?
-
(cis)-Pro residue in nuclease Nuc
(trans)-Pro residue in nuclease Nuc
-
-
-
r
(cis)-Pro residue in nuclease Nuc
(trans)-Pro residue in nuclease Nuc
-
-
-
r
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
-
-
-
-
?
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
-
?
AGL24 protein
?
-
-
-
-
?
AGL24 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
Ala-Gln-(cis)-Pro-Phe
Ala-Gln-(trans)-Pro-Phe
-
-
?
Ala-Gln-(cis)-Pro-Phe
Ala-Gln-(trans)-Pro-Phe
-
-
?
Ala-Glu-(cis)-Pro-Phe
Ala-Glu-(trans)-Pro-Phe
-
-
?
Ala-Glu-(cis)-Pro-Phe
Ala-Glu-(trans)-Pro-Phe
-
-
?
Ala-Ile-(cis)-Pro-Phe
Ala-Ile-(trans)-Pro-Phe
-
-
?
Ala-Ile-(cis)-Pro-Phe
Ala-Ile-(trans)-Pro-Phe
-
-
?
Ala-Leu-(cis)-Pro-Phe
Ala-Leu-(trans)-Pro-Phe
-
-
?
Ala-Leu-(cis)-Pro-Phe
Ala-Leu-(trans)-Pro-Phe
-
-
?
Ala-Nle-(cis)-Pro-Phe
Ala-Nle-(trans)-Pro-Phe
-
-
?
Ala-Nle-(cis)-Pro-Phe
Ala-Nle-(trans)-Pro-Phe
-
-
?
colicin M
?
-
-
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
hepatitis C virus NS5A protein
?
-
nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain. Mutations in this domain are linked to cyclosporin A resistance
-
-
?
hepatitis C virus NS5A protein
?
-
substrate is the domain 2 of the nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain, recombinantly expressed His-tagged substrate. Determination of direct molecular interaction between NS5A-D2 and both cyclophilins by NMR spectrometry, overview
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
r
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
6.9% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
ratio kcat to Km value is 15400 per M and s
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
?
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
?
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
ratio kcat to Km value is 397000 per M and s
-
?
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
26.7% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
4.3% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
preferred substrate
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
preferred substrate
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
computational study on protein dynamics, network of protein vibrations, comparison with structures from different species
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
-
solvent-assisted mechanism, H43 and Q52 are active sites
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
-
Pin1 prevents activation of Bax, prevents Bax cleavage by calpain, and prevents Bax translocation to mitochondria
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
-
i.e. Bax
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
-
-
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
-
-
-
-
?
RNA polymerase II
?
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
RNA polymerase II
?
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
RNAse T1
?
-
reduced and carboxymethylated form of the S54G/P55N variant of RNAse T1. In the native state the Rnase T1 contains a single prolyl bond Tyr38-Pro39. Of all reduced and carboxymethylated RNAse T1 molecules, 85% fold in a monophasic and reversible reaction, which is limited in rate by the slow trans to cis isomerization at Pro39
-
?
RNAse T1
?
-
reduced and carboxymethylated RNAse T1, refolding by trans to cis isomerization of peptidyl-prolyl bonds at Pro39 and Pro55
-
?
RNAse T1
?
RNase T1 refolding assay
-
-
?
RNAse T1
?
-
rate-limiting isomerization of -(trans)-Pro to -(cis)-Pro. Disulfide-reduced and S-carboxymethylated form of a variant of Rnase T1 with Ser54Gly and Pro55Asn. The trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
serine/threonine protein kinase B
?
-
-
-
-
?
serine/threonine protein kinase B
?
-
i.e. Akt, reduced activity with Akt mutants T92A/T450A and T92D/T450D. Akt-Pin1 interaction analysis using HA-tagged Akt and GST-tagged Pin1, overview
-
-
?
SOC1 protein
?
-
-
-
-
?
SOC1 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
-
-
?
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
trans
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
38% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
70fold decrease in activity compared with succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
11% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
67% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Lys-Pro-Phe-4-nitroanilide
?
-
-
-
-
?
succinyl-Ala-Lys-Pro-Phe-4-nitroanilide
?
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
mimicyp lacks peptidyl-prolyl isomerase activity
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
33% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
-
35% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
TRYWNAKMK-(cis)-PFIFGA
TRYWNAKMK-(trans)-PFIFGA
-
-
-
r
TRYWNAKMK-(cis)-PFIFGA
TRYWNAKMK-(trans)-PFIFGA
-
-
-
r
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24
-
-
?
additional information
?
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
additional information
?
-
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
additional information
?
-
-
only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity
-
?
additional information
?
-
-
only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity. The prolyl isomerases become essential for growth under starvation conditions
-
?
additional information
?
-
isoform Par27 displays both prolyl-peptidyl isomerase and chaperone activities in vitro
-
-
?
additional information
?
-
-
isoform Par27 displays both prolyl-peptidyl isomerase and chaperone activities in vitro
-
-
?
additional information
?
-
-
Par27 exhibits both chaperone and PPIase activities in vitro. Full-length and isolated PPIase domain show PPIase activity using either reduced carboxymethylated RNAse T1 or a 16-mer peptide as substrates, product analysis by NMR, overview. Functional analysis of enzyme domains and structure modeling, overview
-
-
?
additional information
?
-
-
catalyzes refolding of RNAase T1
-
-
?
additional information
?
-
-
the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
-
-
?
additional information
?
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
class3 cyclophilins are involved in cellular responses to stress caused by changes in redox environment or by upregulation of cellular activity
-
?
additional information
?
-
-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
the kinesin-related protein, KRMP1 is a mitotic target regulated by Pin1 and vice versa
-
?
additional information
?
-
-
increases the refolding of type IV procollagen
-
-
?
additional information
?
-
-
catalyzes the refolding of thermally denatured type III collagen
-
-
?
additional information
?
-
the enzyme has peptidylprolyl isomerase activity and chaperone activity
-
?
additional information
?
-
-
the enzyme has peptidylprolyl isomerase activity and chaperone activity
-
?
additional information
?
-
-
the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
-
-
?
additional information
?
-
-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
additional information
?
-
-
PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS, and derived model peptides. Substrate specificity of PpiD is less specific than that for isoform SurA. The substrate specificity of PpiD is determined more by the hydrophobicity of residues in the model peptides than the presence of aromatic residues
-
-
?
additional information
?
-
-
peptidyl-prolyl cis-trans isomerase FKBP22 binds FK506 and rapamycin, that are both immunosuppressive drugs
-
-
?
additional information
?
-
-
increases the refolding of type IV procollagen
-
-
?
additional information
?
-
-
catalyzes the refolding of type III collagen
-
-
?
additional information
?
-
purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
-
-
?
additional information
?
-
-
purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
-
-
?
additional information
?
-
purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
substrate specificity of the 3 isoforms
-
-
?
additional information
?
-
-
cyclophilin B complexed to cyclosporin A inhibits phosphatase activity of recombinant human calcineurin
-
?
additional information
?
-
-
no catalysis is observed with the substrates Ala-(cis)-Pro, Ala-Ala-(cis)-Pro, Ala-(cis)-Pro-Ala, Ser-(cis)-Pro and Ser(PO3H2)-(cis)-Pro
-
?
additional information
?
-
the mechanism determining the substrate specificity seems to be different between hPAR14 and hPin1
-
?
additional information
?
-
-
the mechanism determining the substrate specificity seems to be different between hPAR14 and hPin1
-
?
additional information
?
-
-
the presence of cyclophilin A in the human immunodeficiency virus type 1, HIV-1, is required for HIV-1 to infect and replicate
-
-
?
additional information
?
-
-
the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
-
-
?
additional information
?
-
cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
-
-
?
additional information
?
-
-
cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
-
-
?
additional information
?
-
-
enzyme is required for cell cycle progression
-
?
additional information
?
-
-
folding helper enzyme that plays a role in cell-cycle and chromatin remodeling
-
?
additional information
?
-
-
peptidylprolyl isomerase Pin1 interacts with Cdk9-phosphorylated hSpt5. Cdk9 dependent phosphorylation of Rpb1 and hSpt5 followed by Pin1 interaction might contribute to the regulation of transcription, pre-mRNA maturation and the dynamics of proteins in interphase and mitosis
-
?
additional information
?
-
substrates are proteins involved in regulation of cell cycle, transcription, Alzheimers disease, and cancer pathogenesis
-
?
additional information
?
-
-
the peptidylprolyl isomerase Cyp40, FKBP51 and FKBP52 are components of the Hsp90 chaperone complex. The peptidylprolyl isomerase monomers bind to a Hsp90 dimer. The three isomerase differ both in their affinity for Hsp90 and their chaperone activity suggesting that they play distinct roles in the Hsp90 chaperone complex
-
?
additional information
?
-
-
selective for substrate SRC-3, phosphorylated steroid receptor coactivator 3. Enzyme and SRC-3 synergistically activate nuclear-receptor-regulated transcription
-
-
?
additional information
?
-
enzyme isoform Pin1 interacts with Bruton tyrosine kinase in a cell-cycle dependent manner, regulating the Bruton tyrosine kinase expression level. Interaction requires a functionally intact tyrosine kinase and occurs via S21 and S115 residues of the kinase
-
-
?
additional information
?
-
-
enzyme isoform Pin1 interacts with Bruton tyrosine kinase in a cell-cycle dependent manner, regulating the Bruton tyrosine kinase expression level. Interaction requires a functionally intact tyrosine kinase and occurs via S21 and S115 residues of the kinase
-
-
?
additional information
?
-
isoform Pin1 modulates oxidative stress-induced neurofilament NF-H phosphorylation. In vitro, the addition of Pin1 substantially increases phosphorylation of NF-H KSP repeats by proline-directed kinases, Erk1/2, Cdk5/p35, and JNK3 in a concentration-dependent manner. In vivo, dominant-negative Pin1 and Pin1 small interfering RNA inhibit epidermal growth factor-induced NF-H phosphorylation
-
-
?
additional information
?
-
-
incorporation of the HCV polymerase into the replication complex depends on its interaction with a cellular chaperone protein, cyclosporine inhibits HCV replication by blocking this critical interaction and the PPIase activity of CyPA, modeling of the pathway, overview. CyPA is associated with CRC-incorporated HCV replicase in a cyclosporine-sensitive manner
-
-
?
additional information
?
-
-
Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
-
-
?
additional information
?
-
-
Pin1 enhances Plk1-mediated phosphorylation of the centrosome protein Cep55, overview
-
-
?
additional information
?
-
-
Pin1 interacts with human T-cell leukemia virus type 1 Tax, phosphorylated at Ser258, and modulates its activation of NF-kappaB. Pin1 contributes to Tax signaling through NF-kappaB, and it cooperates with Tax to enhance cellular proliferation
-
-
?
additional information
?
-
-
Pin1 interacts with NF-kappaB via its WW domain
-
-
?
additional information
?
-
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins from cis to trans, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, that produce the phosphorylated substrates of the isomerase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, regulation, overview
-
-
?
additional information
?
-
-
prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways
-
-
?
additional information
?
-
-
promyelocytic leukemia protein, PML, and silencing mediator for retinoic acid and thyroid hormone receptor, SMRT, are Pin1 substrates
-
-
?
additional information
?
-
-
Pin1 can stimulate proteins phosphorylation, e.g. of the RNA polymerase II CTD domain, but it can also inhibit protein dephosphorylation, e.g. of NFAT transcription factor or calcineurin. Pin1 interacts with neuronal cytoskeleton proteins such as tau, amyloid-beta protein precursor, alpha-synuclein, and with neurofilaments
-
-
?
additional information
?
-
-
Pin1 inhibits the dephosphorylation of NF by PP2A in vitro
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
Pin1 specifically recognizes the phosphorylated serine/threonine residue followed by proline. Pin1 binds preferentially to the phosphorylated Ser16-Pro17 motif of the capsid core of the human immunodeficiency virus type 1
-
-
?
additional information
?
-
Pin1 is a peptidyl-prolyl isomerase (PPIase), that catalyzes the cis-trans isomerization of pSer/pThr-Pro substrates in vivo and in vitro
-
-
?
additional information
?
-
-
the enzyme is not essential for Legionella pneumophila although the Cyp18-negative mutant strain is less infective for Acanthamoeba castellanii
-
-
?
additional information
?
-
-
the IF domain is a novel-folding motif and exposes a hydrophobic surface, which is considered to play an important role in the chaperone-like activity
-
?
additional information
?
-
-
the enzyme is involved in cell cycle progression
-
?
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
-
-
?
additional information
?
-
-
Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
-
-
?
additional information
?
-
-
neither the active domain nor the intact protein can catalyze the cis/trans isomerization of the tripeptide Ala-Pro-Phe, less than 5% of the activity with succinyl-Ala-Ala-Pro-Phe-p-nitroanilide is observed with: succinyl-Ala-Gly-Pro-Phe-p-nitroanilide, succinyl-Ala-Lys-Pro-Phe-p-nitroanilide, succinyl-Ala-Glu-Pro-Phe-p-nitroanilide. The organism is devoid of all known peptidyl-prolyl cis/trans isomerases except the trigger factor. The trigger factor shows dual function as chaperone and prolyl isomerase
-
?
additional information
?
-
-
the trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
additional information
?
-
-
protein is not involved in binding to macrophages and does not impair the ability of macrophages to phagocytose the gonococci
-
-
?
additional information
?
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Val-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Val-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
-
-
?
additional information
?
-
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
?
additional information
?
-
-
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
?
additional information
?
-
-
enzyme inhibits the phosphatase activity of calcineurin independently of FK506 binding. Enzyme also inhibits thermal aggregation of two model substrates indicating chaperone proterties
-
-
?
additional information
?
-
PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview
-
-
?
additional information
?
-
-
PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview
-
-
?
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
additional information
?
-
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins from cis to trans, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, that produce the phosphorylated substrates of the isomerase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, regulation, overview
-
-
?
additional information
?
-
-
prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways
-
-
?
additional information
?
-
-
Pin1 can stimulate proteins phosphorylation, e.g. of the RNA polymerase II CTD domain, but it can also inhibit protein dephosphorylation, e.g. of NFAT transcription factor or calcineurin. Pin1 interacts with neuronal cytoskeleton proteins such as tau, amyloid-beta protein precursor, alpha-synuclein, and with neurofilaments
-
-
?
additional information
?
-
-
Pin1 inhibits the dephosphorylation of NF by PP2A in vitro
-
-
?
additional information
?
-
-
cyclophilin A and Ess1 function in parallel pathways and act on common targets by a mechanism that requires prolyl isomerization. One of these targets is the Sin3-Rdp3 histone deacetylase complex. Cyclophilin A increases and Ess1 decreases disruption of gene silencing by this complex. Ess1 and cyclophilin A modulate the activity of the Sin3-Rdp3 complex, and excess histone deacetylation causes mitotic arrest in ess1 mutants
-
?
additional information
?
-
-
the peptidylprolyl isomerase activity of cyclophilin A promotes proper subcellular localization of Zpr1p. Zpr1p is an essential zinc-finger-containing protein that translocates to the nucleus in response to groth stimuli
-
?
additional information
?
-
-
Fpr4 mediates cis-trans conversion of proline residues within histone tails, Pro16 and Pro30 of histone H3 are the major proline targets of Fpr4, with little activity against Pro38, mechanistic importance of substrate residues C-terminal to the peptidylprolyl bond
-
-
?
additional information
?
-
-
proline isomerization of histone peptides by Fpr4(280-392)
-
-
?
additional information
?
-
-
enzyme enhances the refolding of urea-denatured ribonuclease A
-
-
?
additional information
?
-
-
enzyme increases refolding of denatured type III collagen
-
-
?
additional information
?
-
-
catalyzes slow steps in the refolding of a number of proteins. The efficiency of catalysis depends on the accessibility for the isomerase of the particular proline peptide bonds in the refolding protein chain
-
-
?
additional information
?
-
-
increases refolding of cytochrome c and RNAase T1
-
-
?
additional information
?
-
-
isomerase activity of peptidylprolyl isomerase is independent of the chaperone activity. The proper molar ratio is important for the chaperone activity. The cysteine residues of peptidylprolyl isomerase may be a peptide binding site, and may be an essential group for the chaperone function
-
?
additional information
?
-
-
the enzyme is essential for protein folding during protein synthesis and may be involved in events, such as those occuring early in T-cell activation
-
-
?
additional information
?
-
-
the enzyme shows chaperone-like protein refolding activity in addition to peptidylprolyl isomerase
-
?
additional information
?
-
-
cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins.The enzyme might be important at growth temperatures lower than the optimum in Thermococcus sp. KS-1
-
?
additional information
?
-
-
the enzyme shows chaperone-like protein refolding activity in addition to peptidylprolyl isomerase
-
?
additional information
?
-
-
cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins.The enzyme might be important at growth temperatures lower than the optimum in Thermococcus sp. KS-1
-
?
additional information
?
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
-
heat-stress-induced protein
-
?
additional information
?
-
Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds
-
-
?
additional information
?
-
-
Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
-
?
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
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(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
-
-
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
-
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
-
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
-
(6,8aR)-6-N,N-monophenylimino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: above 0.2 mM
(6R,8a,R)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.017 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-acetyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.0015 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.047 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-indolizidine methyl ester
-
dissociation constant: 0.077 mM
(6R,8aR)-6-benzyl-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.14 mM
(6R,8aR)-6-benzyl-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.124 mM
(6R,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: 0.2 mM
(6S,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: above 0.2 mM
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
-
(E)-6-phenylhexyl 3-(3,4-dihydroxyphenyl)acrylate
20 micorM, 15% residual activity
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
-
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
2,7-dimethylbenzo[lmn][3,8]phenanthroline-1,3,6,8(2H,7H)-tetrone
-
IC50: 0.002 mM
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
-
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
-
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
-
-
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
-
-
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
-
-
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells. Compound is able to significantly speed nerve regeneration in a rat sciatic nerve neurotomy model
5-hydroxy-1,4-naphthoquinone
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
-
-
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
-
-
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
-
-
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.127 mM
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.001 mM
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.085 mM
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
-
IC50: 7 mM
acetyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.77 mM
alpha-lactalbumin
-
unfolded
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
cyclic CRYPEVEIC
-
the cyclic peptide is specific for the active site of the PPIase domain
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
-
-
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
-
-
cyclolinopeptide A
-
interaction with several synthetic analogues cyclolinopeptide A
D-Ser(PO3H2)-Pro
-
1 mM, 20% inhibition
diethyl 1,3,8,10-tetrahydro-1,3,8,10-tetraoxoanthra[2,1,9-def:6,5,10-d'e'f']diisoquinoline-2,9-diacetate
-
IC50: 0.0015 mM
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo[lmn][3,8]phenanthroline 2,7-diacetate
-
IC50: 0.0015 mM, inhibitor with the least non-specific toxicity
dipentamethylene thiuram monosulfide
epigallocatechin-3-gallate
10 microM, 55% residual activity
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
lactalbumin
-
reduced and carboxymethylated, strong inhibition by the permanently unfolded protein
-
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
-
-
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
-
-
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
-
-
NEM
-
cytosolic enzyme form
non-folding vartiant of ribonuclease T1
-
that lacks Pro39
-
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.004 mM
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.097 mM
Phenylglyoxal
-
cytosolic enzyme form
QAEGPK
peptide corresponding to peptide QAEGP487KR at the N-terminus of the enzyme's isomerase domain. Peptide binds to the active site, but the enzyme does not catalyze its isomerization
RNase T1
-
reduced and carboxymethylated form of the P39A variant, strong inhibition by the permanently unfolded protein
-
Ser(PO3H2)-Pro
-
IC50: 2.0 mM
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.138 mM
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.02 mM. Selectively inhibits Cyp-18, but not enzyme isoform FKBP12
succinyl-Ala-Ala-Pro-NH2
-
IC50: 14 mM
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
-
IC50: 4.4 mM
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.54 mM
succinyl-Ala-Pro-Phe-4-aminoanilide
-
IC50: 5.8 mM
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
-
IC50: 0.7 mM
succinyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.17 mM
succinyl-Pro-Phe-4-nitroanilide
-
IC50: 1.09 mM
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[3-[(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)carbonyl]-2-methyl-1-benzofuran-5-yl]acetonitrile
-
-
5-hydroxy-1,4-naphthoquinone
-
i.e. juglone, 0.0057 mM, complete inhibition of wild-type and mutant C69A within 30 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity
5-hydroxy-1,4-naphthoquinone
-
i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity
5-hydroxy-1,4-naphthoquinone
-
i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity
Ala-Pro
-
-
ATP
-
at least 3fold stimulation, excess of ATP over Mg2+ is inhibitory
ATP
-
at least 3fold stimulation, excess of ATP over Mg2+ is inhibitory
Cu2+
-
cyclosporin A
-
cyclosporin A
-
IC50: 16 nM
cyclosporin A
IC50: 50 nM
cyclosporin A
-
no inhibition
cyclosporin A
-
the combination of cyclosporin A or its analogues with other drugs, such as nucleotide analogues, e.g. 3'-azido-3'-deoxy-thymidine, or 2',3'-dideoxycytidine, HIV-1-protease inhibitors, and antibiotics, might provide long-term benefit to HIV-1-infected individuals
cyclosporin A
-
the sequence MeLeu9-trans-MeLeu10-MeVal is responsible for the efficient binding in the active site of cyclophilin. The cis-conformer is inactive as inhibitor
cyclosporin A
-
and analogs
cyclosporin A
-
forms an inhibitory complex with cyclophilin. CyPA is a major intracellular target of cyclosporines
cyclosporin A
no inhibition by cyclosporins
cyclosporin A
and cyclosporin derivative with modifications in the D-Ser side chain. Inhibition leads to failure of polymerization of the extracellular multi-domain protein hensin, plus the loss of the apical cytoskeleton, apical microvilli, and the columnar epithelial shape of clone C cells
cyclosporin A
-
inhibits the activity largely localized to the mitochondrial matrix
cyclosporin A
-
and analogs
cyclosporin A
almost complete inhibition
cyclosporin A
-
inhibits cytosolic and microsomal enzyme form
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
-
-
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
-
-
diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
-
-
diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
-
-
dipentamethylene thiuram monosulfide
-
-
dipentamethylene thiuram monosulfide
-
-
FK506
-
FK506
0.0005 mM, almost complete inhibition
FK506
-
only one of the 4 domains can be inhibited by the immunosuppressive drug
FK506
-
50% inhibition at 0.00032 mM
FK506
an immunosuppressive drug
FK506
-
binds at the catalytic domain
GPI-1046
-
juglone
-
Pin1 inhibition leads to relocalization of endogenous c-Rel to the cytoplasm coincident with lymphoma cell death and/or growth inhibition
juglone
-
i.e. 5-hydroxy-1,4-naphthalenedione, from leaves, roots, and bark of plants of family Juglandaceae. The compound causes a partial unfolding of the PPIase active site
juglone
-
i.e. 5-hydroxy-1,4-naphthoquinone, selective and irreversible inhibition. Juglone reduces PPIase activity but does not alter Pin1 expression
juglone
-
i.e. 5-hydroxy-1,4-naphthoquinone, natural inhibitor of Pin1
juglone
pharmacological inhibitor of isoform Pin1, application of juglone partially prevents dephosphorylation of phosphoptotein Tau at Thr231
juglone
-
i.e. 5-hydroxy-1,4-naphthalenedione, from leaves, roots, and bark of plants of family Juglandaceae. The compound causes a partial unfolding of the PPIase active site
Rapamycin
-
50% inhibition at 5 nM
Rapamycin
-
inhibits the activity associated with the mitochondrial membranes
Rapamycin
-
50% inhibition at 0.00048 mM
Rapamycin
an immunosuppressive drug
Rapamycin
-
binds at the catalytic domain
additional information
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
-
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
not inhibitory: FK506
-
additional information
-
not inhibitory: FK506
-
additional information
-
the OBOC peptide library screening for and selection of selected inhibitors containing a consensus motif of D-pThr-L-piperidine-2-carboxylic acid-L-2-naphthylalanine using inactive enzyme mutant S16A/Y23A, interaction analysis by Isothermal titration calorimetry, overview. A second generation of cell permeable Pin1 inhibitors, that have have antiproliferative activity against the cancer cells, is designed by replacing the noncritical residues within the cyclic peptide ring with arginine residues. Effects of inhibitor peptides in vivo on cancer cells, e.g. HeLa cells, overview
-
additional information
-
inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis
-
additional information
-
no inhibition by 3-[(2,5-dimethyl-1-benzofuran-3-yl)carbonyl]-4-hydroxybenzonitrile
-
additional information
food polyphenols carrying a galloyl group show significant inhibition
-
additional information
-
no inhibition by cyclosporine, even at 0.01 mM
-
additional information
no inhibition by cyclosporine, even at 0.01 mM
-
additional information
-
Pin1 inhibitors may be used as a novel type of anticancer drug that acts by blocking cell cycle progression
-
additional information
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
-
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
-
cyclosporin A is not inhibitory up to 0.005 mM
-
additional information
-
inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis
-
additional information
not inhibitory: FK506
-
additional information
-
not inhibitory: FK506
-
additional information
no inhibition by FK506
-
additional information
-
no inhibition by FK506
-
additional information
-
no inhibition: chlorotosylamidophenylbutane, diisopropylphosphorofluoridate
-
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0.00222
(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.00001
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
0.01
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.007
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.004 - 0.01
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000005
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.002 - 0.006
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.01
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.02
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.000005
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00016
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.000007
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0002
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
0.001
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
pH and temperature not specified in the publication
0.0074
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
pH and temperature not specified in the publication
0.0041
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
pH and temperature not specified in the publication
0.0072
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
pH and temperature not specified in the publication
0.00366
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.0001
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
0.000001
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
0.0021
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0037
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
pH and temperature not specified in the publication
0.0018
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0006
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0029
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0026
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0086
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
0°C, pH 8.0
0.00005
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0167
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
0.0092
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.0079
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.000084
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.055
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000059
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0083
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
pH 8.0
0.03
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
0.0012
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.0081
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.000012
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.012
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00023
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.00006
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.0023
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
0.00009
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.000019
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0000559
5-hydroxy-1,4-naphthoquinone
-
mutant enzyme C69A
0.258
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0012
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.183
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0048
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0183
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.547
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.00005
alpha-lactalbumin
-
unfolded alpha-lactalbumin
-
0.000068
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0000028
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.000081
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0002 - 0.00052
cyclic CRYPEVEIC
0.0000039 - 0.0000188
cyclosporin A
0.00066
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0043
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.008
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
0.004
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.044
linear CRYPEVEIC
-
using succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C
0.009
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.026
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.016
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.015
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.044
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.032
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.0002
cyclic CRYPEVEIC
-
using Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C
0.00052
cyclic CRYPEVEIC
-
using succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C
0.0000039
cyclosporin A
-
-
0.0000188
cyclosporin A
pH 8.0, 15°C
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evolution
ROF2 encodes a peptidyl-prolyl cis-trans isomerase of the FK506-binding protein class
evolution
-
the enzyme belongs to the FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases, PPIases, which share a canonical domain fold consisting of a beta-sheet composed of four large and two small -strands, opposed by a single main alpha-helix
evolution
the enzyme belongs to the FK506-binding protein (FKBP) family whose members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum. Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. All FKBP-EFs contain an endoplasmic reticulum retention signal at the C-terminus
evolution
the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
evolution
-
the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
-
malfunction
-
Pin1 blockade leads to Bax cleavage, mitochondrial translocation and caspase 9 and 3 activation, irrespective of the presence of cytokines, and Pin1 blockade accelerates eosinophil apoptosis
malfunction
-
Pin1 is deregulated in many tumors
malfunction
-
Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
malfunction
-
Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
malfunction
-
Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
malfunction
-
knockdown of FKBP1B induces eye formation malfunction
malfunction
-
knockdown of Pin1 does not prevent CK2alpha phosphorylation
malfunction
-
Pin1 depletion is linked to a dysfunction of uncoating of human immunodeficiency virus type 1
malfunction
-
Pin1 knock-out mice exhibit impaired insulin signaling with glucose intolerance. Pin1 knock-out mice are resistant to diet-induced obesity
malfunction
-
silencing of Pin1 expression results in decrease of hepatitis C virus replication in both hepatitis C virus replicon cells and cell culture grown hepatitis C virus-infected cells
malfunction
a DELTAef0685/DELTAef1534 mutant is more resistant to oxidative stress, is able to grow under a high manganese concentration, and shows altered resistance to ampicillin and quinolone antibiotics
malfunction
loss of function of ROF2, and especially double mutation of ROF2 and the closely related gene ROF1, results in acid sensitivity, stress and development phenotypes of ROF mutants, overview
malfunction
-
Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
-
physiological function
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24. The Ser/Thr-Pro motifs are important for Pin1At function in promoting flowering through AGL24 and SOC1. Phosphorylation-dependent prolyl cis/trans isomerization of key transcription factors is an important flowering regulatory mechanism, overview
physiological function
-
Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
physiological function
-
cyclophilin A is an essential cofactor for hepatitis C virus infection and the intracellular target of cyclosporines anti-HCV effect, mechanism by which CyPA facilitates HCV replication, overview
physiological function
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
-
peptidyl-prolyl isomerase, Pin1, is a critical regulator of NF-kappaB activation facilitating NF-kappaB binding in hepatocytes and protects against hepatic ischemia/reperfusion injury. Pin1 is required for full production of MIP-2, but not for production of TNFalpha
physiological function
peptidylprolyl isomerases play essential roles in protein folding and are implicated in immune response and cell cycle control. Bombyx mori PPIases may be involved in anti-Bombyx mori nucleopolyhedrovirus response, mechanism, overview
physiological function
-
Pin1 is a key mediator of pro-survival signaling and a regulator of the pro-apoptotic Bcl-2-associated X protein, Bax, function. Pin1 likely functions as a downstream effector of GM-CSF and IL-5 signaling, and regulates cell death through the intrinsic, mitochondria- and caspase 9-dependent, apoptotic pathway, overview
physiological function
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibility to cancer and neurogenerative diseases, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 mediates the neural-specific apoptosis machinery. Pin1 is involved in regulation of SMRT levels. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 is involved in regulation of SMRT levels. Pin1 mediates the neural-specific apoptosis machinery. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
-
Pin1 is critical for the regulation of serine/threonine protein kinase B, PKB/Akt, stability and activation phosphorylation at S473 through the phosphorylated Thr-Pro motifs of Akt. Roles of Akt and Pin1 in oncogenesis, overview
physiological function
-
Pin1 markedly enhances transformation in primary lymphocytes by the c-Rel protein and by viral Rel/NF-kappaB oncoprotein v-Rel, it enhances the nuclear translocation of the Rel proteins, overview
physiological function
-
Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
-
Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
-
Pin1 regulates the function and/or stability of phosphoproteins by altering the conformation of specific pSer/pThr-Pro peptide bonds
physiological function
-
SurA may function to repair, or prevent damage to, the outer membrane upon exposure to PmB and may consequently limit damage to the inner-membrane
physiological function
-
the Pin1 is located in the midbody ring in HeLa cells and regulates cell cycle progression and cytokinesis through centrosome protein Cep55, which is an essential component of the midbody ring
physiological function
-
colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
physiological function
Par45 is a phosphorylation-independent parvulin required for normal cell proliferation in a unicellular eukaryotic cell
physiological function
-
peptidyl-prolyl isomerase Pin1 is required for CK2alpha mitotic spindle localization. Pin1 protects CK2alpha from dephosphorylation in vivo
physiological function
-
peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
physiological function
-
Pin1 is a host factor for hepatitis C virus propagation and may contribute to hepatitis C virus-induced liver pathogenesis. Both binding and isomerase activities of Pin1 are essential for hepatitis C virus replication
physiological function
-
Pin1 plays a critical role in adipose differentiation. Pin1 binds to IRS-1 and thereby markedly enhances insulin action, essential for adipogenesis
physiological function
-
Pin1 plays a critical role in adipose differentiation. Pin1 binds to IRS-1 and thereby markedly enhances insulin action, essential for adipogenesis
physiological function
-
Pin1 prolyl isomerase activity is required for the disassembly of the human immunodeficiency virus type 1 core
physiological function
-
PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
physiological function
-
Xenopus peptidyl-prolyl cis-trans isomerase FKBP1B induces ectopic secondary axis and is involved in eye formation during Xenopus embryogenesis
physiological function
-
Fpr4 has been described as a histone chaperone, and is implicated in epigenetic function in part due to its mediation of cis-trans conversion of proline residues within histone tails
physiological function
peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis. As ROF2 induction and intracellular acidification are common consequences of many stresses, this mechanism of pH homeostasis may be of general importance for stress tolerance. Chaperone ROF2 not only helps to refold proteins but also activates H+ extrusion to restore intracellular pH
physiological function
-
peptidyl-prolyl isomerase activity of FKBP12 is essential for prevention of aggregation of tau, an Alzheimer's disease-related protein. Tau aggregates into neurofibrillary tangles when it is hyperphosphorylated, only the cis-isomer can aggregate. FKBP12 catalyzes isomerization of the tau R3 peptide peptide in both the monomeric and aggregative states, once the cis-isomer is converted into the trans-isomer in the aggregative state, the trans-isomer is quickly released from the aggregation because the trans-isomer cannot aggregate, inhibitory mechanism of R3 peptide aggregation by simple binding of FKBP12, overview. IC50 of FKBP12 is 0.003 mM. The aggregation inhibitory activity of FKBP12 is independent of the affinity between FKBP12 and the R3 peptide. Therefore, the aggregation inhibitory activity of FKBP12 depends only on the PPIase activity of FKBP12
physiological function
peptidylprolyl cis/trans isomerases are enzymes involved in protein folding. The parvulin family rotamase EF0685 and the cyclophilin family member EF1534 are important for virulence and resistance to NaCl, while EF2898 is not important for the Enterococcus faecalis stress response or virulence
physiological function
-
CYPJ promotes the transition of cells from G1 phase to S phase by activating cyclin D1 promoter. CYPJ overexpression accelerates liver cell growth in vitro and in vivo. Inhibition of CYPJ by cyclosporin A or CYPJ-specific RNAi diminishes the growth of liver cancer cells in vitro and in vivo
physiological function
deletion of PrsA leads to a decrease in secreted protease and phospholipase activity. Deletion does not alter the growth characteristics of Staphylococcus aureus
physiological function
disruption of ppiB does not alter the growth characteristics of the strains but results in decreased activity of secreted virulence factor nuclease Nuc in culture supernatants, probably resulting from misfolding of Nuc in the absence of PpiB. Ppib directly interacts with Nuc in vitro
physiological function
-
enzyme displays chaperone activity in a citrate synthase thermal aggregation activity assay
physiological function
enzyme interacts with calmodulin in vivo and in vitro. In vitro interaction is Ca2+-dependent, and the calmodulin-binding domain is localized to 35-70 amino acid residues in the N-terminus
physiological function
enzyme regulates lysyl hydroxylase LH2-mediated collagen cross-linking. FKBP65 deficiency diminishes hydroxylysine-aldehyde derived intermolecular collagen cross-links and increases the non-hydroxylated lysine-aldehyde-derived collagen cross-links
physiological function
expression of a wheat cyclophilin CypA-1 confers thermotolerance to Escherichia coli. Expression of deletion mutants that lack peptidyl-prolyl cis-trans isomerase activity, results in abrogation of thermotolerance. CypA-1 interacts with calmodulin, and the Calmodulin-binding domain is localized to amino acid residues 51-71 in the N-terminal region
physiological function
FkpA delays the aggregation of citrate synthase in vitro and has a positive effect on the activity and temperature range of citrate synthase in vitro. Deletion of FkpA causes a 50% reduced biomass yield compared to that of the wild type when grown at 37°C, whereas there is only a 10% reduced biomass yield at the optimal growth temperature of 30°C accompanied by accumulation of 7 mM L-glutamate and 22 mM 2-oxoglutarate
physiological function
HepG2 cells treated with recombinant isomerase protein exhibit a reduction in the formation of hydrogen peroxide-mediated reactive oxygen species. Treatment diminishes H2O2-mediated oxidative stress and restores both the expression and the activity of antioxidant enzymes, including superoxide dismutase, catalase, glutathione peroxidase and thioredoxin reductase. Superoxide dismutase, catalase and thioredoxin reductase activixadties are upregulated by treatment with the purified protein
physiological function
In response to genotoxic drug doxorubicin, Pin1 binds and decreases levels of the phosphorylated Foxo3, the positive transcription factor of P-glycoprotein (P-gp) gene. Thereby, Pin1 decreases the level of P-gp and signals the cell to pump the genotoxic drugs out
physiological function
loss of PinA leads to decreased growth rate, reduced spore formation and abnormal prespore-prestalk patterning. Expression of PinA complements the temperature sensitivity phenotype associated with a mutation in ESS1 in Saccharomyces cerevisiae
physiological function
mice lacking the Pin1 gene form more megakaryocytes than wild type mice, and the proplatelet formation of megakaryocytes is poorer in Pin1-/- mice than in wild-type mice. Treatment of megakaryoblastic floating cell line Meg-01 with shRNA against Pin1 suppresses the proplatelet formation. Expression of tau, a microtubule associated protein is induced in megakaryocytes during proplatelet formation. Pin1 binds tau and promotes microtubule polymerization
physiological function
overexpression lengthens the locomotor behavioral period. Dod associates preferentially with phosphorylated species of PERIOD, associated with the circadian clock machinery, which delays the phosphorylation-dependent degradation of PERIOD. PERIOD protein levels are higher in flies overexpressing Dod
physiological function
PIN1 directly interacts with hypoxia-inducible factor HIF-1alpha in human colon cancer cells. PIN1 binding occurs in a phosphorylation-dependent manner, and at both exogenous and endogenous levels. Binding stabilizes the HIF-1alpha protein, resulting in increased transcriptional activity, and upregulating expression of vascular endothelial growth factor. Silencing of PIN1 or pharmacologic inhibition of its activity abrogates the angiogenesis
physiological function
PIN1 inhibition dramatically reduces the tumor volume in a subcutaneous mouse xenograft model and angiogenesis as well as hypoxia-induced transcriptional activity of hypoxia-inducible factor HIF-1alpha
physiological function
Pin1 interacts with hypoxia-inducible transcription factor HIF-1alpha. The interaction is regulated through p42/p44 MAPK pathway activation, and Pin1 catalytic activity generates a conformational change in HIF-1alpha. Pin1 is required for gene-specific HIF-1 transcriptional activity
physiological function
Pin1 interacts with the cytoplasmic domain of tissue factor. Pin1 is able to bind wild-type and mutant forms of overexpressed tissue factor-tGFP fusion proteins. Pin1 coimmunoprecipitates with overexpressed wild-type tissue factor-tGFP but not Ser258Ala or Pro259Ala substituted mutants. Pin1 is capable of interfering with the ubiquitination and dephosphorylation of tissue factor-derived peptides
physiological function
recombinant expression in Escherichia coli increases its temperature and salinity tolerance´
physiological function
-
PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
-
physiological function
-
enzyme displays chaperone activity in a citrate synthase thermal aggregation activity assay
-
physiological function
-
FkpA delays the aggregation of citrate synthase in vitro and has a positive effect on the activity and temperature range of citrate synthase in vitro. Deletion of FkpA causes a 50% reduced biomass yield compared to that of the wild type when grown at 37°C, whereas there is only a 10% reduced biomass yield at the optimal growth temperature of 30°C accompanied by accumulation of 7 mM L-glutamate and 22 mM 2-oxoglutarate
-
physiological function
-
deletion of PrsA leads to a decrease in secreted protease and phospholipase activity. Deletion does not alter the growth characteristics of Staphylococcus aureus
-
physiological function
-
disruption of ppiB does not alter the growth characteristics of the strains but results in decreased activity of secreted virulence factor nuclease Nuc in culture supernatants, probably resulting from misfolding of Nuc in the absence of PpiB. Ppib directly interacts with Nuc in vitro
-
physiological function
-
peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
-
physiological function
-
Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
-
physiological function
-
colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
-
additional information
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SurA and FkpA are not involved in the starvation-stress response, SSR. Genes surA and fkpA appear to be dispensable for the cross-resistance of carbon-starved cells to oxidative stress
additional information
active site Cys113
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
-
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
-
length of helix alpha3 contributes significantly to the preservation of the structure, function, and stability of Escherichia coli FKBP22. Homology modeling of the three-dimensional enzyme structure, overview
additional information
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
-
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
-
the canonical FKBP catalytic domain actively increases the rate of isomerization of three decapeptides derived from the N-terminus of yeast histone H3, whereas maintaining intrinsic cis and trans populations. A notable feature of the FKBP catalytic domain is a prominent hydrophobic pocket that is thought to bind the proline. Specifically, Trp345 lies at the bottom of the hydrophobic pocket, with the additional residues Tyr313, Phe323, Phe332, Phe334, Val341, Ile342, Tyr368, and Phe384 forming the sides of the proline-binding cavity. The final residue, Asp324, provides a contrast to the largely hydrophic nature of the cavity. Asp324 along with the less-conserved Glu340 together comprise a small acidic region at the side of the hydrophobic pocket in Fpr4 that is otherwise surrounded by a large surface region enriched in positively charged amino acids
additional information
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
-
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview
additional information
-
Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview
additional information
-
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
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C129S
presence of dithiothreitol, 49% of wild-type activity, presence of H2O2, 84% of wild-type activity
C171S
presence of dithiothreitol, 25% of wild-type activity, presence of H2O2, 87% of wild-type activity
C176S
presence of dithiothreitol, 94% of wild-type activity, presence of H2O2, 231% of wild-type activity
C54S
presence of dithiothreitol, 40% of wild-type activity, presence of H2O2, 123% of wild-type activity
A82P
mutation in hinge region, 41% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
C69A
-
about one equivalent of 5-hydroxy-1,4-naphthoquinone results in complete inactivation of the mutant enzyme compared to two equivalent for the wild-type enzyme
E178V
-
slightly more active than wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, as active as wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F198A
-
inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, inactive in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F233L
-
inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
G148D
-
the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme)
I42S
-
about 50% of wild-type peptidylprolyl isomerase activity, cells show moderate deficiency in nickel uptake under anaerobic conditions
I42S/F132Y
-
almost complete loss of peptidylprolyl isomerase activity, retains most of hydrogenase activity and cells show moderate deficiency in nickel uptake under anaerobic conditions
I65P
mutation in hinge region, 6% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
V72P
mutation in hinge region, 60% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea
Y15A
residue Tyr 15 is indispensable for dimerization ability, catalytic activity, and structure but contributes little to its inhibitor binding ability and stability
Y221F
-
mutant enzyme shows 15% of the activity of the wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide as substrate, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
G148D
-
the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme)
-
C138A
site-directed mutagenesis, the mutant shows 93% of wild-type activity
C41A
site-directed mutagenesis, the mutant shows 104% of wild-type activity
C51A
site-directed mutagenesis, the mutant shows 93% of wild-type activity
C90A
site-directed mutagenesis, the mutant shows 35% of wild-type activity
F111A
site-directed mutagenesis, the mutant shows 30% of wild-type activity
F111Y
site-directed mutagenesis, the mutant shows 20% of wild-type activity
H131A
site-directed mutagenesis, the mutant shows 19% of wild-type activity
H134A
site-directed mutagenesis, the mutant shows 30% of wild-type activity
H48A
site-directed mutagenesis, the mutant shows 7.8% of wild-type activity
M107A
site-directed mutagenesis, the mutant shows 73% of wild-type activity
T130A
site-directed mutagenesis, the mutant shows 68% of wild-type activity
C138A
-
site-directed mutagenesis, the mutant shows 93% of wild-type activity
-
C51A
-
site-directed mutagenesis, the mutant shows 93% of wild-type activity
-
H131A
-
site-directed mutagenesis, the mutant shows 19% of wild-type activity
-
H134A
-
site-directed mutagenesis, the mutant shows 30% of wild-type activity
-
H48A
-
site-directed mutagenesis, the mutant shows 7.8% of wild-type activity
-
A16S
-
site-directed mutagenesis, dominant-negative Pin1 point mutation
C113D
mutation does not compromise isoform Pin1 function in vivo nor does it abolish catalytic activity. C113 may not be the catalytic nucleophile
C115A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C161A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C52A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C62A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
D155R
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
D158R
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
DELTA208-213
-
dramatic reduction of peptidylprolyl isomerase activity and 400fold reduction of protein phosphatase 2A activation
F133A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
F60A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
G77H
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
H126Q
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H157A
-
mutant supports viability in yeast complementation assay
H157F
-
mutant supports viability in yeast complementation assay
H157L
-
mutant supports viability in yeast complementation assay
H157N
-
mutant supports viability in yeast complementation assay
H157S
-
mutant supports viability in yeast complementation assay
H47Q
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H59A
-
mutant supports viability in yeast complementation assay
H59F
-
mutant supports viability in yeast complementation assay but displays significantly reduced growth in yeast compared to wild-type Pin1
H59L
-
mutant is not viable
H59L/H157A
-
about 50% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157F
-
about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, 3% activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157L
-
mutant supports viability in yeast complementation assay, mutation H157L rescues mutant H59L
H59L/H157S
-
about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59N
-
mutant supports viability in yeast complementation assay
H59S
-
mutant supports viability in yeast complementation assay
K120A
-
87% of wild-type activity
P16S
-
10fold decrease in ratio kcat/Km at 10°C. Mutant is extremely sensitive to guanidinium-HCl and shows increased susceptibility to urea. Folding time of the mutant is extended
P9Q/R13F/K17V/R18F
-
mutant designed for crytallizability, crystal structure in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
Q111A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
R44A
-
57% of wild-type activity
R44A/F49A
-
32% of wild-type activity
R55A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
R68/69A
-
catalytically inactive
R68A/R69A
decrease in both kcat and Km value
S16A/Y23A
-
the mutations of Pin1 protein do not affect the structure of Pin1 but abolishes the ability of the WW domain to bind pSer/pThr-Pro ligands
S16E
-
mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
S19A
-
mutation abolishes phosphorylation and alters the subcellular localization from predominantly nuclear to significantly cytoplasmic
S19E
-
mutant enzyme is localized around the nuclear envelope, but does not penetrate into the nucleoplasm, in vitro DNA-binding affinity is strongly reduced
V55R
-
site-directed mutagenesis, the mutation increases the PPIase activity by a factor of 11
W121A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
W34A/K63A
-
catalytically inactive
Y82K
-
site-directed mutagenesis, the mutation decreases the PPIase activity by a factor of 7
R68/69A
mutant has lost the binding site to the phosphorylated Ser/Thre-Pro residues of substrates, still is able to decrease the transcriptional activity of FOXO3
W34A
mutant lacks the WW motif of the FOXO3 binding site, is not able to decrease the transcriptional activity of FOXO3
DELTA208-213
-
almost no enzymic activity, 400fold less activity in the activation reaction of PP2A phosphatase
Y100A
site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme
Y100E
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Y100F
site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme
Y100L
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Y100P
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
Y100R
site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme
Y100W
site-directed mutagenesis, the mutant shows about 30% reduced activity compared to the wild-type enzyme
R62A
-
overexpression of wild-type isoform CypB attenuates endoplasmic reticulum stress-induced cell death, whereas overexpression of isomerase activity-defective mutant R62A increases Ca2+ leakage from the endoplasmic reticulum and generation of reactive oxygen species and decreases mitochondrial membrane potential resulting in cell death
S16A
-
a dominant negative mutant
A78G
52% of wild-type activity
D23A
78% of wild-type activity
F128A
35% of wild-type activity
H119A
84% of wild-type activity
I37G
50% of wild-type activity
M96A
39% of wild-type activity
N35A
71% of wild-type activity
Q94A
98% of wild-type activity
Y13F
92% of wild-type activity
Y63A
21% of wild-type activity
Y63F
76% of wild-type activity
Y92A
36% of wild-type activity
D23A
-
78% of wild-type activity
-
H119A
-
84% of wild-type activity
-
N35A
-
71% of wild-type activity
-
Y92A
-
36% of wild-type activity
-
C113A
-
mutation in isomerase domain, catalytically inert. Mutation diminishes binding to brain-specifc protein BNIP-H
C113A
-
isomerase-inactive
C113S
-
catalytically inactive
C113S
decrease in kcat, small in Km value. C113 may not be the catalytic nucleophile
K63A
decrease in kcat, increase in Km value
K63A
-
mutant lacking isomerase activity. Wild-type inhibits FOXO4-induced expression of p27kip1, while mutant K63A does not
S16A
-
mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
S16A
-
a dominant negative mutant
S16A
-
isomerase-inactive
W34A
-
cells expressing Pin1 mutant W34A do not inhibit FOXO4 relocalization to the nucleus upon stimulation with hydrogen peroxide
W34A
-
mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
D205G
-
essential for petidyl-prolyl cis/trans isomerase activity and activation of PP2A phosphatase
D205G
-
D205 is required for both peptidylprolyl isomerase activity and protein phosphatase 2A activation
additional information
construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
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construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
additional information
-
overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
additional information
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construction of a cj0596 deletion mutant derivative of strain 81-176, isolation of a revertant of this mutant by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrates a slightly decreased growth rate and lower final growth yield, yet it is more motile and more invasive of human intestinal epithelial cells than wild-type, phenotype, overview
additional information
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construction of a cj0596 deletion mutant derivative of strain 81-176, isolation of a revertant of this mutant by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrates a slightly decreased growth rate and lower final growth yield, yet it is more motile and more invasive of human intestinal epithelial cells than wild-type, phenotype, overview
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generation of genes ef2898, ef0685, and ef1534 deletion mutants
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generation of genes ef2898, ef0685, and ef1534 deletion mutants
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generation of genes ef2898, ef0685, and ef1534 deletion mutants
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generation of genes ef2898, ef0685, and ef1534 deletion mutants
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the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
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the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
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genetic inactivation of isoforms FkpA, PpiA, PpiD, SurA results in a viable strain with decreased growth rate and increased susceptibility to certain antibodies. Expression of P and type 1 pili is severely diminished in the quadruple mutant as well as in absence of SurA alone
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the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C)
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construction of FKBP22 four helix alpha3 mutant variants by various in vitro probes, rFKBP22D5 and rFKBP22D30 are deletion mutants, while rFKBP22I3 and rFKBP22I6 are insertion mutants. The molecular dimensions, dimerization efficiencies, secondary structures, tertiary structures, stabilities, and protein folding abilities of all mutant proteins differ from those of wild-type rFKBP22, but the rapamycin binding affinities of the mutant proteins are affected very little
additional information
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the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C)
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silencing of isoform cyclophilin A by RNAi leads to a significant reduction in the body weight of engorged ticks and their failure to lay eggs
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silencing of isoform cyclophilin A by RNAi leads to a significant reduction in the body weight of engorged ticks and their failure to lay eggs
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silencing of isoform cyclophilin B by RNAi does not lead to detectable phenotypic changes
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silencing of isoform cyclophilin B by RNAi does not lead to detectable phenotypic changes
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depletion of enzyme by siRNA reduces hormone-dependent transcription from both transfected reporters and an endogenous steroid receptor target gene. Depletion of enzyme in MCF-7 cells reduces the endogenous estrogen-dependent recruitment of p300 to the promoters of estrogen receptor-dependent genes. Enzyme overexpression enhances SRC-3 cellular turnover
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analysis of residues conserved in natural Pin1 sequences and during unigenic evolution and screen for completely conserved residues in functional Pin1 mutants by complementation of Ess1 mutant in Saccharomyces cerevisiae
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analysis of residues conserved in natural Pin1 sequences and during unigenic evolution and screen for completely conserved residues in functional Pin1 mutants by complementation of Ess1 mutant in Saccharomyces cerevisiae
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both hydrogen peroxide and heat stresses induce phosphorylation of neurofilament protein NF-H in transfected HEK-293 cells and primary cortical cultures. Knockdown of Pin1 by transfected Pin1 short interference RNA and dominant negative-Pin1 rescues the effect of stress-induced NF-H phosphorylation
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co-expression of cyclophilin B with TRPV6 channel protein in Xenopus laevis oocytes results in significant increase in TRPV6-mediated calcium uptake. Effect is reversed by addition of cyclosporin A
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Pin1 overexpression increases the reporter activities in cells transfected with reporters containing the vascular endothelial growth factor VEGF gene promoter or with minimal reporters of activator protein-1 and hypoxia response element. VEGF reporter gene activity is significantly inhibited by either hypoxia-inducible factor-alpha siRNA or AP-1 decoy ODN. Pin1 stimulates VEGF expression by activating HIF-1alpha and AP-1, and is a potential therapeutic target of angiogenesis during cancer development
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a WW domain mutant of Pin1 can no longer interact with NF-kappaB
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depletion of Pin1 from HeLa cells causes a cytokinesis defect, overview
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introduction of point mutations in the prolyl-peptidyl isomerase motif of CyPA. Downregulation of host CyPA by RNA interference, and mutations in viral NS5B, that confers cyclosporine-resistant binding to CyPA, contribute to the cyclosporine resistance of the replicons harboring these mutations
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overexpression of Pin1 reduces wild-type tau stability but increases P301L mutant tau stability
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Par14 knockout leads to suppression of cell growth, phenotype, overview
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repression of Pin1 expression through either homologue Pin1 knockout or small interfering RNA-mediated knockdown compromises its ability to protect Akt from degradation
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mutation of active site residues of Pin1 results in weakened, but not total, abrogation of activity
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enzyme defective mutant lacks 40-70% of secreted p-nitrophenol phosphorylcholine hydrolase activity. C-terminus of Mip is required for activation/secretion of p-nitrophenol phosphorylcholine hydrolase
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mutants lacking PpiB activity exhibit reduced growth at 17°C
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Pin1 knockout mice show reduced neutrophile accumulation in the liver, reduced NF-kappaB activation, and increased nuclear p65 protein expression compared to wild-type mice, phenotypes, overview
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enzyme deletion mutant, enzyme is not required in log phase of growth. Mutation does not affect the binding of strain to macrophages but decreases intracellular survival in macrophages
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enzyme overexpression renders isolated mitochondria far more susceptible to the permeability transition induced by Ca2+ and oxidative stress. Overexpressing cells maintain a lower inner-membrane potential of mitochondria than those of normal cells. Effects are abolished by cyclosporin A. Cyclosporin-D overexpression promotes NO-induced necrosis and inhibits staurosporine-induced apoptosis
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in isoform Pin1-deficient neuronal cell cultures, H2O2 stress-induced phosphoprotein Tau dephosphorylation at Thr231 is significantly lower than in wild-type neurons
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overexpression of wild-type isoform CypB attenuates endoplasmic reticulum stress-induced cell death, whereas overexpression of isomerase activity-defective mutant R62A increases Ca2+ leakage from the endoplasmic reticulum and generation of reactive oxygen species and decreases mitochondrial membrane potential resulting in cell death. siRNA-mediated inhibition of CypB expression renders cells more vulnerable to endoplasmic reticulum stress. CypB interacts with the endoplasmic reticulum stress-related chaperones, Bip and Grp94
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overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation
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overexpression of Pin1 reduces wild-type tau stability but increases P301L mutant tau stability
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silencing of Pin1 by siRNA, Pin1 siRNA-transfected neurons show the reduction in perikaryal phosphorylation of NF, siRNA inhibits okadaic acid-induced perikaryal phosphorylation of NF-M/H, immunohistochemic analysis, overview
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disruption of the fkpA gene results in a 47.9fold and 32.1fold decrease in thermotolerance in 5-h and 24-h CS cells, respectively, compared to the parental strain
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enzyme knockout mutant, in mouse pneumonia model no significant difference to wild-type. Deficiency in enzyme does not reduce binding activity of strain to host target proteins but results in enhanced uptake by professional phagocytes
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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enzyme is able to replace the essential homolog Ess1 in Saccharomyces cerevisiae
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enzyme is able to replace the essential homolog Ess1 in Saccharomyces cerevisiae
additional information
overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation
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