Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C51S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C55S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C85S/C92S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C92S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
K56G
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C21S
site-directed mutagenesis, almost inactive mutant
C24S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C27S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D29N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N
-
site-directed mutagenesis, unstable protein that still dimerizes but then aggregates, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N/R41S
-
site-directed mutagenesis, monomeric mutant, slightly decreased Pipe processing efficiency compared to the wild-type enzyme
D50A
-
site-directed mutagenesis, inactive mutant, normal dimerization
D50N
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
D50S
-
site-directed mutagenesis, altered Pipe targeting compared to the wild-type enzyme, normal dimerization
D85N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E32K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E60A
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E60Q
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
E60Y
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E88K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E88Q
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R/D29N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R/E60A
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
G87S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
H59Y
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K58S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K84D
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
K84N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K84S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
L219S/E212Q
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
L232K
-
site-directed mutagenesis, increased Pipe processing efficiency compared to the wild-type enzyme
P106D
-
site-directed mutagenesis, similar to the wild-type enzyme, altered conformation
R215A
-
site-directed mutagenesis, unaltered Pipe processing efficiency but eliminated Pipe targeting compared to the wild-type enzyme
R218D
-
site-directed mutagenesis, increased Pipe processing efficiency compared to the wild-type enzyme
R41S
-
site-directed mutagenesis, sligtly reduced dimerization of the mutant and processing of Pipe
T25K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
T63K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
V28D
-
site-directed mutagenesis, monomeric mutant, no dimerization, mutant aggregates
V28Y
-
site-directed mutagenesis, monomeric mutant, no dimerization, mutant aggregates
Y53S
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
Y55K
-
site-directed mutagenesis, mutant shows increased affinity for substrate Pipe but decreased processing efficiency compared to the wild-type enzyme
Y55K/D31N/R41S
-
site-directed mutagenesis, slightly decreased Pipe processing efficiency compared to the wild-type enzyme
Y55S
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
Y86F
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
Y86L
-
site-directed mutagenesis, highly decreased Pipe processing efficiency compared to the wild-type enzyme
Y86Q
-
site-directed mutagenesis, highly decreased Pipe processing efficiency compared to the wild-type enzyme
Y86S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D180R/D181R
the mutant shows 26.7% of wild type activity
D439A
119% of wild-type 4-hydroxylase activity
E231A/W232A/D233G
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
E231K
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
E431K
the mutant shows 53.6% of wild type activity
E454A
76% of wild-type 4-hydroxylase activity
F258A
-
strongly reduced binding of DELTA-somatostatin
F258I
-
no binding of DELTA-somatostatin
F258W
-
reduced binding of DELTA-somatostatin
F258W/I272A
-
the mutant shows stronger binding of signal peptide peptidase, SPP, than the wild-type enzyme. PDI F258W/I272A-myc competes with endogenous PDI for SPP and remains attached to SPP, leading to a reduced pool of SPP available for US2-mediated degradation of MHC class I
F299W
-
site-directed mutagenesis, the mutation reduces the interaction between the two chaperones ERP-57 and CANX, but no difference between wild-type and mutant ERP-57 chaperone is observed, even when CANX is additionally transfected, in plasma membrane expression of the enzyme, overview
F449A
63% of wild-type 4-hydroxylase activity
F449E
9% of wild-type 4-hydroxylase activity
F452R
115% of wild-type 4-hydroxylase activity
F454A
-
binds DELTA-somatostatin like wild-type
H278L
-
the mutant protein does not have an appreciable E2-binding activity
I196W
site-directed mutagenesis, the ERp27 mutant shows a structure and ERp57 binding similar to the wild-type enzyme
I272L
-
no binding of DELTA-somatostatin
I272N
-
no binding of DELTA-somatostatin
I272Q
-
no binding of DELTA-somatostatin
I272W
-
no binding of DELTA-somatostatin
I438E
79% of wild-type 4-hydroxylase activity
K246A
-
reduced binding of DELTA-somatostatin
K259A
-
binds DELTA-somatostatin like wild-type
K274A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
K326E
the mutant shows 56% of wild type activity
K326E/E431K
the mutant shows 82.2% of wild type activity
K332A
site-directed mutagenesis, the mutant shows binding affinity with calnexin identical to wild-type enzyme
K401Q
the mutant shows about 1.5fold less activity than the wild type enzyme
K451A
74% of wild-type 4-hydroxylase activity
K57A/K401A
the mutant shows about 4fold less activity than the wild type enzyme
K57E/K401E
the mutant shows about 7fold less activity than the wild type enzyme
K57Q
the mutant shows about 1.5fold less activity than the wild type enzyme
K57Q/K401Q
the mutant shows about 2.5fold less activity than the wild type enzyme
L242A
-
binds DELTA-somatostatin like wild-type
L242T
-
strongly reduced binding of DELTA-somatostatin
L244A
-
reduced binding of DELTA-somatostatin
L244W
-
strongly reduced binding of DELTA-somatostatin
L255A
-
binds DELTA-somatostatin like wild-type
L255R
-
reduced binding of DELTA-somatostatin
L343A
-
the mutant is more sensitive to proteinase K than wild type enzyme. The mutant shows the same chaperone activity as that of wild type PDI
L446E
107% of wild-type 4-hydroxylase activity
P235G
the mutant shows 61.3% of wild type activity
P245K
-
no full length protein
Q265L
-
the mutant displays similar E2-binding activity as the corresponding wild type proteins
Q265L/H278L
-
the mutant protein does not have any E2-binding activity
R120D
-
less than 2% of wild-type activity in NRCSQGSCWN oxidation assay
R120K
-
71% of wild-type activity in NRCSQGSCWN oxidation assay
R120Q
-
26% of wild-type activity in NRCSQGSCWN oxidation assay
R120S
-
40% of wild-type activity in NRCSQGSCWN oxidation assay
R280A
site-directed mutagenesis, the mutant shows a structure reduced binding of ERp27, wild-type and mutants, as compared to the wild-type ERp57
R282A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
R97E
the mutant shows 68.2% of wild type activity
S249A
-
reduced binding of DELTA-somatostatin
S249K
-
binds DELTA-somatostatin like wild-type
S256D
-
reduced binding of DELTA-somatostatin
V220I
-
binds DELTA-somatostatin like wild-type
V437D
102% of wild-type 4-hydroxylase activity
W128F
-
95% of wild-type activity in NRCSQGSCWN oxidation assay
H278L
-
the mutant protein does not have an appreciable E2-binding activity
-
Q265L
-
the mutant displays similar E2-binding activity as the corresponding wild type proteins
-
Q265L/H278L
-
the mutant protein does not have any E2-binding activity
-
C365S/C368S
active site mutant
Cys59/62/195/198Ala
the PDIL2-3 active site mutant is evenly dispersed within the endoplasmic reticulum lumen
C34S
-
site-directed mutagenesis, the mutant shows impaired lipase activity, the defect cannot be rescued by constitutive expression of lipA gene encoding lipase A
C146S
-
site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme
C35A
-
site-directed mutagenesis, reduced reduction activity compared to the wild-type enzyme
C35A/C146S
-
site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme
C294S/C325S
-
site-directed mutagenesis, exchange of the enzyme's cysteine residues involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
C35S
-
mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity
C379S
-
mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity
C398A/C401A
-
90% residual isomerase activity
C54A/C57A
-
30% residual isomerase activity
C54A/C57A/C398A/C401A
-
15% residual isomerase activity
C55S/C379S
-
The double active site mutant Cys55Ser, Cys379Ser is not capable of catalyzing protein folding
G36A
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
H37P
-
Mutagenesis of His37 to a Pro causes almost complete loss of activity
L39R
-
Mutagenesis of Lys39 to an Arg results in only a modest loss of activity
W34S
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
C409A
-
site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme
C64A
-
site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme
C90A
-
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme
C90A/C97A
-
site-directed mutagenesis, mutation of both non-active site cysteine residues, 60% and 80% reduced oxidase and isomerase activities, respectively, compared to the wild-type enzyme
C97A
-
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
F449R
-
mutation in the last alpha helix of domain a', 7.5-8fold reduced appearance rate of folding product RNase A
F449R
no 4-hydroxylase activity, 85% and 93% of wild-type isomerase and reductase activity, respectively
F449W
59%, 133% and 94% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
F449W
-
no DELTA-somatostatin binding
F449Y
79%, 42% and 87% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
F449Y
-
binds DELTA-somatostatin like wild-type
G448R
43%, 85% and 93% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
G448R
-
binds DELTA-somatostatin like wild-type
I272A
-
no binding of DELTA-somatostatin
I272A
-
the mutant shows similar proteinase K sensitivity like the wild type protein. The mutant shows significantly lower potency than wild type PDI in suppressing aggregation of denatured rhodanese
K450A
113% of wild-type 4-hydroxylase activity
K450A
-
binds DELTA-somatostatin like wild-type
L453E
13%, 23% and 48% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
L453E
-
no DELTA-somatostatin binding
R444A
43%, 83% and 79% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
R444A
-
binds DELTA-somatostatin like wild-type
additional information
the enzyme-deficient cyo1 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves, chloroplasts develop abnormally in cyo1 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark, albino phenotype, overview
additional information
-
the enzyme-deficient cyo1 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves, chloroplasts develop abnormally in cyo1 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark, albino phenotype, overview
additional information
-
certain T-DNA insertions in isoform PDIL2-1 have reduced seed set, due to delays in embryo sac maturation. These mutations act sporophytically, and funicular and micropylar pollen tube guidance are disrupted. A PDIL2-1-yellow fluorescent protein fusion is mainly localized in the endoplasmic reticulum and is expressed in all tissues examined. In ovules, expression in integument tissues is much higher in the micropylar region in later developmental stages, but there is no expression in embryo sacs
additional information
-
development of a versatile baculovirus expression and secretion system, using the enzyme as a fusion partner. Fusion improves the secretions and antibacterial activities of recombinant nuecin proteins
additional information
expression of full protein, domain a + part of domain b comprised of residues 1-162, parts of domains b + b' comprised of residues 163-315, and part of domain b' + domain a' including c comprised of resiudes 316-494, respectively, in Escherichia coli. Segment 1-162 lacks isomerase activity, while segment 316-494 displays wild-type like activity
additional information
-
expression of full protein, domain a + part of domain b comprised of residues 1-162, parts of domains b + b' comprised of residues 163-315, and part of domain b' + domain a' including c comprised of resiudes 316-494, respectively, in Escherichia coli. Segment 1-162 lacks isomerase activity, while segment 316-494 displays wild-type like activity
additional information
-
construction of a PDI-2 defective mutant, mutations in gene pdi-2 result in severe body morphology defects, uncoordinated movement, adult sterility, abnormal molting and aberrant collagen deposition, cuticle collagens are disrupted in pdi-2 mutants, role of PDI-2 in collagen biogenesis can be restored following complementation of the mutant with human PDI, complementation of the pdi-2 mutant phenotype requires intact thioredoxin active sites, overview
additional information
-
pdi-3(ka1) crosses with specific collagen and collagen enzyme mutants, three transgenic lines all express the spliced transgenic product, phenotypes and genotypes, overview
additional information
-
construction of deletion mutants DELTA28RB60, L28 and L50
additional information
-
construction of deletion mutants DELTA28RB60, L28 and L50
-
additional information
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
a naturally occuring mutant strain with mutated, nonfunctional PDI shows complete resistance to infection, attachement and entry, of Chlamydia species, expression of enzymatically nonfunctional PDI can restore Chlamydia sp. attachment but not entry into mutant CHO6 cells, while expression of functional PDI restores the complete Chlamydia infection, overview
additional information
-
construction of several functional-Trx-domain mutants, that are affected in their in vivo oxidative folding activity to different extents, overview
additional information
-
dsbC null mutants do not show an altered phenotype, mutation of the entire DsbC disulfide isomerization pathway causes an increased sensitivity to the redox-active copper in cells
additional information
-
the mutational introduction of the AppA nonconsecutive disulfide bond into the AppA homologue Agp, which is independent of DsbC, renders the Agp mutant dependent on DsbC, overview
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
chromosomal insertion of the human PDI gene into the Saccharomyces cerevisiae PDI1 disruption mutant strain cannot rescue the mutant, the human enzyme is functionally not equivalent to the yeast enzyme, tetrad analysis, overview
additional information
construction of several deletion mutants of PDI by elimination of partial domains or whole domains, overview
additional information
-
under thermally denaturing conditions of 80°C or at 1 M guanidine-HCl the wild-type PDI is still active in renaturing LDH, while the mutant abb'a', lacking the C-terminal domain c, loses its chaperone function
additional information
construction of deletion mutants of ERp27 with deletions at the N terminus to P34 and/or at the C terminus to Leu257, overview
additional information
-
construction of deletion mutants of ERp27 with deletions at the N terminus to P34 and/or at the C terminus to Leu257, overview
additional information
-
eliminating the isomerase activity of PDI does not affect ERalpha-ERE complex formation, overview
additional information
-
analysis of binding and dissociation constants of various antibiotics with PDI and PDI domain deletion mutants lacking domains abb', domains b'a'c, domains aba'c
additional information
-
knockdown of PDI in MCF-7 human breast cancer cells with RNAi down-regulates estrogen receptor alpha protein but upregulates estrogen receptor beta protein, resulting in a drastic increase in estrogen receptor alpha/beta ratio, which is a crucial determinant of different cellular responses to estrogens. PDI can directly interact with estrogen receptor alpha, but it does not interact with estrogen receptor beta
additional information
-
overexpression has significant effects on cell-cell fusion mediated by Newcastle disease virus. Overexpression results in increased membrane fusion, and enhanced production of free thiols in Newcastle disease virus fusion protein when expressed without hemagglutinin-neuraminidase protein but drecreased free thiols in Newcastle disease virus fusion protein expressed with hemagglutinin-neuraminidase protein. Overexpression favors a postfusion conformation of surface-expressed Newcastle disease virus fusion protein in the presence of hemagglutinin-neuraminidase protein
additional information
-
overexpression of isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit results in increased protein disulfide isomerase activity and abrogates the apoptosis-enhancing effect of inhibitor bacitracin. Overexpression of a mutant lacking protein disulfide isomerase activity does not increase cellular enzymic activity or block the effects of bacitracin
additional information
-
transfection of EA.hy926 cells and exposure to Mn2+ results in the appearance of surface protein thiol groups, which can be found in PDI and integrin alphaVbeta3, both proteins colocalizing on the cellular surface, and the formation of the PDI-alphaVbeta3 complex, which dissociates upon reduction. The PDI-alphaVbeta3 complex induces conversion of the integrin to the ligand-competent high-affinity state
additional information
-
HeLa cells are transfected with PDI-targeting siRNA for PDI knockdown leading to resistance to Chlamydia inefctions
additional information
-
knockdown of PDI by RNA-mediated interference inhibits the degradation of MHC class I molecules catalysed by human cytomegalovirus glycoprotein US2 but not by its functional homolog US11. Overexpression of the substrate-binding mutant of PDI, but not the catalytically inactive mutant, dominant-negatively inhibits US2-mediated dislocation of MHC class I molecules by preventing their release from US2. PDI associated with signal peptide peptidase, SPP, independently of US2 and knockdown of PDI inhibits SPP-mediated degradation of CD3d but not Derlin-1-dependent degradation of CFTR DeltaF508
additional information
loss of the two cysteines in the C-terminal a' domain increases the Km for substarte RNase A, and loss of an additional cysteine in the a domain resulted in an even further increase of the Km
additional information
-
loss of the two cysteines in the C-terminal a' domain increases the Km for substarte RNase A, and loss of an additional cysteine in the a domain resulted in an even further increase of the Km
additional information
mutation of the cysteine residues in PDIp's active sites, resulting in mutants DELTAC1, DELTAC2 and DELTAC1DELTAC2, completely abolishes its enzymatic activity but does not affect its chaperone activity, the b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
additional information
-
mutation of the cysteine residues in PDIp's active sites, resulting in mutants DELTAC1, DELTAC2 and DELTAC1DELTAC2, completely abolishes its enzymatic activity but does not affect its chaperone activity, the b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
additional information
-
transfection of HUVECs with PDI siRNA using electroporation by nucleofector
additional information
-
transiently silencing PDI mRNA and increasing the intracellular levels of members of the PDI family, PDI, ERp72, and PDIp, have an effect on the mRNA levels, assembly and secretion of an IgG4 isotype, overview
additional information
-
wild-type PDI or PDI mutated in all four redox cysteines overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression, with 2.5fold enhanced basal cellular ROS production and membrane NADPH oxidase activity, with 3-fold increase in Nox1, but not Nox4 mRNA, phenotype, overview. Knockdown of PDI leads to Nox1 mRNA and protein downregulation
additional information
TXNDC5 knockdown in lung cancer cells generation of TXNDC5 mutants with individual thioredoxin-like domain being deleted. Knockdown of TXNDC5 in lung cancer cells leads to more localization of Srx in the cytosol. Mutation of cysteines in the thioredoxin domains of TXNDC5 leads to the loss of its binding to Srx. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death and enhances EGF-induced MAPK activation in in A549 cells
additional information
-
TXNDC5 knockdown in lung cancer cells generation of TXNDC5 mutants with individual thioredoxin-like domain being deleted. Knockdown of TXNDC5 in lung cancer cells leads to more localization of Srx in the cytosol. Mutation of cysteines in the thioredoxin domains of TXNDC5 leads to the loss of its binding to Srx. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death and enhances EGF-induced MAPK activation in in A549 cells
additional information
-
downregulation of protein disulfide isomerase gene expression by siRNA leads to an average 36.8% inhibition of gene expression and correlates with a 3.2fold increase in tumor necrosis factor alpha release into the cell supernatant
additional information
-
mutant Agr2-/- mice lacking AGR2 are viable but are highly susceptible to colitis, the mutant mice show a 3fold reduced Muc2 mRNA level
additional information
-
PDI gene silencing in NS0/2N2 cells by transfection with two different PDI siRNAs, PDI1 and PDI2, respectively. Transiently silencing PDI mRNA in NS0/2N2 cells and increasing the intracellular levels of members of the PDI family, PDI, ERp72, and PDIp, have an effect on the mRNA levels, assembly and secretion of an IgG4 isotype, overview
additional information
-
replacement of the signal sequence and ER retention sequence by those of Pichia pastoris for elimination of glycosylation sites facilitating the recombinant expression in yeast
additional information
AY919669
replacement of the signal sequence and ER retention sequence by those of Pichia pastoris for elimination of glycosylation sites facilitating the recombinant expression in yeast
additional information
-
construction of mutants deficient in either DsbA or DsbC, or both, the dsbA mutant does no longer produce extracellular enzymes elastase, alkaline phosphatase, and lipase, while in the dcbC mutant the lipase activity is doubled, introduction of dsbC into the dsbA mutant results in low extracellular lipase activity, overview
additional information
suppression of cell-surface PDI expression with antisense oligodeoxynucleotide in RPAE cells
additional information
-
a domain a'-deletion mutant shows reduced activity in refolding of RNase compared to the wild-type enzyme
additional information
-
construction of a mutant PDI defective in the a' domain, which bears the isomerase activity, a PDI deletion yeast mutant cannot be rescued by the rat PDI
additional information
-
PDI can rescue a PDI-deficient mutant strain as well as mutants deficient in PDI homologues Eug1p, Mpd1p, Mpd2p, and Eps1p
additional information
-
the PDI1 disruption mutant strain cannot be rescued by chromosomal insertion of the human PDI gene, the human enzyme is not functionally equivalent to the yeast enzyme, tetrad analysis, overview
additional information
-
the PDI1 disruption mutant strain cannot be rescued by chromosomal insertion of the human PDI gene, the human enzyme is not functionally equivalent to the yeast enzyme, tetrad analysis, overview
-
additional information
gene silencing of PDI-1 and PDI-2 by RNAi constructs does not influence the cell growth
additional information
-
gene silencing of PDI-1 and PDI-2 by RNAi constructs does not influence the cell growth