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

Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: a link between the apoptosome and the proteasome pathway.

The Journal of experimental medicine - 7 Jun 1999

Dimmeler S, Breitschopf K, Haendeler J, Zeiher A M

Abstract excerpt

Injury of the endothelial cells by the induction of apoptotic cell death may play an important role in the pathophysiology of atherosclerosis and the progression of inflammatory diseases. Here, we demonstrate an essential role for the ubiquitin-dependent proteasome complex in stimulus-induced degradation of the antiapoptotic protein Bcl-2. Bcl-2 is specifically degraded after stimulation of human endothelial...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Calmodulin-Dependent Protein Kinases
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endothelium, Vascular

Share to Genes, bcl-2

Share to Multienzyme Complexes

Share to Proto-Oncogene Proteins c-bcl-2

Share to Staurosporine

Share to Ubiquitins

Source

Open in PubMed Open full text

Identifiers

PMID: 10359585
DOI: 10.1084/jem.189.11.1815
PMCID: PMC2193081

Genes

TNF

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

Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: a link between the apoptosome and the proteasome pathway.PMID 10359585Read ↗

Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway.Semantic proximity Read ↗

S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis.Semantic proximity Read ↗

On to the road to degradation: atherosclerosis and the proteasome.Semantic proximity Read ↗

xIAP induces cell-cycle arrest and activates nuclear factor-kappaB : new survival pathways disabled by caspase-mediated cleavage during apoptosis of human endothelial cells.Semantic proximity Read ↗

Transcription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cells.Semantic proximity Read ↗

UGP2, a novel target gene of TP53, inhibits endothelial cells apoptosis and atherosclerosisSemantic proximity Read ↗

Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection.Semantic proximity Read ↗

Pericytes promote endothelial cell survival through induction of autocrine VEGF-A signaling and Bcl-w expressionSemantic proximity Read ↗

Cloning of human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cellsSemantic proximity Read ↗

"Loop" domain is necessary for taxol-induced mobility shift and phosphorylation of Bcl-2 as well as for inhibiting taxol-induced cytosolic accumulation of cytochrome c and apoptosis.Semantic proximity Read ↗

SerpinB2 protection of retinoblastoma protein from calpain enhances tumor cell survival.Semantic proximity Read ↗

Bcl-2 Is a Key Factor for Cardiac Fibroblast Resistance to Programmed Cell DeathSemantic proximity Read ↗

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