Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function (Q24293924)

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8 January 2020

title

Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function (English)

1 reference

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Phorbol-12-myristate-13-acetate-induced protein 1

8 January 2020

main subject

apoptotic process

0 references

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BCL2-like 11 (apoptosis facilitator)

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B cell leukemia/lymphoma 2 related protein A1a

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Myeloid cell leukemia sequence 1

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BCL2-associated agonist of cell death

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BCL2 modifying factor

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author

Brian J. Smith

4

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8 January 2020

Catherine Day

8

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8 January 2020

Jerry Adams

9

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8 January 2020

David C Huang

10

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8 January 2020

author name string

Lin Chen

1

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8 January 2020

Simon N Willis

2

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8 January 2020

Andrew Wei

3

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8 January 2020

Jamie I Fletcher

5

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8 January 2020

Mark G Hinds

6

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8 January 2020

Peter M Colman

7

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8 January 2020

publication date

1 February 2005

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8 January 2020

language of work or name

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8 January 2020

volume

17

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issue

3

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page(s)

393-403

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Shape complementarity at protein/protein interfaces

8 January 2020

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Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair

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BH3-Only proteins-essential initiators of apoptotic cell death

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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The structure of a Bcl-xL/Bim fragment complex: implications for Bim function

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The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues

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The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex

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7 January 2021

BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis

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Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics

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Puma is an essential mediator of p53-dependent and -independent apoptotic pathways

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Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

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Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions

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Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins

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7 January 2021

MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2

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7 January 2021

Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

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8 January 2020

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Consolidated OpenCitations Corpus – April 2017