Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death (Q24336389)

cysteine-type peptidase activity

GOA release 2020-03-11

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Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities

GOA release 2020-03-11

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M P Boldin

1

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T M Goncharov

series ordinal

2

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Y V Goltsev

series ordinal

3

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D Wallach

series ordinal

4

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language of work or name

English

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publication date

14 June 1996

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published in

Cell

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volume

85

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issue

6

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page(s)

803-15

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cites work

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The baculovirus p35 protein inhibits Fas- and tumor necrosis factor-induced apoptosis.

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Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

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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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Molecular cloning of the interleukin-1 beta converting enzyme

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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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FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis

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Multiple pathways originate at the Fas/APO-1 (CD95) receptor: sequential involvement of phosphatidylcholine-specific phospholipase C and acidic sphingomyelinase in the propagation of the apoptotic signal.

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Fas and tumor necrosis factor receptor-mediated cell death: similarities and distinctions

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The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit

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Genetic control of programmed cell death in the nematode C. elegans.

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Involvement of an ICE-like protease in Fas-mediated apoptosis

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A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells

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Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method

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A novel genetic system to detect protein-protein interactions

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Segregation of APO‐1/Fas antigen‐ and tumor necrosis factor receptor‐mediated apoptosis

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ICE family proteases: mediators of all apoptotic cell death?

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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

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

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Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases

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Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme

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ICE-like proteases in apoptosis

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Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

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Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis

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Proteolysis of fodrin (non-erythroid spectrin) during apoptosis.

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Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway

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Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases

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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

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Protection from tumor necrosis factor cytotoxicity by protease inhibitors

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CPP32/apopain is a key interleukin 1 beta converting enzyme-like protease involved in Fas-mediated apoptosis

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

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Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product

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CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas- and tumor necrosis factor-induced apoptosis

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Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

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A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes

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Two tumour necrosis factor receptors: structure and function.

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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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The pathophysiology of tumor necrosis factors

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Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death

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Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein

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The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

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