Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA. (Q35107469)

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English	Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 August 2017

Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA. (English)

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Europe PubMed Central

PubMed publication ID

6 August 2017

endoplasmic reticulum

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author name string

Tina C Albershardt

1

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Europe PubMed Central

PubMed publication ID

6 August 2017

Bethany L Salerni

2

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Europe PubMed Central

PubMed publication ID

6 August 2017

Ryan S Soderquist

3

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Europe PubMed Central

PubMed publication ID

6 August 2017

Darcy J P Bates

4

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Europe PubMed Central

PubMed publication ID

6 August 2017

Alexandre A Pletnev

5

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Europe PubMed Central

PubMed publication ID

6 August 2017

Alexei F Kisselev

6

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Europe PubMed Central

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6 August 2017

Alan Eastman

7

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PubMed publication ID

6 August 2017

language of work or name

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publication date

31 May 2011

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Europe PubMed Central

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6 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

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6 August 2017

286

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Europe PubMed Central

PubMed publication ID

6 August 2017

28

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Europe PubMed Central

PubMed publication ID

6 August 2017

24882-24895

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Vinblastine induces acute, cell cycle phase-independent apoptosis in some leukemias and lymphomas and can induce acute apoptosis in others when Mcl-1 is suppressed

1 reference

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The BCL-2 family reunion

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1 reference

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1 reference

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1 reference

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Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak

1 reference

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1 reference

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1 reference

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BCL-2 in the crosshairs: tipping the balance of life and death

1 reference

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Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha

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Bcl-2 changes conformation to inhibit Bax oligomerization

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1 reference

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ER stress and the unfolded protein response

1 reference

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Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate.

1 reference

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During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria

1 reference

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1 reference

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Simultaneous release of adenylate kinase and cytochrome c in cell death

1 reference

https://pubmed.ncbi.nlm.nih.gov/21628457

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Comparison of chemical inhibitors of antiapoptotic Bcl-2-family proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/21628457

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M111.255828

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

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