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-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.

Cell death and differentiation - 1 Sept 2001

Lindenboim L, Borner C, Stein R

Abstract excerpt

Proteins of the Bcl-2 family regulate apoptosis, some antagonizing cell death and others, such as Bcl-x(S), promoting it. We previously showed that expression of Bcl-x(S) in PC12 cells is a useful system for studying the mechanism of Bcl-x(S)-induced apoptosis. To further investigate this apoptotic effect and its prevention by anti-apoptotic agents, we assessed the role of distinct Bcl-x(S) domains, via the study...

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 Dimerization

Share to Nerve Growth Factor

Share to PC12 Cells

Share to Precipitin Tests

Share to Protein Structure, Quaternary

Share to Proto-Oncogene Proteins c-bcl-2

Source

Identifiers

PMID: 11526448
DOI: 10.1038/sj.cdd.4400888

Genes

NGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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.PMID 11526448Read ↗

The BH3 domain of Bcl-x(S) is required for inhibition of the antiapoptotic function of Bcl-x(L).Semantic proximity Read ↗

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

Characterization of the anti-apoptotic mechanism of Bcl-B.Semantic proximity Read ↗

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

Unknotting the roles of Bcl-2 and Bcl-xL in cell deathSemantic proximity Read ↗

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

Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers.Semantic proximity Read ↗

Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak.Semantic proximity Read ↗

Bcl-xS and Bax induce different apoptotic pathways in PC12 cellsSemantic proximity Read ↗

Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2.Semantic proximity Read ↗

Selective regulation of IP3-receptor-mediated Ca2+ signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl.Semantic proximity Read ↗

Subcellular localization and physiological consequences of introducing a mitochondrial matrix targeting signal sequence in bax and its mutants.Semantic proximity Read ↗

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