Evidence map›Paper›PMID 24904158›Full record

ArticleScience (New York, N.Y.)2014

Structural basis for a pH-sensitive calcium leak across membranes.

Yanqi Chang, Renato Bruni, Brian Kloss, Zahra Assur, Edda Kloppmann, Burkhard Rost, Wayne A Hendrickson, Qun Liu

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 100 citations in OpenAlex.

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  20. TheJournal of bacteriology · 2022
    Article
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

8 authors at 2 institutions in 1 country.

Yanqi ChangNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA.
Renato BruniNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA.
Brian KlossNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA.
Zahra AssurDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.
Edda KloppmannNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA. Department of Bioinformatics and Computational Biology, Fakultät für Informatik, Technische Universität München, Garching, Germany.
Burkhard RostNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA. Department of Bioinformatics and Computational Biology, Fakultät für Informatik, Technische Universität München, Garching, Germany.
Wayne A HendricksonNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA. Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA. New York Structural Biology Center, National Synchrotron Light Source (NSLS) X4, Brookhaven National Laboratory, Upton, NY 11973, USA. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Qun LiuNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA. New York Structural Biology Center, National Synchrotron Light Source (NSLS) X4, Brookhaven National Laboratory, Upton, NY 11973, USA. qunliu@bnl.gov.
New York Structural Biology Center · USColumbia University · US

Funding

Structural Genomics on Membrane ProteinsU54GM095315 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ROST, BURKHARD · 2010 to 2014
$15.2M
Proposal for an Administrative Supplement for Equipment Purchases for NIGMS Awardees NOT-GM-18-022R01GM107462 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI HENDRICKSON, WAYNE A. · 2014 to 2021
$3.6M
NIGMS NIH HHS GM095315NIGMS NIH HHS GM107462NIGMS NIH HHS R01 GM107462NIGMS NIH HHS U54 GM095315
6 · The paper itself

Abstract

Calcium homeostasis balances passive calcium leak and active calcium uptake. Human Bax inhibitor-1 (hBI-1) is an antiapoptotic protein that mediates a calcium leak and is representative of a highly conserved and widely distributed family, the transmembrane Bax inhibitor motif (TMBIM) proteins. Here, we present crystal structures of a bacterial homolog and characterize its calcium leak activity. The structure has a seven-transmembrane-helix fold that features two triple-helix sandwiches wrapped around a central C-terminal helix. Structures obtained in closed and open conformations are reversibly interconvertible by change of pH. A hydrogen-bonded, pKa (where Ka is the acid dissociation constant)-perturbed pair of conserved aspartate residues explains the pH dependence of this transition, and biochemical studies show that pH regulates calcium influx in proteoliposomes. Homology models for hBI-1 provide insights into TMBIM-mediated calcium leak and cytoprotective activity.

Indexed as

Bacillus subtilisBacterial ProteinsCalciumCell MembraneCrystallography, X-RayHumansHydrogen-Ion ConcentrationMembrane ProteinsModels, MolecularProtein Structure, SecondaryBacterial ProteinsCalciumMembrane Proteins

Identifiers

PMID24904158
PMCPMC4119810
OpenAlexW2037500108

What OpenQuestion holds

Textmetadata
LicenceTDM
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.