The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation. (Q54078688)

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31 October 2019

title

The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation (English)

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31 October 2019

9

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31 October 2019

Marek Łos

6

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31 October 2019

author name string

Belka C

1

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31 October 2019

Marini P

2

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31 October 2019

Lepple-Wienhues A

3

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31 October 2019

Budach W

4

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31 October 2019

Jekle A

5

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31 October 2019

Lang F

7

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31 October 2019

Schulze-Osthoff K

8

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31 October 2019

Bamberg M

10

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31 October 2019

language of work or name

English

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publication date

1 September 1999

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31 October 2019

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31 October 2019

volume

18

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31 October 2019

issue

35

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31 October 2019

page(s)

4983-4992

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https://scigraph.springernature.com/pub.10.1038/sj.onc.1202878

31 October 2019

exact match

0 references

cites work

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Role of reactive oxygen intermediates in activation-induced CD95 (APO-1/Fas) ligand expression

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

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Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment

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Regulation of the Lck SH2 domain by tyrosine phosphorylation

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Differential regulation and ATP requirement for caspase-8 and caspase-3 activation during CD95- and anticancer drug-induced apoptosis

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Ceramide-induced inhibition of T lymphocyte voltage-gated potassium channel is mediated by tyrosine kinases

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Differential requirement for caspase 9 in apoptotic pathways in vivo.

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Lck regulates Vav activation of members of the Rho family of GTPases

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Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis

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T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis

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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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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

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Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells

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Distinctive functions of Syk and Lyn in mediating osmotic stress- and ultraviolet C irradiation-induced apoptosis in chicken B cells.

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