Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Bcl-xL inhibits cytochrome c release but not mitochondrial depolarization during the activation of multiple death pathways by tumor necrosis factor-alpha.

The Journal of biological chemistry - 6 Oct 2000

Johnson B W, Cepero E, Boise L H

Abstract excerpt

Cells can respond differently to anti-CD95 antibody treatment. Type I cells show strong activation of caspase-8 and directly activate caspase-3. Type II cells weakly activate caspase-8 and must amplify their death signal through the mitochondria. These cells can be rescued by Bcl-x(L). Here we show that tumor necrosis factor-alpha induces both Type I and II pathways, which can be inhibited by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Chloromethyl Ketones
Share to bcl-X Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Caspase 8

Share to Caspase 9

Share to Caspase Inhibitors

Share to Cytochrome c Group

Share to Enzyme Precursors

Share to Serpins

Source

Identifiers

PMID: 10913120
DOI: 10.1074/jbc.M001363200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bcl-xL inhibits cytochrome c release but not mitochondrial depolarization during the activation of multiple death pathways by tumor necrosis factor-alpha.PMID 10913120Read ↗

Bcl-x(S) can form homodimers and heterodimers and its apoptotic activity requires localization of Bcl-x(S) to the mitochondria and its BH3 and loop domains.Semantic proximity Read ↗

Inhibition of caspase activity induces a switch from apoptosis to necrosisSemantic proximity Read ↗

Differential regulation of apoptosis in AK-5 tumor cells by the proto-oncogene Bcl-2: presence of Bcl-2 dependent and independent pathways.Semantic proximity Read ↗

The Bcl-xL and Bax-<FONT FACE = "SYMBOL">a</FONT> control points: modulation of apoptosis induced by cancer chemotherapy and relation to TPCK-sensitive protease and caspase activationSemantic proximity Read ↗

Vesicular Stomatitis Virus Induces Apoptosis Primarily through Bak Rather than Bax by Inactivating Mcl-1 and Bcl-X LSemantic proximity Read ↗

Bax activation by engagement with, then release from, the BH3 binding site of Bcl-xL.Semantic proximity Read ↗

Cell type specific involvement of death receptor and mitochondrial pathways in drug-induced apoptosis.Semantic proximity Read ↗

Conversion of Bcl-2 to a Bax-like death effector by caspases.Semantic proximity Read ↗

Modulation of cell death by Bcl-XL through caspase interaction.Semantic proximity Read ↗

2-Methoxy antimycin reveals a unique mechanism for Bcl-x(L) inhibition.Semantic proximity Read ↗

Distinct domains of Bcl-XL are involved in Bax and Bad antagonism and in apoptosis inhibition.Semantic proximity Read ↗

Bcl-x(S) anatagonizes the protective effects of Bcl-x(L).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.