Structure/Function analysis of p55 tumor necrosis factor receptor and fas-associated death domain. Effect on necrosis in L929sA cells. (Q40855061)

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10 November 2019

title

Structure/Function analysis of p55 tumor necrosis factor receptor and fas-associated death domain. Effect on necrosis in L929sA cells (English)

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10 November 2019

9

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10 November 2019

author name string

Boone E

1

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10 November 2019

Vanden Berghe T

2

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10 November 2019

Van Loo G

3

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10 November 2019

De Wilde G

4

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10 November 2019

De Wael N

5

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10 November 2019

Vercammen D

6

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Fiers W

7

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10 November 2019

Haegeman G

8

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10 November 2019

language of work or name

English

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publication date

1 December 2000

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Journal of Biological Chemistry

10 November 2019

published in

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10 November 2019

volume

275

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10 November 2019

issue

48

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10 November 2019

page(s)

37596-37603

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Cell membrane permeabilization and cellular collapse, followed by loss of dehydrogenase activity: early events in tumour necrosis factor-induced cytotoxicity.

10 November 2019

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A novel domain within the 55 kd TNF receptor signals cell death

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The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis

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TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways

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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

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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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A potential mechanism of "cross-talk" between the p55 tumor necrosis factor receptor and Fas/APO1: proteins binding to the death domains of the two receptors also bind to each other

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Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

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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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Two CD95 (APO-1/Fas) signaling pathways

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Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity

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Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor.

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Activation of p42/p44 mitogen-activated protein kinases (MAPK) and p38 MAPK by tumor necrosis factor (TNF) is mediated through the death domain of the 55-kDa TNF receptor

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The 55-kDa tumor necrosis factor receptor induces clustering of mitochondria through its membrane-proximal region

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RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

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Apoptosis signaling by death receptors.

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21 January 2018

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A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway

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21 January 2018

Identifiers

DOI

10.1074/JBC.M007166200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10988295%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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