Evidence map›Paper›PMID 27381287›Full record

ArticleScientific reports2016

Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore Formation.

Chenyi Liao, Zhi Zhang, Justin Kale, David W Andrews, Jialing Lin, Jianing Li

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  6. Concerted Rolling and Penetration of Peptides during Membrane Binding.Journal of chemical theory and computation · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 5 institutions in 2 countries.

Chenyi LiaoDepartment of Chemistry, University of Vermont, Burlington, VT 05405, USA.
Zhi ZhangDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73126, USA.
Justin KaleBiological Sciences, Sunnybrook Research Institute, University of Toronto, Toronto, ON, Canada.
David W AndrewsBiological Sciences, Sunnybrook Research Institute, University of Toronto, Toronto, ON, Canada.
Jialing LinDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73126, USA.
Jianing LiDepartment of Chemistry, University of Vermont, Burlington, VT 05405, USA.
University of Vermont · USOklahoma State University Oklahoma City · USSunnybrook Health Science Centre · CAUniversity of Oklahoma Health Sciences Center · USUniversity of Toronto · CA

Funding

Structure-Function of Bcl-2 Related Apoptosis Regulators in MembranesR01GM062964 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI LIN, JIALING · 2001 to 2014
$3.3M
CIHRNIGMS NIH HHS R01 GM062964
6 · The paper itself

Abstract

Helix α9 of Bax protein can dimerize in the mitochondrial outer membrane (MOM) and lead to apoptotic pores. However, it remains unclear how different conformations of the dimer contribute to the pore formation on the molecular level. Thus we have investigated various conformational states of the α9 dimer in a MOM model - using computer simulations supplemented with site-specific mutagenesis and crosslinking of the α9 helices. Our data not only confirmed the critical membrane environment for the α9 stability and dimerization, but also revealed the distinct lipid-binding preference of the dimer in different conformational states. In our proposed pathway, a crucial iso-parallel dimer that mediates the conformational transition was discovered computationally and validated experimentally. The corroborating evidence from simulations and experiments suggests that, helix α9 assists Bax activation via the dimer heterogeneity and interactions with specific MOM lipids, which eventually facilitate proteolipidic pore formation in apoptosis regulation.

Indexed as

ApoptosisAmino Acid Motifsbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinComputer SimulationDisulfidesHumansLipidsMitochondriaMitochondrial MembranesMolecular Dynamics SimulationProtein MultimerizationProtein Structure, SecondaryBAK1 protein, humanBAX protein, humanbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinDisulfidesLipids

Identifiers

PMID27381287
PMCPMC4933972
OpenAlexW2466606494

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.