BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo (Q40615180)

22 September 2017

title

BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo (English)

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22 September 2017

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Rie Sugioka

1

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22 September 2017

Shigeomi Shimizu

2

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22 September 2017

Toshihiro Funatsu

3

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22 September 2017

Hiroshi Tamagawa

4

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22 September 2017

Yoshiki Sawa

5

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22 September 2017

Toru Kawakami

6

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22 September 2017

Yoshihide Tsujimoto

7

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22 September 2017

language of work or name

English

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publication date

1 November 2003

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22 September 2017

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22 September 2017

volume

22

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22 September 2017

issue

52

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22 September 2017

page(s)

8432-8440

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The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis

22 September 2017

cites work

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https://api.crossref.org/works/10.1038/SJ.ONC.1207180

Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax.

21 January 2018

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NH2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis

21 January 2018

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Evidence for alpha-helical conformation of an essential N-terminal region in the human Bcl2 protein.

21 January 2018

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Breaking the mitochondrial barrier

21 January 2018

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HIV-1 Tat induces microvascular endothelial apoptosis through caspase activation

21 January 2018

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Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells

21 January 2018

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Selective Activation of the Sodium-Independent, Cyclosporine A-Sensitive Calcium Pore of Cardiac Mitochondria by Doxorubicin

21 January 2018

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In vivo gene transfection with heat shock protein 70 enhances myocardial tolerance to ischemia-reperfusion injury in rat

21 January 2018

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The mitochondrion in apoptosis: how Pandora's box opens

21 January 2018

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The Bcl-2 protein family: arbiters of cell survival

21 January 2018

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7 January 2021

Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

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7 January 2021

Mitochondria and apoptosis

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7 January 2021

Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

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7 January 2021

Susceptibility of HIV-1-TAT transfected cells to undergo apoptosis. Biochemical mechanisms

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7 January 2021

Efficient selection for high-expression transfectants with a novel eukaryotic vector

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7 January 2021

Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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7 January 2021

Mechanisms of cell death in hypoxia/reoxygenation injury

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7 January 2021

In vivo protein transduction: delivery of a biologically active protein into the mouse

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7 January 2021

Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2.

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7 January 2021

Enzyme release from mitochondria during reoxygenation of rat liver

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7 January 2021

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

1 reference

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7 January 2021

Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c.

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7 January 2021

BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death

1 reference

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7 January 2021

Bcl-2 family: life-or-death switch

1 reference

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7 January 2021

VDAC regulation by the Bcl-2 family of proteins

1 reference

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7 January 2021

Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

1 reference

https://api.crossref.org/works/10.1038/SJ.ONC.1207180

7 January 2021

Bcl-2 targets the protein kinase Raf-1 to mitochondria

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https://api.crossref.org/works/10.1038/SJ.ONC.1207180

7 January 2021

Prevention of Hypoxic Liver Cell Necrosis byin VivoHumanbcl-2Gene Transfection

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https://api.crossref.org/works/10.1038/SJ.ONC.1207180

7 January 2021

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

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https://api.crossref.org/works/10.1038/SJ.ONC.1207180

7 January 2021

Identifiers

DOI

10.1038/SJ.ONC.1207180

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Dimensions Publication ID

22 September 2017

1026331936

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