About: Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) im Jahr 1998 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Nature (en) наукова стаття, опублікована в Nature в січні 1998 (uk)
publication date	wds:Q59055150-C692306C-6F54-4C75-86E9-A0CE8413A101
publication date	1998-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59055150-3F23915D-A0E7-48DF-B342-E8F8424ADC08
language of work or name	English
exact match	wds:Q59055150-B692C40F-08FC-401F-A86A-476C73014080
exact match	https://scigraph.springernature.com/pub.10.1038/35160
cites work	wds:Q59055150-0E0F36F3-07F1-4007-A687-303E5335D7A6 wds:Q59055150-1F235D66-60C6-4135-8A0A-790782990D4A wds:Q59055150-7502ED0C-EEE6-494B-B320-1C4D57DCC10B wds:Q59055150-7D20013B-65E2-432C-8724-05F852209BF7 wds:Q59055150-86B3675C-0FF4-45A7-9A7F-D78947D53361 wds:Q59055150-8FEC7407-5D38-4EC8-93CD-A8C73FA26890 wds:Q59055150-94F59DAD-81DB-4165-BAC9-EAA732FCF872 wds:Q59055150-B6EF9C41-6791-4A60-9495-24933506FB81 wds:Q59055150-BA2016AF-CA7B-4646-9D51-1DD306B6C5E2 wds:Q59055150-C0FA16F9-89C6-44B3-AC82-0948C9EECD82 wds:Q59055150-C503FFD1-A09A-471C-A89A-F4D3F223A768 wds:Q59055150-D82D1EA8-33FE-4ADE-B449-81110D147D46
cites work	Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases The binding properties and biological activities of Bcl-2 and Bax in cells exposed to apoptotic stimuli The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis
author name string	wds:Q59055150-0B22CCCA-7A2D-4DDC-A5D9-C38C80A0459C wds:Q59055150-12AC47B3-0A63-4863-A25A-20BBE143EA91 wds:Q59055150-3B5E44FE-643E-400B-9F11-37E8D823AB9E wds:Q59055150-5CBB0BCA-F76A-4283-B5BA-8635D1169DF5 wds:Q59055150-9B189F7F-7565-43B9-89BE-41F064E8B2E9 wds:Q59055150-9CD2FA40-1B69-4B09-B059-822E42867F60 wds:Q59055150-A9B5F678-E9B8-4921-BD01-52A8FCC2C082 wds:Q59055150-D94BC25A-E899-40C4-A1EB-85CE8A018348
author name string	Borner C Jansen B Olivier R Fellay I Monney L Conus S Rossé T Rager M
rdfs:label	Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (en) Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (nl)
skos:prefLabel	Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (en) Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (nl)
name	Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (en) Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (nl)
title	wds:Q59055150-40461278-4C5D-44E3-9F00-63543EDA1AF0
title	Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c (en)
page(s)	wds:Q59055150-CA2CAC5F-D2F4-4617-8359-DAAAD1ACFED0
page(s)	496-499
instance of	wds:Q59055150-40367FE0-7258-48B1-8CA1-FB8496764389
instance of	scholarly article
PubMed ID	wds:Q59055150-6A6451F6-0984-41CF-94E2-1858A7628EE8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9461218
PubMed ID	9461218
published in	wds:Q59055150-DFC7B246-DAC4-4A65-87B2-1939297B5AF9
published in	Nature
issue	wds:Q59055150-AF683045-EB74-42C8-9268-946D0415A56F
volume	wds:Q59055150-A23726BE-5939-4188-8726-A231CD48A64E
issue	6666
volume	391
DOI	wds:Q59055150-17321489-1AC1-4E38-9749-3D0751FED932
DOI	http://dx.doi.org/10.1038/35160
DOI	10.1038/35160
Dimensions Publication ID	wds:Q59055150-DBA7D360-15BF-4596-981D-2FFFB35DE64C
Dimensions Publication ID	1028538597
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59055150
is cites work of	Adeno-associated virus vector-mediated bcl-2 gene transfer into post-ischemic gerbil brain in vivo: prospects for gene therapy of ischemia-induced neuronal death Bench-to-bedside review: Apoptosis/programmed cell death triggered by traumatic brain injury Scythe: a novel reaper-binding apoptotic regulator. Resensitization of breast cancer cells to anoikis by tropomyosin-1: role of Rho kinase-dependent cytoskeleton and adhesion Driving p53 response to Bax activation greatly enhances sensitivity to taxol by inducing massive apoptosis. Apogossypolone induces autophagy and apoptosis in breast cancer MCF-7 cells in vitro and in vivo Interleukin-7: physiological roles and mechanisms of action Loss of outer retinal neurons and circuitry alterations in the DBA/2J mouse Calphostin C-mediated translocation and integration of Bax into mitochondria induces cytochrome c release before mitochondrial dysfunction. Cif (Cytochrome c efflux-inducing factor) activity is regulated by Bcl-2 and caspases and correlates with the activation of Bid. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane STAT1-mediated down-regulation of Bcl-2 expression is involved in IFN-γ/TNF-α-induced apoptosis in NIT-1 cells Oncogene-dependent apoptosis is mediated by caspase-9. 15d-PGJ2 inhibits cell growth and induces apoptosis of MCG-803 human gastric cancer cell line Protective Effect of Procyanidin B2 against CCl4-Induced Acute Liver Injury in Mice. Ultrastructural localization of cytochrome c in apoptosis demonstrates mitochondrial heterogeneity. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria Differences in bcl-2- and bax-independent function in regulating apoptosis in sensory neuron populations p73 Induces apoptosis via PUMA transactivation and Bax mitochondrial translocation Solution structure of BID, an intracellular amplifier of apoptotic signaling

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