CDK11(p58) protein kinase activity is associated with Bcl-2 down-regulation in pro-apoptosis pathway (Q80362724)

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30 December 2019

title

CDK11(p58) protein kinase activity is associated with Bcl-2 down-regulation in pro-apoptosis pathway (English)

1 reference

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30 December 2019

author name string

Xiaojing Yun

1

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30 December 2019

Yihong Wu

2

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30 December 2019

Luyang Yao

3

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30 December 2019

Hongliang Zong

4

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30 December 2019

Yi Hong

5

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30 December 2019

Jianhai Jiang

6

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30 December 2019

Junwu Yang

7

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30 December 2019

Zhou Zhang

8

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30 December 2019

Jianxin Gu

9

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30 December 2019

publication date

22 May 2007

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Molecular and Cellular Biochemistry

30 December 2019

published in

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30 December 2019

volume

304

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30 December 2019

issue

1-2

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30 December 2019

page(s)

213-218

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https://scigraph.springernature.com/pub.10.1007/s11010-007-9502-x

30 December 2019

exact match

0 references

cites work

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

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12 December 2020

Cyclin-dependent kinase 11(p58) interacts with HBO1 and enhances its histone acetyltransferase activity

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Identification and characterization of a novel cell cycle-regulated internal ribosome entry site

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Downregulation of beta1,4-galactosyltransferase 1 inhibits CDK11(p58)-mediated apoptosis induced by cycloheximide.

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Fas-induced activation of the cell death-related protease CPP32 Is inhibited by Bcl-2 and by ICE family protease inhibitors

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PITSLRE protein kinase activity is associated with apoptosis

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BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax.

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p53 mediates bcl-2 phosphorylation and apoptosis via activation of the Cdc42/JNK1 pathway

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12 December 2020

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

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