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) anatagonizes the protective effects of Bcl-x(L).

The Journal of biological chemistry - 15 Mar 1996

Minn A J, Boise L H, Thompson C B

Abstract excerpt

Bcl-x, a member of the Bcl-2 family, has two alternatively spliced forms, Bcl-x(L) and Bcl-x(S). Bcl-x(L), like Bcl-2, is able to protect cells from a wide variety of apoptotic stimuli. Bcl-x(S), as a result of alternative splicing, lacks 63 amino acids that comprise the region of greatest amino...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to DNA Primers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Phenotype

Share to Proto-Oncogene Proteins

Share to Transfection

Source

Identifiers

PMID: 8626425
DOI: 10.1074/jbc.271.11.6306

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8626425-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bcl-x(S) anatagonizes the protective effects of Bcl-x(L).PMID 8626425Read ↗

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 ↗

Antiapoptotic potency of Bcl-2 proteins primarily relies on their stability, not binding selectivitySemantic proximity Read ↗

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 ↗

Non-apoptotic functions of BCL-2 family proteinsSemantic proximity Read ↗

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapySemantic proximity Read ↗

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

The Bcl-2 family: roles in cell survival and oncogenesisSemantic proximity Read ↗

BCL-2 family proteins: regulators of cell death involved in the pathogenesis of cancer and resistance to therapy.Semantic proximity Read ↗

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

BCL-2 family proteins: Regulators of cell death involved in the pathogenesis of cancer and resistance to therapySemantic proximity Read ↗

Bcl-B, a Novel Bcl-2 Family Member That Differentially Binds and Regulates Bax and BakSemantic proximity Read ↗

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