Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. - Wikidata - awgldk - TriplyDB

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

http://www.wikidata.org/entity/Q39779420

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The human protein disulfide isomerase gene family ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor Disulphide production by Ero1α-PDI relay is rapid and effectively regulated Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface An interaction map of endoplasmic reticulum chaperones and foldases Inflammatory and oxidative stress in rotavirus infection The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration Protein folding and quality control in the ER Disulfide bond formation in the mammalian endoplasmic reticulum The P5 disulfide switch: taming the aging unfolded protein response Orchestration of secretory protein folding by ER chaperones Redox regulation in amyotrophic lateral sclerosis ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation Structure of the third catalytic domain of the protein disulfide isomerase ERp46 Co- and Post-Translational Protein Folding in the ER Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis Disulfide bonds in ER protein folding and homeostasis The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase.Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum Separation and identification of HSP-associated protein complexes from pancreatic cancer cell lines using 2D CN/SDS-PAGE coupled with mass spectrometry.Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis.Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases Endoplasmic reticulum protein ERp46 in renal cell carcinoma Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Novel roles for protein disulphide isomerase in disease states: a double edged sword?Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates Cyclophilin C Participates in the US2-Mediated Degradation of Major Histocompatibility Complex Class I Molecules.Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.Whole genome expression profiling associates activation of unfolded protein response with impaired production and release of epinephrine after recurrent hypoglycemia.Modulation of conotoxin structure and function is achieved through a multienzyme complex in the venom glands of cone snails.Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A.The disulfide isomerase ERp72 supports arterial thrombosis in mice.Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response.PDIA6 regulates insulin secretion by selectively inhibiting the RIDD activity of IRE1.Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.

P2860

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P2860

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

http://www.wikidata.org/entity/Q39779420

description

2009 nî lūn-bûn

@nan

2009年の論文

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2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@en

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@nl

type

label

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@en

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@nl

prefLabel

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@en

Protein disulphide isomerase f ...... rgeted to BiP client proteins.

@nl

P1433

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P1476

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P932

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P356

P1433

Journal of Cell Science

P1476

Protein disulphide isomerase f ...... argeted to BiP client proteins

@en

P2093

Catherine E Jessop

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

Jennifer J Simmons

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

Mohammed Tasab

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

Rachel H Watkins

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

P2860

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

The protein disulfide isomerase AGR2 is essential for production of intestinal mucus

ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C

ERp57 is essential for efficient folding of glycoproteins sharing common structural domains

The human protein disulphide isomerase family: substrate interactions and functional properties

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase

Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72

P304

4287-4295

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scholarly article

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10.1242/JCS.059154

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P407

P433

Pt 23

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P478

122

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P50

Neil J. Bulleid

P577

2009-11-03T00:00:00Z

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P5875

38416015

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P698

19887585

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P932

2779130

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