(Q40918013)

English

ATPase activity of the heat shock protein hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat-induced apoptosis

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scholarly article

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Europe PubMed Central

PubMed publication ID

24 September 2017

ATPase activity of the heat shock protein hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat-induced apoptosis (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

apoptotic process

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author name string

Volloch V

1

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Gabai VL

2

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Rits S

3

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Sherman MY

4

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Europe PubMed Central

PubMed publication ID

24 September 2017

language of work or name

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publication date

1 November 1999

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Europe PubMed Central

PubMed publication ID

24 September 2017

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Europe PubMed Central

PubMed publication ID

24 September 2017

461

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Europe PubMed Central

PubMed publication ID

24 September 2017

1-2

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

73-76

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Constitutive expression of heat-shock protein 70 in mammalian cells confers thermoresistance

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Induced thermotolerance to apoptosis in a human T lymphocyte cell line

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Importance of the ATP-binding domain and nucleolar localization domain of HSP72 in the protection of nuclear proteins against heat-induced aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Effects of expressing human Hsp70 and its deletion derivatives on heat killing and on RNA and protein synthesis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Role of Hsp70 in regulation of stress-kinase JNK: implications in apoptosis and aging

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Heat shock proteins: regulators of stress response and apoptosis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Escaping cell death: survival proteins in cancer

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

21 January 2018

Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

7 January 2021

The function of HSP72 in suppression of c-Jun N-terminal kinase activation can be dissociated from its role in prevention of protein damage

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901428-3

7 January 2021

Identifiers

10.1016/S0014-5793(99)01428-3

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

ResearchGate publication ID

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