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1-aminocyclopropane-1-carboxylic acid synthase 6 + H2O
?
-
phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase 6 introduces negative charges to the C-terminus of ACS6, which reduces the turnover of 1-aminocyclopropane-1-carboxylic acid synthase 6 by the 26S proteasome degradation machinery
-
-
?
4-hydroxy-3-nitrophenol-Leu-Leu-Asn-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
4-hydroxy-3-nitrophenyl-Leu-Leu-Lys-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
AAF-7-amido-4-methylcoumarin + H2O
?
-
highest activity in testicle, kidney and brain
-
?
ABZ-Val-Val-Ser-Arg-Ser-Leu-Gly-Tyr(3-NO2)-NH2 + H2O
?
-
synthetic, internally quenched substrate
-
-
?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
acetyl-Arg-hSer-Thr-Arg-7-amido-4-methylcoumarin + H2O
acetyl-Arg-hSer-Thr-Arg + 7-amino-4-methylcoumarin
-
substrate for trypsin-like activity
-
-
?
acetyl-betaAla-Met(sulfone)-Thr-Arg-7-amido-4-methylcoumarin + H2O
acetyl-betaAla-Met(sulfone)-Thr-Arg + 7-amino-4-methylcoumarin
-
substrate for trypsin-like activity
-
-
?
acetyl-DPSD-7-amido-4-methylcoumarin + H2O
?
-
cleaved by the beta1 subunit of the 20S proteasome
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
acetyl-hArg-Pro-2-fluoro-Phe-Asp-7-amido-4-methylcoumarin + H2O
acetyl-hArg-Pro-2-fluoro-Phe-Asp + 7-amino-4-methylcoumarin
-
substrate for caspase-like activity
-
-
?
acetyl-hArg-Pro-Abu-Asp-7-amido-4-methylcoumarin + H2O
acetyl-hArg-Pro-Abu-Asp + 7-amino-4-methylcoumarin
-
substrate for caspase-like activity
-
-
?
acetyl-HHSL-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
acetyl-Phe-Thr(Bzl)-His(3-benzyloxymethyl)-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Phe-Thr(Bzl)-His(3-benzyloxymethyl)-Leu + 7-amino-4-methylcoumarin
-
substrate for chymotrypsin-like activity
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-VGR-4-methyl-7-amido-coumarin + H2O
benzoyl-VGR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity
-
-
?
benzoyl-VGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-D-Ala-Leu-Arg-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-dALR-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-GAPLG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GGF-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GGF-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GGL-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-GGL-4-nitroanilide + H2O
?
-
chymotrypsin-like activity
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGR-2-naphthylamide + H2O
?
-
trypsin-like activity
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Gly-Gly-Arg-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
benzyloxycarbonyl-Gly-Pro-Ala-Gly-Gly-p-aminobenzoate + aminopeptidase-N + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala-Leu-Ala-p-aminobenzoate + aminopeptidase-N + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPAFG-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPAFG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GPAGG-4-aminobenzoate + H2O
?
-
highest activity in soleus and brain
-
?
benzyloxycarbonyl-GPAGG-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
benzyloxycarbonyl-GPALG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-LAF-4-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
?
-
11% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin + H2O
?
-
36% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
benzyloxycarbonyl-LLE-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-beta-naphthylamide + H2O
?
-
caspase-like activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
Boc-Leu-Leu-Glu-4-methylcoumarin-7-amide + H2O
Boc-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bz-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Bz-DL-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Bz-VGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
DBC2 protein + H2O
?
-
-
-
-
?
dihydrofolate reductase + H2O
?
ERM transcription factor + H2O
?
-
-
-
-
?
erythroid Krueppel-like factor + H2O
?
-
-
-
-
?
fructose-1,6-bisphosphatase + H2O
?
-
-
-
-
?
Glu-Gly-Gly-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
H-VLK-7-amido-4-methylcoumarin + H2O
?
-
very-low activity
-
?
hepatitis B virus X protein + H2O
?
-
-
-
-
?
IkappaBalpha + H2O
?
-
can be directly degraded by 20S proteasomes. Deletion constructs of IkappaBalpha allow us to the determine that N-terminal (DELTA1-70)and C-terminal regions (DELTA280-327, removing the PEST region) of IkappaBalpha are not required for IkappaBalpha degradation,while a further C-terminal deletion including part of the arm repeats (DELTAC2 245-327) almost completely suppress the degradation by 20S proteasome. Degradation of IkappaBalpha involves specific interactions with a C3 subunit of the proteasome
-
-
?
Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Leu-Arg-Arg + H2O
?
-
-
-
-
?
Leu-Leu-Glu + H2O
?
-
-
-
-
?
Leu-Leu-Val-Tyr + H2O
?
-
-
-
-
?
Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
MATalpha2 repressor + H2O
?
-
-
-
-
?
methyl-casein + H2O
?
-
-
-
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
N-Cbz-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
N-methoxysuccinyl-Glu-Val-Lys-Met-p-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
N-succinyl-LLVY-aminoluciferin + H2O
?
-
-
-
-
?
N-t-Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butyloxycarbonyl-LSTR-7-amido-4-methylcoumarin + H2O
?
-
highest activity in kidney
-
?
ovalbumin + H2O
?
-
-
-
-
?
oxidized insulin B chain + H2O
?
-
-
-
-
?
p27(KIP1) + H2O
?
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
PS1/gamma-secretase complex component + H2O
?
S-RNase + H2O
?
-
S-RNase is ubiquitinated and degraded by the 26S proteasome
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + Suc-Leu-Leu-Val-Tyr
-
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
succinyl-AAF-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide
?
-
-
-
-
?
tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
65% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
Tyr-Leu-Leu-Leu-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
ubiquitinylated proteins
?
unstable green fluorescence protein + H2O
?
-
artificial substrate for the proteasome. The model proteasomal substrate is stabilized by the carboxyl-terminal half of S5a, S5aC
-
-
?
Z-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Z-LLE-2-naphthylamide + H2O
Z-LLE + 2-naphthylamine
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
Z-LLE-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Z-LRR-aminoluciferin + H2O
?
-
-
-
-
?
Z-nLPnLD-aminoluciferin + H2O
?
-
-
-
-
?
additional information
?
-
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
-
tryspin-like activity
-
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
highest activity in testicle, brain and soleus
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
peptidyl-glutamyl-peptide-hydrolyzing activity
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
highest activity in testicle
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
for trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
for trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
casein + H2O
?
-
-
-
?
dihydrofolate reductase + H2O
?
-
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions. The folate metabolism may be impaired by an increased degradation of dihydrofolate reductase, mediated by the 20S proteasome
-
-
?
dihydrofolate reductase + H2O
?
-
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
-
most optimal combination of substrate residues identified
-
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
-
most optimal combination of substrate residues identified
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
highest activity in testicle, liver and spleen
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
PS1/gamma-secretase complex component + H2O
?
-
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1. Degradation of the complex components involves the proteasome, but regulation of their activity involves the PI3K/Akt pathway, overview. PS1/gamma-secretase is involved in the activation of phosphatidylinositol-3 kinase/Akt pathway, and is responsible for the intramembranous cleavage of various type-I membrane proteins. PS1/gamma-secretase is also deeply involved in the production of amyloid beta protein
-
-
?
PS1/gamma-secretase complex component + H2O
?
-
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
for chymotrypsin-like activity
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
for chymotrypsin-like activity
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
chymotrypsin-like activity
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
substrate for chymotrypsin-like activity of the 20S proteasome
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
A0A286S218; A0A286S1Z7; A0A286S200
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
for caspase-like activity
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
for caspase-like activity
-
-
?
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
for calpain-like activity
-
-
?
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
for calpain-like activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
peptidylglutamyl peptide hydrolase proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity with the specific fluorogenic substrate
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity
-
-
?
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
?
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
?
additional information
?
-
-
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
-
-
?
additional information
?
-
-
the 20S proteasome of Trypanosoma brucei shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
proteasome status in KG1a and U937 cells, overview
-
-
?
additional information
?
-
-
three major proteolytic activities of the proteasome can be distinguished as trypsin-like, chymotrypsin-like, and peptidyl-glutamyl peptide hydrolase activities, which cleave peptide bonds on the carboxyl side of basic, hydrophobic, and acidic amino acid residues, respectively. The catalytic core of the 20S proteasome is a Thr residue, responsible for the catalytic cleavage of substrates through nucleophilic attack
-
-
?
additional information
?
-
-
proteasome complexes possess three main catalytic activities, which are trypsin-like, chymotrypsin-like, and caspase-like
-
-
?
additional information
?
-
-
substrate docking sites, e.g. S5a, contain ubiquitin-interacting motifs that selectively recruit ubiquinated proteins to the proteasome. Human S5a-ubiquitin-interacting motifs stabilize only a subset of proteasomal substrates. Proliferation of A549 lung cancer cells is inhibited by S5a-ubiquitin-interacting motifs. S5a-ubiquitin-interacting motifs result in an increase in the number of apoptotic G0 cells, presumably because of inhibition of a subset of proteasomal substrate proteins
-
-
?
additional information
?
-
-
the proteasome cannot efficiently degrade unassembled R239C GFAP, and the interaction of R239C GFAP with proteasomes actually inhibits proteasomal protease activity. Soluble wild-type GFAP, but not R239C GFAP, is partially degraded by the 20 S proteasome
-
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Caspase-like sites cleave after aspartates better than after glutamates
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites
-
?
additional information
?
-
-
the chymotrypsin-like and trypsin-like activities, but not the peptidylglutamyl peptide hydrolyzing activity plays a key role in oocyte maturation
-
?
additional information
?
-
-
enzyme has a preference for aromatic residues at P1 such as Phe, Tyr, Trp, and His. Aliphatic side chains (propyl, butyl) are well tolerated in the P2 position. The S3 pocket accommodates bulky and hydrophobic residues
-
-
?
additional information
?
-
-
enzyme has a preference for aromatic residues at P1 such as Phe, Tyr, Trp, and His. Aliphatic side chains (propyl, butyl) are well tolerated in the P2 position. The S3 pocket accommodates bulky and hydrophobic residues
-
-
?
additional information
?
-
-
maximal chymotrypsin-like activity of the 20S proteasome, which contributes to the cytolytic mechanism of the natural killer cells, is associated with the conformational changes occuring in a cluster of highly conserved proteasome residues from the alpha-subunit that lead to the proteasome open conformation, allowing substrate access into the proteolytic chamber
-
-
?
additional information
?
-
-
the proteasome is a cylindrical, multicatalytic proteolytic machine with three peptidase activities, chymotryptic, tryptic and postglutamyl peptide hydrolytic
-
-
?
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
?
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
?
additional information
?
-
-
the purified proteasome, comprising 102 distinct proteins, shows high chymotrypsin-like activity, mass spectrometry and protein identifications, overview
-
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
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(-)-epigallocatechin-3-gallate
-
i.e. EGCG, inhibits the proteasomal chymotrypsin-like activity
(2E)-3-(4-tert-butylphenyl)-1-[4-(4-nitrophenyl)piperazin-1-yl]prop-2-en-1-one
-
-
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-triethoxybenzoate)
-
inhibits 48% of MDA-MB-231 cell proliferation at 0.05 mM
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-trihydroxybenzoate)
-
-
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-diethoxybenzoate)
-
70-79% inhibition in MDA-MB-231 cells at 0.025-0.050 mM
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-dihydroxybenzoate)
-
-
(acetato-kappaO)[2,4-diiodo-6-({[(pyridin-2-yl-kappaN)methyl]amino-kappaN}methyl)phenolato-kappaO]copper
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
2-(2-bromo-4-tert-butylphenoxy)-1-[4-(4-nitrophenyl)piperazin-1-yl]ethanone
-
-
2-(2-chlorophenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
-
2-(4-tert-butylphenoxy)-1-[4-(4-methoxy-2-nitrophenyl)piperazin-1-yl]ethanone
-
-
2-methyl-5-[4-(phenylamino)phthalazin-1-yl]-N-(tetrahydrofuran-2-ylmethyl)benzenesulfonamide
-
-
4-(4-methoxyphenyl)-N-(4-nitrophenyl)piperazine-1-carbothioamide
-
-
4-hydroxy-2-nonenal
-
specific subunits of the 20S proteasome are targeted for modification by 4-hydroxy-2-nonenal (0.5 mM)
4-tert-butyl-N-[4-(diethylsulfamoyl)phenyl]benzamide
-
-
4-tert-butyl-N-[4-(dipropylsulfamoyl)phenyl]benzamide
-
-
4-tert-butyl-N-[4-[di(prop-2-en-1-yl)sulfamoyl]phenyl]benzamide
-
-
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
acetyl-Leu-Leu-Arg
-
IC50: 0.85 mM for chymotrypsin-like activity, 0.0056 mM for trypsin-like activity
acetyl-Leu-Leu-norleucinal
-
competitive
adamantaneacetyl-(6-aminohexanoyl)3-(leucyl)3-vinylmethyl sulfone
-
-
AEBSF
-
25% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, 22% inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 19% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 21% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 26% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, 98% inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin
Aprotinin
-
0.0133 mg/ml, 53.62% inhibition
ATP
-
inhibits trypsin-like, peptidylglutamyl peptide hydrolase, and branched-chain amino acid preferring activities
belactosin A
-
isolated from a Streptomyces sp. strain
Belactosin C
-
isolated from a Streptomyces sp. strain
benzyloxycarbonyl-Ala-Ala-Phe-CH2Cl
-
-
benzyloxycarbonyl-GPAF aldehyde
-
-
benzyloxycarbonyl-GPFL aldehyde
-
-
benzyloxycarbonyl-IE-(Ot-Bu)-AL aldehyde
-
0.002 mg/ml, 75% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.002 mM, 8% inhibition of peptidyl-glutamyl-peptide-hydrolyzing activity, hydrolysis of benzyloxycarbonyl-LLE-2-naphthylamide
benzyloxycarbonyl-Leu-Gly-Arg
-
IC50: 0.11 mM for chymotrypsin-like activity, 0.0066 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Leu
-
0.1 mM, 84% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 43% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 20% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, 86% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
Benzyloxycarbonyl-Leu-Leu-Arg
-
IC50: 0.056 mM for chymotrypsin-like activity, 0.0014 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Leu-CH2Cl
-
-
benzyloxycarbonyl-Leu-Leu-Leu-CHO
-
reversible inhibitor, modulation by sodium ion
benzyloxycarbonyl-Leu-Ser-Arg
-
IC50: 0.017 mM for chymotrypsin-like activity, 0.0017 mM for trypsin-like activity
benzyloxycarbonyl-Leu-Thr-Arg
-
IC50: 0.065 mM for chymotrypsin-like activity, 0.0021 mM for trypsin-like activity
benzyloxycarbonyl-LLF aldehyde
-
-
benzyloxycarbonyl-LLL aldehyde
-
0.001 mg/ml, 69% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide
benzyloxycarbonyl-Phe-Ser-Arg
-
IC50: 0.0089 mM for chymotrypsin-like activity, 0.002 mM for trypsin-like activity
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
calpeptin
-
inhibits calpain-like activity
carbobenzoxy-L-leucyl-L-leucyl-leucinal
-
MG-132
cetyltrimethylammonium bromide
-
-
chloro[2,4-diiodo-6-({[(pyridin-2-yl-kappaN)methyl]amino-kappaN}methyl)phenolato-kappaO]copper
-
a copper complex, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
Cl-
-
inhibits peptidylglutamyl peptide hydrolase activity
clasto-lactacystin beta-lactone
-
complete inhibition of the chymotrypsin-like activity at 0.01 mM, complete inhibition of the trypsin-like activity at 0.02 mM, and complete inhibition of caspase-activity of the 26S proteasome at 0.02 mM
clastolactacystin-beta-lactone
-
-
cystatin
-
0.0133 mg/mL 46.38% inhibition
-
c[Ala-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Gly-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Ser-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
c[Val-Leu-Leu-Glu(Leu-vinyl ester)]
-
-
delanzomib
-
slow-binding inhibitor, kinetic analysis
dibromo[(dimethylamino)methanedithiolato(2-)-kappa2S1,S1]aurate(3-)
-
proteasome inhibition and apoptosis induction are completely blocked by addition of dithiothreitol or N-acetyl-L-cysteine, showing that process of oxidation is required for proteasome inhibition
diisopropylfluorophosphate
-
-
E-64
-
0.0133 mg/ml, 71.15% inhibition
E-64-d
-
0.1 mM, 30% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
ethanol
-
ethanol-induced proteasome inhibition in liver cells
glial fibrillary acidic protein
-
human recombinant GFP-tagged, accumulation of the intermediate filament protein, glial fibrillary acidic protein, GFAP, in astrocytes of Alexander disease impairs proteasome function in astrocytes, also oligomers of R239C mutant GFAP inhibit the proteasome system in Alexander disease astrocytes to an even higher extent compared to the wild-type GFAP. The small heat shock protein chaperone alphaB-crystallin reverses the inhibition by shifting the size of the mutant protein from larger oligomers to smaller oligomers and monomers. The proteasome cannot efficiently degrade unassembled R239C GFAP, and the interaction of R239C GFAP with proteasomes actually inhibits proteasomal protease activity in a non-competitive manner, detailed overview
-
H-Ala-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Gly-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Ser-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
H-Val-Leu-Leu-Glu(Leu-vinyl ester)-NH2
-
-
hepatitis B virus X protein
-
-
-
histone H3
-
activity with benzyloxycarbonyl-LAF-4-aminobenzoate, 87%, benzyloxycarbonyl-dALR-4-aminobenzoate, 43%, or benzyloxycarbonyl-LLE-2-naphthylamide, 81% as substrates
-
iodoacetic acid
-
1.0 mM, 54.04 mM inhibition
ixazomib
-
slow-binding inhibitor, kinetic analysis
Mn2+
-
inhibits peptidylglutamyl peptide hydrolase activity
mutant huntingtin
-
mutant huntingtin filamentous aggregates can inhibit 26S proteasome activity, but only when not recruited inclusion bodies
-
N,N'-bis(4-methoxyphenyl)tricyclo[3.3.1.13,7]decane-1,3-dicarboxamide
-
-
N-(1-hydroxy-2-methylpropan-2-yl)-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-(2-methyl-1,3-thiazole-5-carbonyl)-5-phenyl-L-norvalyl-N-[(1E,3S)-1-(methanesulfonyl)-5-methylhex-1-en-3-yl]-L-homoserinamide
-
compound has low nanomolar activity at killing parasite in the 72 h treatment with exceptionally low toxicity against human foreskin fibroblast resulting in greatly enhanced selectivity ratio. Compound has no toxicity to HepG2 cells even after 72 h treatment with doses as high as 10 microM
N-(3-hydroxy-2-oxopropyl)-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-(4-methoxyphenyl)-3-(4-methylphenyl)tricyclo[3.3.1.13,7]decane-1-carboxamide
-
-
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
60.06% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
89.7% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
69.7% inhibition at 0.01 mM
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
shows significant inhibition of 20S proteasome chymotrypsin-like, b5 activity
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
shows significant inhibition of 20S proteasome chymotrypsin-like, b5 activity
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
N-acetyl-Leu-Leu-norleucinal
-
-
N-acetyl-leucyl-leucyl-norleucinal
-
MG132, 0.03 mM
N-carbobenzoxy-L-leucyl-L-norvalinal
-
-
N-Cbz-Leu-Leu-leucinal
-
MG132
N-methoxysuccinyl-Glu-Val-Lys-Phe-H
-
modified
N-tert-butyl-5-[4-[(3-hydroxyphenyl)amino]phthalazin-1-yl]-2-methylbenzenesulfonamide
-
-
N-tosylphenylalanylchloromethylketone
-
-
N-[(1S)-1-benzyl-2-[[(1S)-1-(furan-2-ylcarbonyl)-3-methylbutyl]amino]-2-oxoethyl]-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
-
inhibits chymotrypsin-like activity of the 26S proteasome
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
58.5% inhibition at 0.01 mM
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
73.4% inhibition at 0.01 mM
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
82.2% inhibition at 0.01 mM
N-[4-(acetylsulfamoyl)phenyl]-2-(4-ethoxyphenyl)quinoline-4-carboxamide
-
-
N-[4-(acetylsulfamoyl)phenyl]-2-(4-ethylphenyl)quinoline-4-carboxamide
-
-
N-[4-(azepan-1-ylsulfonyl)phenyl]-4-tert-butylbenzamide
-
-
N-[4-(benzylsulfamoyl)phenyl]-2-methylbenzamide
-
-
N-[4-(benzylsulfamoyl)phenyl]-2-[4-(thiophen-2-yl)phenyl]quinoline-4-carboxamide
-
-
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
-
rational design and synthesis of a syringolin A-based lipophilic derivative, which proves to be a very potent syrbactin-based proteasome inhibitor
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
-
-
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
-
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
-
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
7.7% inhibition at 0.01 mM
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
16.5% inhibition at 0.01 mM
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]-O-methyl-L-tyrosinamide
-
73% inhibition at 0.01 mM
Nalpha-[(2S)-2-[2-(tert-butoxycarbonyl)hydrazinyl]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
-
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-(4-methoxyphenyl)butanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
84.8% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
47.5% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
67.1% inhibition at 0.01 mM
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
14.9% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
-
5.7% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
-
13.6% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-3-(4-methoxyphenyl)-1-oxopropan-2-yl]-O-methyl-L-tyrosinamide
-
60.5% inhibition at 0.01 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
-
36.4% inhibition at 0.01 mM
NH4Cl
-
lysosomal inhibitor
NLVS
-
irreversible inhibitor
NMDA
-
exposure causes the disassembly of 26S proteasomes and dissociation of E3, i.e. KCMF1, HUWE1, and UBE3A
NPLLLVS
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.04 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.007 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
NPLLNVS
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.063 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-carbamoylcoumarin. IC50: 0.077 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
ONX0912
-
a selective, irreversible inhibitor of the chymotrypsin-like activity of constitutive proteasome 20S and immunoproteasome 20S. ONX0912 exerts toxicity in Waldenstroem macroglobulinemia cells, by reducing bone marrow-derived interleukin-6 and insulin-like growth factor 1 secretion, thus inhibiting BM-induced p-Akt and phosphorylated extracellular signal-related kinase activation in Waldenstroem macroglobulinemia cells, overview. ONX0912 acts synergistically with bortezomib
p-chloromercuribenzoic acid
p65/relA
-
inhibits the degradation of IkappaBalpha by the proteasome
-
PA28
-
inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview
-
pepstatin
-
0.0133 mg/ml 76.09% inhibition
phenylmethylsulfonyl fluoride
prion protein
-
recombinant mouse aggregated beta-PrP binds directly to human 20S and 26S proteasomes, i.e. its 20S core particle, overview. Conversion of cellular prion protein, PrPC, to toxic beta-sheet isoforms, PrPSc, which inhibit the ubiquitin-proteasome system and lead to accumulation of the system substrates, are associated with the prion diseases. PrP aggregates inhibit by stabilising the closed conformation of the substrate entry channel. The 20S proteasome is not inhibited when the gate in the alpha-ring is open due to a truncation mutation or by association with PA26/PA28. Modelling of location of aggregated beta-sheet rich PrP binding to the 20S proteasome and inhibition mechanism, detailed overview
-
pro-epigallocatechin-3-gallate
-
i.e. pro-EGCG, inhibitory efficacy is greatly improved from 42% inhibition to 89% inhibition when combined with 3,5-dinitrocatechol
PSI
-
0.1 mM, 93% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin and benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
syringolin A methyl ester
-
-
-
syringolin B
-
SylB, synthesis and inhibitory potency, overview
TLCK
-
0.133 mg/ml, 79.57% inhibition
YLLLVS
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.048 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.033 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
Z-b-Ala-Val-Ser-Leu-vinyl ester
-
-
Z-beta-Ala-Leu-Leu-Leu-vinyl ester
-
-
Z-Gly-Leu-Leu-Leu-vinyl ester
-
-
Z-Gly-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)3-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)3-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)4-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)4-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)5-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)5-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)6-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)6-CO-Val-Ser-Leu-vinyl ester
-
-
Z-NH-(CH2)7-CO-Leu-Leu-Leu-vinyl ester
-
-
Z-NH-(CH2)7-CO-Val-Ser-Leu-vinyl ester
-
-
Zn2+
-
inhibits peptidylglutamyl peptide hydrolase activity
[Cu(HLI)(LI)]OAc
-
a copper complex, HLI is the ligand 2,4-diiodo-6-((pyridine-2-ylmethylamino)methyl)phenol, causes selective 20S proteasomal inhibition and apoptosis induction in several lines of cancer cells
-
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
-
i.e. S-2209, potently inhibits chymotrypsin-like proteasome activity of the human 20S proteasome. S-2209 targets NFkappaB activity, overview. S-2209 inhibits cell growth and induces apoptosis in human multiple myeloma cells, mechanisms, overview
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
-
i.e. S-2209, targets NFkappaB activity, overview
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
benzyloxycarbonyl-GGL-4-nitroanilide as substrate
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 89% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 24% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde
-
-
antipain
-
0.0133 mg/ml, 74.04% inhibition
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 91% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 12% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde
-
-
bortezomib
-
ONX0912 acts synergistically with bortezomib
bortezomib
-
induces apoptosis in primary myeloma cells, but causes no induction of apoptosis in peripheral blood mononuclear cells from healthy humans
bortezomib
-
the proteasome inhibitor bortezomib sensitizes previously resistant tumor cells, melanoma cells, for cytolytic T-cell attack
bortezomib
-
activates the mitochondrial pathway of apoptosis in activated CD4+ T cells by disrupting the equilibrium of pro-apoptotic and anti-apoptotic proteins at the outer mitochondrial membrane and by inducing the generation of reactive oxygen species
bortezomib
-
slow-binding inhibitor, kinetic analysis
bortezomib
-
proteasome inhibition with bortezomib led to an increased susceptibility to viral infection, e.g. with lymphocytic choriomeningitis virus, and proteasome inhibitors can alter Ag processing in vivo
bortezomib
-
i.e. [(1R)-3-methyl-1-[[(2S)-1-oxo-3-phenyl-2-[(pyrazinylcarbonyl)amino]propyl]amino]butyl]boronic acid, treatment of human respiratory syncytial virus-infected Balb/C mice with the proteasome inhibitor results in increased inflammation and mortality, in contrast to infected Vero cells, overview
bortezomib
-
an N-terminally blocked Phe-Leu dipeptide inhibitor containing a C-terminal boronic acid, inhibits chymotrypsin-likeand caspase-like actitivities of the proteasome, inhibitory pattern with the chymotrypsin-like activity of the intermediate-proteasome subtypes, overview
bortezomib
-
also termed VELCADE
Ca2+
-
-
Ca2+
-
inhibits peptidylglutamyl peptide hydrolase activity
Ca2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
carfilzomib
-
irreversible
carfilzomib
-
irreversible
CEP-18770
-
reversible
chymostatin
-
0.05 mg/ml, 98% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.05 mg/ml, 15% inhibition of trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
chymostatin
-
0.1 mM, 93% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 94% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, no inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, 93% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
chymostatin
-
partial inhibition
chymostatin
-
inhibits chymotrypsin-like activity
chymostatin
-
inhibits chymotrypsin-like activity
epoxomicin
-
-
epoxomicin
-
inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview
epoxomicin
-
irreversible inhibitor
epoxomicin
-
inhibits the proteasome and causes cell cycle arrest at G2/M
epoxomicin
-
EPOX, a specific proteasome inhibitor, abolishes chymotrypsin-like activity in both wild-type 20S and a3DN 20S mutant proteasomes after pre-treatment with 50 mM epoxomicin
epoxomicin
-
inhibits trypsin-like activity
epoxomycin
-
effect on mRNA and protein abundance in HeLa cells, overview
epoxomycin
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
epoxomycin
-
effect on mRNA and protein abundance in PC-12 cells, overview
H2O2
A0A286S218; A0A286S1Z7; A0A286S200
stable until 0.04 mM
H2O2
-
30% inhibition at 0.003 mM
K+
-
-
K+
-
inhibits peptidylglutamyl peptide hydrolase activity
lactacystin
-
-
lactacystin
-
effect on mRNA and protein abundance in HeLa cells, overview
lactacystin
-
a specific proteasome inhibitor
lactacystin
-
specific inhibitor of the proteasome, partial inhibition of proteasome activity enhances remyelination after cuprizone-induced demyelination, overview
lactacystin
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
lactacystin
-
effect on mRNA and protein abundance in PC-12 cells, overview
leupeptin
-
0.0133 mg/ml, 53.19% inhibition
leupeptin
-
0.05 mg/ml, 25% inhibition of chymotrypsin-like activity, hydrolysis of benzyloxycarbonyl-GGL-4-nitroanilide. 0.05 mg/ml, 88% inhibition of trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
leupeptin
-
inhibits trypsin-like activity
leupeptin
-
inhibits trypsin-like activity
leupeptin
-
inhibits trypsin-like activity
leupeptin
-
inhibits trypsin-like activity
leupeptin
-
inhibits trypsin-like activity
leupeptin
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.0015 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.1 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
MG-132
-
reversible inhibitor
MG115
-
-
MG115
-
0.1 mM, 99% inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, 80% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 61% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
MG132
-
-
MG132
-
effect on mRNA and protein abundance in HeLa cells, overview
MG132
-
effect on mRNA and protein abundance in NIH-3T3 and N2A cells, overview
MG132
-
0.1 mM, 98% inhibition of hydrolysis of succinyl-Leu-leu-Val-Tyr-7-amido-4-methylcoumarin, 13% inhibition of hydrolysis of tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, 82% inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin
MG132
-
31% residual chymotrypsin-like activity at 0.04 mM, 24% residual trypsin-like activity at 0.04 mM, and complete inhibition of caspase-activity of the 26S proteasome at 0.02 mM
MG132
-
i.e. Z-Leu-Leu-Leu-aldehyde, inhibits the chymotrypsin-like proteasome activity, inhibitory pattern with the chymotrypsin-like activity of the intermediate-proteasome subtypes, overview. Does not affect the caspase-like activity of subtypes II-2, I,-3, and I-4 at all
MG132
-
effect on mRNA and protein abundance in PC-12 cells
Mg2+
-
inhibits trypsin like activity
Mg2+
-
inhibits peptidylglutamyl peptide hydrolase activity
Mg2+
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
MLN9708
-
an N-capped dipeptidyl leucine boronic acid, a potent inhibitor of the proteasome in tumor cells
MLN9708
-
an N-capped dipeptidyl leucine boronic acid, a potent inhibitor of the proteasome in tumor cells
N-ethylmaleimide
-
1.0 mM, 31.91% inhibition
N-ethylmaleimide
-
inhibits trypsin-like and chymotrypsin-like activities
NPI-0052
-
irreversible
p-chloromercuribenzoic acid
-
0.1 mM, 6.4% inhibition
p-chloromercuribenzoic acid
-
-
p-chloromercuribenzoic acid
-
-
phenylmethylsulfonyl fluoride
-
0.1 mM, 75.36% inhibition
phenylmethylsulfonyl fluoride
-
inhibits trypsin-like activity
phenylmethylsulfonyl fluoride
-
-
PS-341
-
use in cancer therapy
PS-341
-
reversible inhibitor
SDS
-
trypsin-like activity, hydrolysis of benzyloxycarbonyl-GGR-2-naphthylamide
SDS
-
inhibits trypsin-like and chymotrypsin-like activities
SDS
-
inhibits peptidylglutamyl peptide hydrolase activity
SDS
-
significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5
SDS
-
inhibits trypsin-like activity
syringolin A
-
SylA, synthesis and inhibitory potency, overview
syringolin A
-
a tripeptide derivative, from Pseudomonas putida pv. syringae B728a, consisting of an N-terminal valine followed by the two non-proteinogenic amino acids 3,4-dehydrolysine and 5-methyl-4-amino-2-hexenoic acid, the latter two forming a twelve-membered macrolactam ring, irreversibly inhibits the eukaryotic proteasome, mechanism, overview. The biosynthesis of the compound involves genes sylA-sylE, structure, overview
Yu101
-
-
Yu101
-
Nrf1-/- mouse embryonic fibroblasts are impaired in the recovery of proteasome activity after transient treatment with the covalent proteasome inhibitor YU101
[Au(ESDT)]2
-
i.e. AUL15, a gold(I)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome and 26S proteasome in breast cancer cells
[Au(ESDT)]2
-
i.e. AUL15, a gold(I)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome
[AuBr2(ESDT)]
-
i.e. AUL12, a gold(III)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome and 26S proteasome in breast cancer cells
[AuBr2(ESDT)]
-
i.e. AUL12, a gold(III)-dithiocarbamato species, inhibits the chymotrypsin-like activity of purified 20S proteasome
additional information
-
proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
-
additional information
-
inhibition of purified 20S proteasome and 26S proteasome activities by epigallocatechin-3-gallate and its analogues, overview
-
additional information
-
design and synthesis of boron peptide analogue proteasome inhibitors based on the structure of belactosin C, overview
-
additional information
-
study of potent and selective inhibition of the 20S proteasome beta1 catalytic subsite by a series of vinyl ester cyclopeptide analogues synthesized on the basis of a class of cyclopeptides derived from linear prototype inhibitors, in which the exocyclic pharmacophoric unit Leu-vinyl ester is linked to the c-carboxyl group of the glutamic acid residue at the C-terminus. The compounds inhibit the caspase-like activity of the proteasome at nanomolar concentrations, and demonstrate good resistance to proteolysis and a capacity to permeate the cell membrane
-
additional information
-
screening of compounds for in vitro capacity to inhibit the chymotryptic-, tryptic-like, and post-acidic activities of the proteasome, overview. Detection of N-terminal-prolonged vinyl ester-based peptides as selective proteasome beta1 subunit inhibitors. The inhibitors demonstrate resistance to plasmatic proteases and a good capacity to permeate the cell membrane, but low inhibitory potencies. Inhibitors of the post-acidic activity of proteasomes neither induce cell death nor greatly inhibit cell proliferation
-
additional information
-
MLN9708 has a shorter proteasome dissociation half-life and improved pharmacokinetics, pharmacodynamics, and antitumor activity compared with bortezomib in clinical trials
-
additional information
-
assignment of species [CuLI]+ as the minimal pharmacophore needed for proteasomal chymotryspin-like activity inhibition, copper complex synthesis and structures, overview. The proteasomal chymotrypsin-like activity is inhibited by 45%, 60%,70% and 80% after 2, 4, 8, and 18 h, respectively, by the copper complexes in C4-2B prostate cancer cells, overview
-
additional information
-
gold(I)- and gold(III)-compound-mediated proteasome inhibition and cell death induction are completely reversed by the addition of reducing agents, e.g. dithiothreitol or N-acetyl-L-cysteine
-
additional information
-
detection of drug-like proteasome inhibitrs by a multistep structure-based virtual ligand screening strategy, effects on trypsin-like, chymotrypsin-like, and post-acidic proteasome activities, overview
-
additional information
-
syrbactins, a family of natural products produced by strains of the plant pathogen Pseudomonas syringae pv. syringae, that belong either to the syringolin or glidobactin class, are highly potent proteasome inhibitors
-
additional information
-
no direct inhibition of the proteasome by LY294002, but treatment with phosphatidylinositol-3 kinase inhibitors LY294002 or wortmannin, leads to increased levels of PS1/gamma-secretase components through an inhibitory effect on their degradation. Phosphatidylinositol-3 kinase inhibition may trigger the multiple mono-ubiquitination of PS1, which precludes the degradation of PS1/gamma-secretase through the proteasomal pathway, overview
-
additional information
-
MLN9708 has a shorter proteasome dissociation half-life and improved pharmacokinetics, pharmacodynamics, and antitumor activity compared with bortezomib in clinical trials
-
additional information
-
although inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity, inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity. When caspase-like sites are occupied by the uncleaved propeptide or inhibitor, their substrates still inhibit the chymotrypsin like activity
-
additional information
-
gold(I)- and gold(III)-compound-mediated proteasome inhibition and cell death induction are completely reversed by the addition of reducing agents, e.g. dithiothreitol or N-acetyl-L-cysteine
-
additional information
-
design and screening method development for protease inhibitors, that do not induce the proteasome, overview
-
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0.000086 - 0.000194
(-)-epigallocatechin-3-gallate
Homo sapiens
-
inhibition of the chymotrypsin-like activity of the proteasome in vitro, pH not specified in the publication, temperature not specified in the publication
0.019
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,4,5-trihydroxybenzoate)
Homo sapiens
-
for the chymotrypsin-like activity, pH 7.5, 37°C
0.029
(2R,3S)-1,2,3,4-tetrahydronaphthalene-2,3-diyl bis(3,5-dihydroxybenzoate)
Homo sapiens
-
for the chymotrypsin-like activity, pH 7.5, 37°C
0.00022
1-[1-(1-[(2,4-dioxoimidazolidin-1-ylimino)-methyl]-2-phenyl-ethylcarbamoyl)-2-(1H-indol-3-yl)-ethylcarbamoyl]-2-(1H-indol)
Homo sapiens
-
pH 7.5, 30°C
0.85
acetyl-Leu-Leu-Arg
Patiria pectinifera
-
IC50: 0.85 mM for chymotrypsin-like activity, 0.0056 mM for trypsin-like activity
0.11
benzyloxycarbonyl-Leu-Gly-Arg
Patiria pectinifera
-
IC50: 0.11 mM for chymotrypsin-like activity, 0.0066 mM for trypsin-like activity
0.056
Benzyloxycarbonyl-Leu-Leu-Arg
Patiria pectinifera
-
IC50: 0.056 mM for chymotrypsin-like activity, 0.0014 mM for trypsin-like activity
0.017
benzyloxycarbonyl-Leu-Ser-Arg
Patiria pectinifera
-
IC50: 0.017 mM for chymotrypsin-like activity, 0.0017 mM for trypsin-like activity
0.065
benzyloxycarbonyl-Leu-Thr-Arg
Patiria pectinifera
-
IC50: 0.065 mM for chymotrypsin-like activity, 0.0021 mM for trypsin-like activity
0.0089
benzyloxycarbonyl-Phe-Ser-Arg
Patiria pectinifera
-
IC50: 0.0089 mM for chymotrypsin-like activity, 0.002 mM for trypsin-like activity
0.0074
dibromo[(dimethylamino)methanedithiolato(2-)-kappa2S1,S1]aurate(3-)
Oryctolagus cuniculus
-
inhibition of the chymotrypsin-like activity of the 20S proteasome
0.000049 - 0.002
glidobactin A
0.0347
KAuBr4
Oryctolagus cuniculus
-
-
0.1
leupeptin
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.0015 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.1 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.0000373
MG-132
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00084 - 0.01
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00428 - 0.01
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.0015 - 0.01
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00942
N-(tert-butoxycarbonyl)-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00147 - 0.01
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00164
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00815
N-(tert-butoxycarbonyl)-O-methyl-L-tyrosyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00054 - 0.01
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
0.00028 - 0.01
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00274 - 0.01
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.00785
N-[(1S)-1-benzyl-2-[[(1S)-1-(furan-2-ylcarbonyl)-3-methylbutyl]amino]-2-oxoethyl]-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
Homo sapiens
-
-
0.00756
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00585
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00262
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00000865 - 0.0000796
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
0.00451 - 0.01
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
0.00723 - 0.01
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
0.00068 - 0.01
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
0.01
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.01
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.00682
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00785
Nalpha-[(2S)-2-[2-(tert-butoxycarbonyl)hydrazinyl]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00327
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-(4-methoxyphenyl)butanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00839
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.00642
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.01
Nalpha-[(2S)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.01
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-phenylalaninamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.01
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]-L-tyrosinamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.00601
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-3-(4-methoxyphenyl)-1-oxopropan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
in 10 mM HEPES (pH 7.6), at 37°C
0.01
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-[[(2S)-1-(furan-2-yl)-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-O-methyl-L-tyrosinamide
Homo sapiens
-
IC50 above 0.01 mM, in 10 mM HEPES (pH 7.6), at 37°C
0.007
NPLLLVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.04 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.007 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, most potent inhibitor for hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-meth
0.077
NPLLNVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.063 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-carbamoylcoumarin. IC50: 0.077 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.00102 - 0.0103
syringolin A
0.000757 - 0.0187
syringolin A methyl ester
-
0.00778 - 0.1078
syringolin B
0.033
YLLLVS
Trypanosoma brucei
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 IC50: 0.048 mM, inhibition of hydrolysis of Gly-Gly-Arg-7-amido-4-methylcoumarin. IC50: 0.033 mM, inhibition of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
additional information
additional information
Homo sapiens
-
cell growth inhibition activities, overview
-
0.000049
glidobactin A
Homo sapiens
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.002
glidobactin A
Homo sapiens
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.00084
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00428
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.0015
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-isoleucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00147
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00054
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00984
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
Homo sapiens
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00028
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00854
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00274
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00000865
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
Homo sapiens
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.0000796
N2-(decylcarbamoyl)-N-[(3E,5S,8S,9E)-2,7-dioxo-5-(propan-2-yl)-1,6-diazacyclododeca-3,9-dien-8-yl]-L-valinamide
Homo sapiens
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.00451
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
Homo sapiens
-
above, caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-3-[(naphthalen-2-ylmethyl)amino]-3-oxo-D-alaninamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00723
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00068
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
caspase-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00412
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
chymotrypsin-like, b5 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.01
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
Homo sapiens
-
above, trypsin-like, b1 activity of 20S proteasome, pH not specified in the publication, temperature not specified in the publication
0.00102
syringolin A
Homo sapiens
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.0103
syringolin A
Homo sapiens
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.000757
syringolin A methyl ester
Homo sapiens
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
-
0.0187
syringolin A methyl ester
Homo sapiens
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
-
0.00778
syringolin B
Homo sapiens
-
for the chymotrypsin-like activity, pH not specified in the publication, temperature not specified in the publication
0.1078
syringolin B
Homo sapiens
-
for the trypsin-like activity, pH not specified in the publication, temperature not specified in the publication
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malfunction
-
reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
malfunction
-
T-DNA insertion mutation in RPN1a results in increased trichome branches on main stem, and trichome number on rosette leaves and the main stem compared with the wild type plant
malfunction
-
reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
-
metabolism
-
inhibition of the proteolytic activity of the proteasome induces apoptosis and suppresses essential functions of activated human CD4+ T cells, and proteasome inhibition activates the mitochondrial pathway of apoptosis in human CD4+ T cells, detailed mechanisms of apoptosis, overview
metabolism
-
the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
-
the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
-
the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
-
the ubiquitin-proteasome pathway plays an important role in a variety of cellular functions, primarily via its proteolytic activity, and is one of the vital pathways in the cell that becomes dysfunctional as a result of chronic ethanol consumption. The inhibition of proteasome activity in the nucleus is therefore etiologically involved in the accumulation of damaged proteins in the nucleus, and in the deregulation of transcription
physiological function
-
it is possible to restore significant levels of enzyme activity to 17 of 18 disease causing missense mutations in human cystathionine beta-synthase expressed in Saccharomyces cerevisiae by exposure to ethanol, proteasome inhibitors, e.g. bortezomib or MG132, or deletion of the Hsp26 small heat shock protein. All three of these treatments induce Hsp70, which is necessary but not sufficient for rescue, overview. The treatment can also rescue disease-causing mutations in human p53 and the methylene tetrahydrofolate reductase gene
physiological function
-
oxidative stress caused by tert-butyl hydroperoxide and proteasome inhibition by lactacystin induce apoptosis in neurons and astrocytes. Suppression of proteasome activity triggers the translocation of cathepsin D from lysosomes to cytosol, mechanism, overview
physiological function
-
physiological effects of partial inhibition of proteolytic activities of the proteasome, overview
physiological function
-
proteasome inhibition increases the sensitivity of tumor cells toward cytolytic T-cell attack by NOXA-mediated enhancement of mitochondrial second mitochondria-derived activator of caspase, SMAC, release, overview
physiological function
-
the 20S proteasome is a multicatalytic protease playing a crucial role in cellular protein turnover in eukaryotes. It is involved in the maintenance of the biological homeostasis and degradation of key components of the cellmachinery. Critical cellular functions such as transcription, cell-cycle progression, cell differenciation, antigen processing, and tumor suppression rely on this molecular system
physiological function
-
the proteasome, a multicatalytic protease, is responsible for the generation of most MHC class I ligands
physiological function
-
the ubiquitin-proteasome pathway is essential for promoting the exchange of transcriptional factors on chromatin
physiological function
-
the ubiquitin-proteasome system is involved in many cellular functions by mediating selective protein degradation. Protein substrates are first selected and marked by polyubiquitination, polyubiquitinated proteins are next recognized and degraded by the 26S proteasome, which consists of a 20S catalytic core particle and a 19S regulatory particle. Once polyubiquitin on a substrate protein is recruited to the 19S RP, the protein moiety is unfolded, translocated into the 20S CP, and finally degraded with release of polyubiquitin, which is processed into free ubiquitin and recycled
physiological function
-
proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
physiological function
-
the 20S proteasome, which is the major proteolytic enzyme of the cell, is responsible for the generation of antigenic peptides derived from endogenously expressed foreign or aberrant protein molecules. The proteasome-generated spliced peptides are presented by MHC class I molecules to the outside world so that they can be specifically recognised by cytotoxic T lymphocytes at the cell surface. Peptide splicing is an intrinsic additional catalytic property of the proteasome
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
-
the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable. Immunoproteasome is responsible for breaking down foreign proteins into short antigenic peptides, which are ligands of MHC class I molecules. ATPase induced gate opening in the 20S CP
physiological function
-
the RPN1a subunit of the 26S proteasome is involved in trichome's branching in Arabidopsis thaliana through the giberellin and cytokinin signaling pathways
physiological function
-
proteasomal substrates usually are tagged by a substrate-anchored polyubiquitin chain, while some proteins are degraded following monoubiquitination. For randomly sampled representative substrates, monoubiquitinated substrates are smaller than the polyubiquitinated ones, are enriched in specific pathways
physiological function
-
proteasomal substrates usually are tagged by a substrate-anchored polyubiquitin chain, while some proteins are degraded following monoubiquitination. For randomly sampled representative substrates, monoubiquitinated substrates are smaller than the polyubiquitinated ones, are enriched in specific pathways, and, in humans, are structurally less disordered
physiological function
subunit PSMA8 is expressed in spermatocytes from the pachytene stage, and assembles a type of testis-specific core proteasome. Deletion of PSMA8 decreases the abundance of proteasome in testes. Meiotic proteins that are normally degraded at late prophase I, such as RAD51 and RPA1, remain stable in PSMA8-deleted spermatocytes. PSMA8-null spermatocytes exhibit delayed M-phase entry and are finally arrested at this stage, resulting in male infertility
physiological function
the 19S regulatory particle in 26S proteasomes performs stepwise substrate unfolding and opens the chamber gate in an ATP-dependent manner. Spontaneous dissociation of the regulatory particle in isolated 26S proteasomes leaves core particles with different gate sizes related presumably to different stages in the gate opening
physiological function
ubiquitin C-terminal hydrolase Ubp6 binds to the regulatory particle non-ATPase (Rpn) 1 via its N-terminal ubiquitin-like domain, whereas its catalytic ubiquitin-specific protease domain is positioned variably. Addition of ubiquitin aldehyde stabilizes the binding of the ubiquitin-specific protease domain in a position where it bridges the proteasome subunits Rpn1 and the regulatory particle triple-A ATPase (Rpt) 1. The ubiquitin-specific protease domain binds to Rpt1 in the immediate vicinity of the Ubp6 active site. The catalytic triad is positioned in proximity to the mouth of the ATPase module and to the deubiquitylating enzyme Rpn11. On the proteasome side, binding of Ubp6 favors conformational switching of the 26S proteasome into an intermediate-energy conformational state, in particular upon the addition of ubiquitin aldehyde
physiological function
-
proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
-
additional information
-
a decrease in proteasome activity induced by the injection of lactacystin in the corpus callosum in the remyelination process that normally occurs after cuprizone-induced demyelination markedly improves the remyelination process. It also attenuates the activation of NFkappaB and the recruitment of microglia and astrocytes, thus helping in the recovery of the mitochondrial respiratory chain activities that are affected by cuprizone treatment
additional information
-
inhibition of the proteasomes by gold complexes results in accumulation of ubiquitinated proteins and proteasome target proteins, and induction of cell death, but at significantly different levels
additional information
-
inhibition of this enzymatic activity with beta-subunit-specific proteasome inhibitors may provide an anti-tumoral effect by inhibiting cell proliferation and angiogenesis, and by selectively inducing apoptosis of tumor cells
additional information
-
primary Waldenstroem macroglobulinemia cells express higher level of immunoproteasome 20S compared with constitutive proteasome 20S. Selective inhibition of the chymotrypsin-like activity of constitutive proteasome 20S and immunoproteasome 20S represents a sufficient and successful strategy to induce antineoplastic effect in hematologic tumors
additional information
-
proteasome inhibitors, but not a Nedd8 pathway inhibitor, upregulate RNA levels of PSM genes in cancer cells
additional information
-
the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively
additional information
-
the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively
additional information
-
the barrel-shaped proteolytic 20S proteasome core particle which consists of four seven-subunit rings, is capped at one or both ends by 19S regulatory particles and is the central part of the large, 2.4 MDa, multi-subunit protease complexes performing ATP-dependent degradation of poly-ubiquitinated proteins, and being responsible for the majority of the non-lysosomal proteolysis which occurs in eukaryotic cells
additional information
-
the proteasomal chymotrypsin-like activity inhibition is associated with accumulated levels of ubiquitinated proteins
additional information
-
activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
additional information
-
development of an integrated proteomic approach, QTAX, for quantitative analysis of tandem affinity purified in vivo cross-linked protein complexes to capture protein interactions of all natures in a single analysis, overview. Investigation of cell cycle specific proteasome interaction networks
additional information
-
development of SpliceMet: a method that combines combinatorial computations with mass spectrometric analyses of proteasome-generated spliced peptides, for analysis of peptides, presented by MHC class I molecules on the cell surface, in a manner independent of cytotoxic T lymphocytes, kinetics, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
-
activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
-
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102300
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
113200
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
21800
-
14 * 27400 + 14 * 21800, surface induced dissociation mass spectrometry
22700
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
23200
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
23800
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
24300
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
24500
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
24700
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
26400
alpha5 subunit, predicted from amino acid sequence
27400
-
14 * 27400 + 14 * 21800, surface induced dissociation mass spectrometry
27500
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
28000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
30200
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
31000
-
x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
33000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
34400
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
37700
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
38500
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
42600
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
43800
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
44200
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
45400
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
45800
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
46900
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
47300
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
47800
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
48500
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
49300
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
56000
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
630000
-
non-denaturing PAGE
665000
-
non-denaturing PAGE
894000
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 scanning transmission electron microscopy
2000000
-
gel filtration
2000000
A0A286S218; A0A286S1Z7; A0A286S200
gel filtration
22000
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
22000
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
24000
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
24000
-
alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
24000
-
x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
24000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
25000
-
alpha, beta x * 27000 + x * 25000, SDS-PAGE
25000
-
x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
25000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
27000
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alpha, beta x * 27000 + x * 25000, SDS-PAGE
27000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
29000
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x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
29000
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
690000
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gel filtration
690000
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surface induced dissociation mass spectrometry
700000
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-
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heteromer
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the 20S proteasomes are cylinder-shaped heteromeric dimers with a subunit configuration of alpha7, beta7, beta7, alpha7
heterooctacosamer
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14 * 27400 + 14 * 21800, surface induced dissociation mass spectrometry
heterotetradecamer
x-ray crystallography
multimer
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7 * ? (20S alpha-type subunits) + 10 * ? (20S beta-type subnits) + 16 * ? (19S ATPase subunits) + 14 * ? (19S non-ATPase subunits)
octadecamer
O18413, P25161, P26270, P48601, P55035, Q7KMP8, Q9U7A2, Q9V3G7, Q9V3H2, Q9V3P6, Q9V3V6, Q9V3Z4, Q9V405, Q9V436, Q9VW54, Q9XZ61 1 * 113200, subunit p110, + 1 * 102300, subunit p97, + 1 * 56000, subunit P58, + 1 * 49300, subunit P56, + 1 + 57700, subunit p55, + 1 * 42600, subunit p54, + 1 * 47800, subunit p50, + 1 * 46900, subunit p48A, + 1 * 48500, subunit p48B, + 1 * 45400, subunit p42A, + 1 * 47300, subunit p42B, + 1 * 45800, subunit p42C, + 1 * 44200, subunit p42D, + 1 * 43800, subunit p39A, + 1 * 38500, subunit p39B, + 1 * 37700, subunit p37A, + 1 * 34400, subunit p37B, + 1 * 30200, subunit p30, theoretically determined by GENETYX-MAC 8.0
oligomer
14 * alpha + 14 * beta, the similarity of the derived amino acid sequences of 233 (alpha subunit) and 211 (beta subunit) residues, respectively, indicates that they arose from a common ancestral gene. The alpha-subunits have regulatory and targeting functions, while the beta-subunits carry the active sites
tetradecamer
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 1 * 28000, alpha1, + 1 * 24300, alpha2, + 1 * 33000, alpha3, + 1 * 27000, alpha4, + 1 * 27500, alpha5, + 1 * 29000, alpha6, + 1 * 25000, alpha7, + 1 * 24700, beta1, + 1 * 24000, beta2, + 1 * 23200, beta3, + 1 * 23800, beta4, + 1 * 22700, beta5, + 1 * 24500, beta6, + 1 * 24000, beta7, the 20S proteasome is made up of seven alpha-subunits and seven beta-subunits. Of the seven beta-type subunits, five contain pro-sequences that are proteolytically removed during assembly, and three of them are predicted to be catalytic based on primary sequence
tetramer
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alpha5-subunit PSMA5 exists as tetramer
polymer
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alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
polymer
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2 * alpah1-alpha7, beta1-beta7
polymer
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alpha, beta, 14 * 24000 + 14 * 22000, SDS-PAGE, alpha7,beta7,beta7,alpha7 in the 20S proteasome
additional information
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AE3 encodes the 26S proteasome lid subunit RPN8a that plays a role in specifying leaf adaxial identity
additional information
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the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
additional information
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the 26 S proteasome is composed of two subparticles, the 20S core protease that compartmentalizes the protease active sites and the 19S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. The 2.5-MDa core protease-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits, mass spectrometric analysis of the complex, overview
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additional information
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thre proteasomal subunits are identified as alpha6/Pre5, alpha3/Y13 and alpha5/Pup2 by internal sequencing of tryptic fragments. A fourth subunit is identified as alpha7/Prs1 by immunorecognition with a monoclonal antibody specific for C8
additional information
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the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings
additional information
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in the catalytic core, the 20S proteasome, the beta1, beta2 and beta5 subunits show peptidylglutamyl peptide hydrolyzing, trypsin-like and chymotrypsin-like activities, respectively. By INF-gamma and TNFalpha stimulus, these subunits are replaced by their counterparts LMP2, MECL-1 and LMP7, defined inducible subunits, thus originating the immunoproteasome
additional information
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in the 20S proteasome, the 20S core particle is composed of 28 subunits arranged in four stacked heptameric rings, alpha7beta7beta7alpha7, forming a symmetrical barrel-shaped structure. Determination of the subunits in proteasomal analysis, method optimization, overview
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha1-7beta1-7beta1-7alpha1-7, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring. Another form of proteasome, called immunoproteasome, in which three beta-subunits of the normal 20S, beta1, beta2, beta5 are replaced by three IFN-gamma induced beta-subunits, beta1i, beta2i, beta5i. ATPase induced gate opening in the 20S CP
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings
additional information
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around 15 subunits from 20000-115000, SDS-PAGE
additional information
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multiple subunits from 22000-110000, SDS-PAGE
additional information
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x * 31000, x * 29000, x * 25000, x * 24000, tricine-SDS-PAGE
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha17beta17beta17alpha17, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring
additional information
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on 1-D SDS-PAGE five to seven bands of molecular weight range 20 to 30 kDa that prove to be entirely proteasome subunits, when the constituents are separated by 2-D SDS-PAGE, an unexpectedly large number of subunits is observed with at least 46 spots present versus an absolute minimum of 14 possible for a 20S core
additional information
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multiple subunits from 21000-32000, SDS-PAGE
additional information
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multiple subunits from 23000-115000, SDS-PAGE
additional information
presence of 7 alpha-type and 7 beta-type subunits in the 20S complex
additional information
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presence of 7 alpha-type and 7 beta-type subunits in the 20S complex
additional information
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subunits from 20000-31000
additional information
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a ladder of 22200-33500 Da bands detected on SDS-PAGE
additional information
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alpha, beta x * 27000 + x * 25000, SDS-PAGE
additional information
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three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry
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