Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

@en

Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

@en

Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

@nl

P1476

Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

@en

P2093

Lisa Bouchier-Hayes

http://www.w3.org/2001/XMLSchema#string

Samuel Sidi

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P2860

Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress

Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype.

Characterization of cytoplasmic caspase-2 activation by induced proximity.

Regulation of CED-3 caspase localization and activation by C. elegans nuclear-membrane protein NPP-14.

Nucleophosmin and cancer.

Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3.

PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling

An Inhibitor of PIDDosome Formation.

NPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus.

P304

e1348325

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P31

scholarly article

P356

10.1080/23723556.2017.1348325

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P433

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P478

http://www.w3.org/2001/XMLSchema#string

P577

2017-07-05T00:00:00Z

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P698

29057309

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P932

5644479

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