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

Characterization of an alternative BAK-binding site for BH3 peptides.

Nature communications - 3 Jul 2020

Ye Kaiqin, Meng Wei X, Sun Hongbin, Wu Bo, Chen Meng, Pang Yuan-Ping, Gao Jia, Wang Hongzhi, Wang Junfeng, Kaufmann Scott H, Dai Haiming

Abstract excerpt

Many cellular stresses are transduced into apoptotic signals through modification or up-regulation of the BH3-only subfamily of BCL2 proteins. Through direct or indirect mechanisms, these proteins activate BAK and BAX to permeabilize the mitochondrial outer membrane. While the BH3-only proteins BIM, PUMA, and tBID have been confirmed to directly activate BAK through its canonical BH3 binding groove, whether the...

Read the complete abstract on PubMed

Topics

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

Share to Apoptosis Regulatory Proteins
Share to bcl-2 Homologous Antagonist-Killer Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Jurkat Cells

Share to Magnetic Resonance Spectroscopy

Share to Mitochondrial Membranes

Share to Molecular Dynamics Simulation

Share to Protein Domains

Share to Proto-Oncogene Proteins c-bcl-2

Source

Open in PubMed Open full text

Identifiers

PMID: 32620849
DOI: 10.1038/s41467-020-17074-y
PMCID: PMC7335050

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of an alternative BAK-binding site for BH3 peptides.PMID 32620849Read ↗

BID-induced structural changes in BAK promote apoptosis.Semantic proximity Read ↗

BAX activation is initiated at a novel interaction site.Semantic proximity Read ↗

Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Semantic proximity Read ↗

Structural Details of BH3 Motifs and BH3-Mediated Interactions: an Updated PerspectiveSemantic proximity Read ↗

To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.Semantic proximity Read ↗

Inhibition of Pro-apoptotic BAX by a noncanonical interaction mechanism.Semantic proximity Read ↗

Binding modes of Bcl-2 homology 3 (BH3) peptides with anti-apoptotic protein A1 and redesign of peptide inhibitors: a computational study.Semantic proximity Read ↗

Binding affinity of pro-apoptotic BH3 peptides for the anti-apoptotic Mcl-1 and A1 proteins: Molecular dynamics simulations of Mcl-1 and A1 in complex with six different BH3 peptides.Semantic proximity Read ↗

Epistatic mutations in PUMA BH3 drive an alternate binding mode to potently and selectively inhibit anti-apoptotic Bfl-1.Semantic proximity Read ↗

Heterodimerization of BAK and MCL-1 activated by detergent micelles.Semantic proximity Read ↗

Relationship between helix stability and binding affinities: molecular dynamics simulations of Bfl-1/A1-binding pro-apoptotic BH3 peptide helices in explicit solvent.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 ↗

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