Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum - Wikidata - awgldk - TriplyDB

Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum

Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum

http://www.wikidata.org/entity/Q33676397

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The disulfide isomerase ERp72 supports arterial thrombosis in mice.Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.

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P2860

Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum

http://www.wikidata.org/entity/Q33676397

description

2014 nî lūn-bûn

@nan

2014 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի մարտին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Transient covalent interaction ...... s of the endoplasmic reticulum

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Transient covalent interaction ...... s of the endoplasmic reticulum

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type

label

Transient covalent interaction ...... s of the endoplasmic reticulum

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Transient covalent interaction ...... s of the endoplasmic reticulum

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prefLabel

Transient covalent interaction ...... s of the endoplasmic reticulum

@ast

Transient covalent interaction ...... s of the endoplasmic reticulum

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JBC.M113.520767

P1433

Journal of Biological Chemistry

P1476

Transient covalent interaction ...... s of the endoplasmic reticulum

@en

P2093

Aaron P Kellogg

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

Antonella S Treglia

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

Francesco Beguinot

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

Peter Arvan

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

Yoshiaki Morishita

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

P2860

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

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.

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry

The protein folding problem

Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum

Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM).

Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer.

P304

11488-11496

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scholarly article

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10.1074/JBC.M113.520767

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16

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289

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P50

Giuseppe Nicolardi

Dario Domenico Lofrumento

P577

2014-03-05T00:00:00Z

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

P5875

260559678

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24599957

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endoplasmic reticulum

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4036284

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