Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer (Q27632929)

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English	Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer	scientific article

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9 November 2019

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer (English)

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9 November 2019

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molecular chaperones

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Gottfried Otting

5

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9 November 2019

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E Liepinsh

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9 November 2019

M Baryshev

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9 November 2019

A Sharipo

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9 November 2019

M Ingelman-Sundberg

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9 November 2019

S Mkrtchian

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1 June 2001

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9 November 2019

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9 November 2019

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9 November 2019

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9 November 2019

457-471

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9 November 2019

Protein folding in the cell

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Protein folding in the ER.

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The protein disulphide-isomerase family: unravelling a string of folds

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Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum

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7 January 2021

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A stress-inducible rat liver endoplasmic reticulum protein, ERp29.

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Oligomerization properties of ERp29, an endoplasmic reticulum stress protein

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ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif

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Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells. Evidence for a unique role in secretory-protein synthesis.

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windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum

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TSH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells.

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Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone

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A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units

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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

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10.1016/S0969-2126(01)00607-4

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11435111%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11435111%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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