Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.
about
ERp57 is essential for efficient folding of glycoproteins sharing common structural domainsMutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease AHuman Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′Is protein disulfide isomerase a redox-dependent molecular chaperone?ERp57 is a multifunctional thiol-disulfide oxidoreductaseComparative Analysis of the Interaction between Different Flavonoids and PDIA3Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.Increasing melanoma cell death using inhibitors of protein disulfide isomerases to abrogate survival responses to endoplasmic reticulum stress.Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.Generating an unfoldase from thioredoxin-like domainsA structural overview of the PDI family of proteins.The primary substrate binding site in the b' domain of ERp57 is adapted for endoplasmic reticulum lectin association.Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains.Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system.Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase.The effect of calnexin deletion on the expression level of PDI in Saccharomyces cerevisiae under heat stress conditions.ER Stress During the Pubertal Growth Spurt Results in Impaired Long-Bone Growth in Chondrocyte-Specific ERp57 Knockout Mice.
P2860
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P2860
Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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name
Domains b' and a' of protein d ...... ted in part by those of ERp57.
@en
type
label
Domains b' and a' of protein d ...... ted in part by those of ERp57.
@en
prefLabel
Domains b' and a' of protein d ...... ted in part by those of ERp57.
@en
P2093
P2860
P356
P1476
Domains b' and a' of protein d ...... ted in part by those of ERp57.
@en
P2093
Freedman RB
Kivirikko KI
Koivunen P
Pirneskoski A
Ruddock LW
P2860
P304
11287-11293
P356
10.1074/JBC.M010656200
P407
P577
2000-12-29T00:00:00Z