Oligomerization properties of ERp29, an endoplasmic reticulum stress protein (Q28580894)

31 January 2017

title

Oligomerization properties of ERp29, an endoplasmic reticulum stress protein (English)

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31 January 2017

main subject

endoplasmic reticulum

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T. Sandalova

5

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Gunter Schneider

object named as

G. Schneider

6

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author name string

S. Mkrtchian

1

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31 January 2017

M. Baryshev

2

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31 January 2017

O. Matvijenko

3

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31 January 2017

A. Sharipo

4

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31 January 2017

M. Ingelman-Sundberg

7

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31 January 2017

S. Mkrtchiana

8

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31 January 2017

language of work or name

English

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publication date

24 July 1998

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31 January 2017

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31 January 2017

volume

431

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31 January 2017

issue

3

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31 January 2017

page(s)

322–326

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Protein folding in the cell

31 January 2017

cites work

1 reference

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

21 January 2018

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

21 January 2018

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

21 January 2018

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Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation

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Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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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

21 January 2018

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

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Combination of Direct DNA Sequencing with Degenerate Primer-Mediated PCR and 5′-/3′-RACE to Screen Novel cDNA Sequences

7 January 2021

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Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit.

7 January 2021

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10.1016/S0014-5793(98)00786-8

7 January 2021

Identifiers

DOI

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1 reference