About: Differential role of caspase-8 and BID activation during radiation- and CD95-induced apoptosis

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About: Differential role of caspase-8 and BID activation during radiation- and CD95-induced apoptosis Goto Sponge NotDistinct Permalink

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scientific article published on 01 February 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 2000 (uk) im Februar 2000 veröffentlichter wissenschaftlicher Artikel (de) wüsseschaftlicher Artikel, wo im Hornig 2000 veröffentlicht worden isch (gsw) article scientifique publié en février 2000 (fr) artículu científicu espublizáu en febreru de 2000 (ast) artikull shkencor i botuar më 01 shkurt 2000 (sq) scientific article published on 01 February 2000 (en)
publication date	wds:Q73540307-0DD2AA16-96B1-4A34-B87E-4232745D4095
publication date	2000-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73540307-753F43CE-0C9F-4FD7-8017-F5D78A777EF3
language of work or name	English
exact match	wds:Q73540307-81321400-1E05-4D5F-8909-D28DA5A45EB1
exact match	https://scigraph.springernature.com/pub.10.1038/sj.onc.1203401
cites work	wds:Q73540307-0F52E7BF-9181-43BD-B7AB-A1BCFAC1F185 wds:Q73540307-11E0DBEA-1F75-42F1-AEB2-534D18454C08 wds:Q73540307-1E855243-BB74-4365-BDDF-31DD65523A16 wds:Q73540307-1FF94EF9-7E8F-415B-89F8-7723DEEB49D9 wds:Q73540307-24AE3613-B4F1-4DC7-9FD2-88E312D1B37A wds:Q73540307-28A30B70-4976-4A18-B7DE-5898DAA6AD36 wds:Q73540307-3153E1B0-4101-4C0E-831D-CC2B2BE55ED2 wds:Q73540307-34AC3D5F-A650-4557-948F-640865AE9BFD wds:Q73540307-3A4752CE-1165-46A2-BE6B-665A03AAFC51 wds:Q73540307-422D6C13-9C20-4E00-A137-31BC6E5D4CC8 wds:Q73540307-46608CC9-D43D-408A-9FCA-DF0FD2E12C5C wds:Q73540307-4B445C64-1653-444E-AB86-AE9BADB7F063 wds:Q73540307-4E5F34B2-393E-4798-97F8-E12EE0228EF4 wds:Q73540307-54D7054B-C389-46C6-93A9-CA5436B25CF4 wds:Q73540307-5660AEB0-4858-4654-81D9-89315E8B83B5 wds:Q73540307-5A292849-53CC-4DC3-A672-012E46BA5ACE wds:Q73540307-5EC1479C-8948-462A-A0EB-97BFEFF7DA6A wds:Q73540307-60921F26-3D81-48D5-B1CC-A1A4D97779AC wds:Q73540307-627F3E06-32B3-495A-9BE5-A1302EC7BCEF wds:Q73540307-6A2573E4-E86C-4AE5-8340-C780EC541680 wds:Q73540307-73A13A7C-373A-4C8D-BCC3-30875C0D84C9 wds:Q73540307-83471124-5F06-415A-9077-1D949B5F5A87 wds:Q73540307-835D40A7-38E6-4B8E-A6E1-47F2FC20B2E0 wds:Q73540307-83B22427-5423-414F-9247-C3621358A347 wds:Q73540307-843BFFA8-C330-4E68-B894-D4D598E72D3F wds:Q73540307-8A8B6016-5C7A-4DE4-BD33-0E6196EDB81E wds:Q73540307-8D332AF5-E353-4695-BF30-FDBB6C80A87D wds:Q73540307-8FC4EA75-828C-4322-843B-65782956FB2D wds:Q73540307-90E08920-8364-400F-937B-12B1A22493CF wds:Q73540307-94CCAB05-A0E6-4B78-AA90-65815F418B6C wds:Q73540307-959DDE73-9216-4DE1-BC49-2F5D540199C2 wds:Q73540307-99494B5B-37E3-4717-A9FB-9E6C725C7479 wds:Q73540307-99E348FF-6FA7-4E9D-B1F6-65C2DCACBEFB wds:Q73540307-9DB43F49-A1F7-43CF-9645-F86AA3483229 wds:Q73540307-A1DABC92-B4B3-4998-A0F7-DD8783C279A6 wds:Q73540307-A4D1F13D-0FBE-4612-9625-D0C66A4C1582 wds:Q73540307-A4DFC1CF-D7A6-4FD5-A9D7-496E84BF21D0 wds:Q73540307-A6F5EA43-AED9-4467-AB40-3B1AEE24E695 wds:Q73540307-AF266DDF-A938-440D-8E5A-ECAD5DE36DDE wds:Q73540307-B1E27C75-5C19-421F-87DF-BFC5D0218AE5 wds:Q73540307-B9F06CCA-AD28-4281-BCF2-210033108218 wds:Q73540307-DC6E0F2A-D095-47F2-A3E5-EAF64BC92687 wds:Q73540307-EA047328-FF90-4D0D-A7D4-BF97EC94C4B2 wds:Q73540307-EC9061CB-5635-43B8-B48D-AD34CC479BB2 wds:Q73540307-EFAFEF4A-83D3-45BF-A08D-BC5361E956CE wds:Q73540307-FE1C17E1-AE14-4F1C-BE2D-E350AFE6C5A1
cites work	Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex Apoptosis signaling by death receptors. Inhibition of caspase activity prevents CD95-mediated hepatic microvascular perfusion failure and restores Kupffer cell clearance capacity Cytofluorometric detection of mitochondrial alterations in early CD95/Fas/APO-1-triggered apoptosis of Jurkat T lymphoma cells. Comparison of seven mitochondrion-specific fluorochromes. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria Bax directly induces release of cytochrome c from isolated mitochondria Modulation of cell death by Bcl-XL through caspase interaction Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria The permeability transition pore complex: a target for apoptosis regulation by caspases and bcl-2-related proteins Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis Tumor suppressor p53 is a direct transcriptional activator of the human bax gene Apaf1 is required for mitochondrial pathways of apoptosis and brain development Mitochondria and apoptosis The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis p53 is required for radiation-induced apoptosis in mouse thymocytes FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex Two CD95 (APO-1/Fas) signaling pathways Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. Involvement of the CD95 (APO–1/Fas) receptor/ligand system in drug–induced apoptosis in leukemia cells Pro-caspase-3 is a major physiologic target of caspase-8. Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Differential requirement for caspase 9 in apoptotic pathways in vivo. Activation of the CD95 (APO-1/Fas) pathway in drug- and gamma-irradiation-induced apoptosis of brain tumor cells. Mitochondrial release of caspase-2 and -9 during the apoptotic process Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9

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