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.

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.

Item

http://www.wikidata.org/entity/Q40832423

Q40832423

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ERp57 is essential for efficient folding of glycoproteins sharing common structural domains Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A Human 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 oxidoreductase Comparative Analysis of the Interaction between Different Flavonoids and PDIA3 Annular 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 domains A 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.

Item

http://www.wikidata.org/entity/Q40832423

description

2000 nî lūn-bûn

@nan

2000年の論文

@ja

2000年学术文章

@wuu

2000年学术文章

@zh-cn

2000年学术文章

@zh-hans

2000年学术文章

@zh-my

2000年学术文章

@zh-sg

2000年學術文章

@yue

2000年學術文章

@zh

2000年學術文章

@zh-hant

name

Domains b' and a' of protein d ...... ted in part by those of ERp57.

@en

type

Item

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

P1476

Domains b' and a' of protein d ...... ted in part by those of ERp57.

@en

P2093

Freedman RB

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Kivirikko KI

http://www.w3.org/2001/XMLSchema#string

Klappa P

http://www.w3.org/2001/XMLSchema#string

Koivunen P

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Pirneskoski A

http://www.w3.org/2001/XMLSchema#string

Ruddock LW

http://www.w3.org/2001/XMLSchema#string

P2860

Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer

Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit

ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase

Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.

Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

Collagens: molecular biology, diseases, and potentials for therapy.

The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity.

Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins.

ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin

P304

11287-11293

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scholarly article

P356

10.1074/JBC.M010656200

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English

P433

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276

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P577

2000-12-29T00:00:00Z

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11134056

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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

P2860

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

name

type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698