Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation (Q24298757)

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English	Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation	scientific article

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2 November 2019

Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation (English)

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2 November 2019

apoptotic process

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endoplasmic reticulum

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molecular chaperones

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Heat shock protein family A (Hsp70) member 5

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GOA release 2020-03-11

negative regulation of apoptotic process

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GOA release 2020-03-11

6

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2 November 2019

author name string

Ramachandra K Reddy

1

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2 November 2019

Changhui Mao

2

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2 November 2019

Peter Baumeister

3

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2 November 2019

Richard C Austin

4

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2 November 2019

Randal J Kaufman

5

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publication date

28 March 2003

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10

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Journal of Biological Chemistry

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278

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23

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20915-20924

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2 November 2019

Protein expression profiles in human breast ductal carcinoma and histologically normal tissue

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Mammalian stress response: induction of the glucose-regulated protein family

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Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78

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The glucose-regulated proteins: stress induction and clinical applications

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Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

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Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver

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Suicidal tendencies: apoptotic cell death by caspase family proteinases

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Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7.

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The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis

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p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release.

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Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation

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In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum

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Identifiers

10.1074/JBC.M212328200

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2 November 2019

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12665508%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

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