Interaction of calreticulin with protein disulfide isomerase (Q38287669)

1 September 2017

Interaction of calreticulin with protein disulfide isomerase (English)

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1 September 2017

Baksh S

1

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1 September 2017

Burns K

series ordinal

2

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1 September 2017

Andrin C

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3

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1 September 2017

Michalak M

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4

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1 September 2017

language of work or name

English

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publication date

1 December 1995

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Journal of Biological Chemistry

1 September 2017

7

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based on heuristic

inferred from page(s)

published in

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1 September 2017

270

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1 September 2017

31338-31344

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1 September 2017

52

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Expression and purification of recombinant and native calreticulin

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Modulation of gene expression by calreticulin binding to the glucocorticoid receptor

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Calreticulin inhibits repetitive intracellular Ca2+ waves

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Inhibition of nuclear hormone receptor activity by calreticulin

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The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes

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Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase

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Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms.

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53 Signal recognition particle: A ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties

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Calreticulin: from Ca2+ binding to control of gene expression

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Protein disulphide isomerase: building bridges in protein folding

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Human liver calreticulin: characterization and Zn(2+)-dependent interaction with phenyl-sepharose

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Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase

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Calcium binding properties of rabbit liver protein disulfide isomerase

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Low-affinity Ca(2+)-binding sites versus Zn(2+)-binding sites in histidine-rich Ca(2+)-binding protein of skeletal muscle sarcoplasmic reticulum

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Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats

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Identifiers

DOI

10.1074/JBC.270.52.31338

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1 September 2017

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