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

Development of a high-throughput fluorescence polarization assay for Bcl-x(L).

Analytical biochemistry - 1 Aug 2002

Zhang Haichao, Nimmer Paul, Rosenberg Saul H, Ng Shi-Chung, Joseph Mary

Abstract excerpt

Antiapoptotic protein Bcl-x(L) has been demonstrated to play a very important role in a variety of diseases such as cancer. Its biological function can be inhibited by proapoptotic proteins such Bak, Bad, and Bax by forming complexes mediated primarily by the Bcl-2 homology 3 (BH3) domain. To facilitate drug discovery for Bcl-x(L) inhibitors, we have developed and optimized a fluorescence polarization assay based...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to bcl-2-Associated X Protein
Share to bcl-Associated Death Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to bcl-X Protein

Share to Fluorescence Polarization

Share to Fluorescent Dyes

Share to Peptide Fragments

Share to Proto-Oncogene Proteins c-bcl-2

Source

Identifiers

PMID: 12137781
DOI: 10.1016/s0003-2697(02)00028-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Development of a high-throughput fluorescence polarization assay for Bcl-x(L).PMID 12137781Read ↗

Structure-activity relationships of Bak derived peptides: affinity and specificity modulations by amino acid replacement.Semantic proximity Read ↗

Structure-activity relationship studies of phenanthridine-based Bcl-XL inhibitors.Semantic proximity Read ↗

Rational Design and Real Time, In-Cell Detection of the Proapoptotic Activity of a Novel Compound Targeting Bcl-XLSemantic proximity Read ↗

Discovery of high affinity and specificity stapled peptide Bcl-xL inhibitors using bacterial surface displaySemantic proximity Read ↗

Efficacy and specificity of inhibitors of BCL-2 family protein interactions assessed by affinity measurements in live cellsSemantic proximity Read ↗

Structure-based redesign of the binding specificity of anti-apoptotic Bcl-x(L).Semantic proximity Read ↗

Conformational changes in Bcl-2 pro-survival proteins determine their capacity to bind ligands.Semantic proximity Read ↗

Interactions of pro-apoptotic BH3 proteins with anti-apoptotic Bcl-2 family proteins measured in live MCF-7 cells using FLIM FRET.Semantic proximity Read ↗

Molecular dynamics simulations of pro-apoptotic BH3 peptide helices in aqueous medium: relationship between helix stability and their binding affinities to the anti-apoptotic protein Bcl-X(L).Semantic proximity Read ↗

Sequence and helicity requirements for the proapoptotic activity of Bax BH3 peptides.Semantic proximity Read ↗

Apogossypol derivatives as antagonists of antiapoptotic Bcl-2 family proteinsSemantic proximity Read ↗

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

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