Evidence map›Paper›PMID 31690630›Full record

ArticleThe Journal of biological chemistry2019

Humanin induces conformational changes in the apoptosis regulator BAX and sequesters it into fibers, preventing mitochondrial outer-membrane permeabilization.

Daniel L Morris, David W Kastner, Sabrina Johnson, Marie-Paule Strub, Yi He, Christopher K E Bleck, Duck-Yeon Lee, Nico Tjandra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.2field-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

20 citing papers in PubMed, 38 citations in OpenAlex.

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  16. Membrane-dependent amyloid aggregation of human BAX α9 (173-192).Protein science : a publication of the Protein Society · 2021
    Article
  17. Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021
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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

8 authors at 1 institution in 1 country.

Daniel L MorrisLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.ORCID 0000-0001-5274-0172
David W KastnerLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.ORCID 0000-0002-7766-4249
Sabrina JohnsonLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.
Marie-Paule StrubLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.
Yi HeLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.
Christopher K E BleckElectron Microscopy Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.ORCID 0000-0003-1029-3444
Duck-Yeon LeeBiochemistry Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland 20814.
Nico TjandraLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20814 tjandran@nhlbi.nih.gov.ORCID 0000-0001-6365-5811
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial, or intrinsic, apoptosis pathway is regulated mainly by members of the B-cell lymphoma 2 (BCL-2) protein family. BCL-2-associated X apoptosis regulator (BAX) plays a pivotal role in the initiation of mitochondria-mediated apoptosis as one of the factors causing mitochondrial outer-membrane permeabilization (MOMP). Of current interest are endogenous BAX ligands that inhibit its MOMP activity. Mitochondrial-derived peptides (MDPs) are a recently identified class of mitochondrial retrograde signaling molecules and are reported to be potent apoptosis inhibitors. Among them, humanin (HN) has been shown to suppress apoptosis by inhibiting BAX translocation to the mitochondrial outer membrane, but the molecular mechanism of this interaction is unknown. Here, using recombinant protein expression, along with light-scattering, CD, and fluorescence spectroscopy, we report that HN and BAX can form fibers together

Indexed as

Apoptosisbcl-2-Associated X ProteinCell Membrane PermeabilityHumansIntracellular Signaling Peptides and ProteinsMitochondrial MembranesMutationPeptidesProtein ConformationBAX protein, humanbcl-2-Associated X ProteinhumaninIntracellular Signaling Peptides and ProteinsPeptidesapoptosisBaxB-cell lymphoma 2 (Bcl-2) familyBCL-2-associated X apoptosis regulator (BAX)conformational changeelectron microscopyfibersfibrilfibrillationhumaninmitochondrial apoptosisprotein aggregationβ-sheet

Identifiers

PMID31690630
PMCPMC6916494
OpenAlexW2987197801

What OpenQuestion holds

Textmetadata
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.