(Q29620467)

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

1 reference

1 reference

3

Walensky LD

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

6

Korsmeyer SJ

1 reference

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30 April 2017

author name string

Letai A

1

1 reference

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30 April 2017

Bassik MC

2

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

Sorcinelli MD

4

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

Weiler S

5

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

language of work or name

1 reference

30 April 2017

publication date

September 2002

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30 April 2017

1 reference

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30 April 2017

volume

2

1 reference

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30 April 2017

issue

3

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

30 April 2017

page(s)

183-92

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12242151

The Bcl-2 protein family: arbiters of cell survival

30 April 2017

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

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Regulation of apoptosis by BH3 domains in a cell-free system

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Anti-cancer activity of targeted pro-apoptotic peptides

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Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane

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Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis

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Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis

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Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases

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Bcl-2-family proteins: the role of the BH3 domain in apoptosis

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Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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Endonuclease G is an apoptotic DNase when released from mitochondria

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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 pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites

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Why and how are peptide-lipid interactions utilized for self defence?

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7 January 2021

Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria

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7 January 2021

Bim: a novel member of the Bcl-2 family that promotes apoptosis

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7 January 2021

Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis

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7 January 2021

Induction of BIM, a proapoptotic BH3-only BCL-2 family member, is critical for neuronal apoptosis

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7 January 2021

Conjugation of arginine oligomers to cyclosporin A facilitates topical delivery and inhibition of inflammation

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7 January 2021

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

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7 January 2021

The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2

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7 January 2021

Direct addition of BimL to mitochondria does not lead to cytochrome c release

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Cell permeable BH3-peptides overcome the cytoprotective effect of Bcl-2 and Bcl-X(L).

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BID: a novel BH3 domain-only death agonist

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7 January 2021

Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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7 January 2021

Magainins and the disruption of membrane-linked free-energy transduction

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Movement of Bax from the cytosol to mitochondria during apoptosis

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Calculation of protein conformation from circular dichroism

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7 January 2021

Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity

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Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis

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BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

145789

OpenCitations bibliographic resource ID

145789

1 reference