The death effector domains of caspase-8 induce terminal differentiation. - Wikidata - wikimedia - TriplyDB

The death effector domains of caspase-8 induce terminal differentiation.

The death effector domains of caspase-8 induce terminal differentiation.

http://www.wikidata.org/entity/Q30895986

about

Caspase-8 regulates TNF-α-induced epithelial necroptosis and terminal ileitis.A novel benzothiazole derivative YLT322 induces apoptosis via the mitochondrial apoptosis pathway in vitro with anti-tumor activity in solid malignancies.Caspase-8 as a therapeutic target in cancer.Proliferative versus apoptotic functions of caspase-8 Hetero or homo: the caspase-8 dimer controls cell fate.Cysteine proteases: mode of action and role in epidermal differentiation.Protease signaling in animal and plant-regulated cell death.FLIP(L) induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity.Caspase-8 isoform 6 promotes death effector filament formation independent of microtubules.

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P2860

The death effector domains of caspase-8 induce terminal differentiation.

http://www.wikidata.org/entity/Q30895986

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The death effector domains of caspase-8 induce terminal differentiation.

@ast

The death effector domains of caspase-8 induce terminal differentiation.

@en

type

label

The death effector domains of caspase-8 induce terminal differentiation.

@ast

The death effector domains of caspase-8 induce terminal differentiation.

@en

prefLabel

The death effector domains of caspase-8 induce terminal differentiation.

@ast

The death effector domains of caspase-8 induce terminal differentiation.

@en

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JOURNAL.PONE.0007879

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The death effector domains of caspase-8 induce terminal differentiation.

@en

P2093

Ainhoa Mielgo

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

Colin Jamora

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

David J Shields

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

Dwayne G Stupack

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

Pedro Lee

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

Ryon Graf

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

Samantha G Zeitlin

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

Simone Barbero

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

Vicente A Torres

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

P2860

Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis

The role of receptor internalization in CD95 signaling.

Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation

Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth

MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops

FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination

Caspase-8 serves both apoptotic and nonapoptotic roles

Desmoplakin: an unexpected regulator of microtubule organization in the epidermis.

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e7879

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scholarly article

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10.1371/JOURNAL.PONE.0007879

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11

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4

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Michael C Schmid

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2009-11-18T00:00:00Z

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38100021

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19924290

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2774162

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