Evidence map›Paper›PMID 33106313›Full record

ArticleThe Journal of biological chemistry2020

Humanin selectively prevents the activation of pro-apoptotic protein BID by sequestering it into fibers.

Daniel L Morris, Sabrina Johnson, Christopher K E Bleck, Duck-Yeon Lee, Nico Tjandra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Daniel L MorrisLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland, USA.
Sabrina JohnsonLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland, USA.
Christopher K E BleckElectron Microscopy Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland, USA.
Duck-Yeon LeeBiochemistry Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland, USA.
Nico TjandraLaboratory of Molecular Biophysics, Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland, USA. Electronic address: tjandran@nhlbi.nih.gov.
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the B-cell lymphoma (BCL-2) protein family regulate mitochondrial outer membrane permeabilization (MOMP), a phenomenon in which mitochondria become porous and release death-propagating complexes during the early stages of apoptosis. Pro-apoptotic BCL-2 proteins oligomerize at the mitochondrial outer membrane during MOMP, inducing pore formation. Of current interest are endogenous factors that can inhibit pro-apoptotic BCL-2 mitochondrial outer membrane translocation and oligomerization. A mitochondrial-derived peptide, Humanin (HN), was reported being expressed from an alternate ORF in the mitochondrial genome and inhibiting apoptosis through interactions with the pro-apoptotic BCL-2 proteins. Specifically, it is known to complex with BAX and BID. We recently reported the fibrillation of HN and BAX into β-sheets. Here, we detail the fibrillation between HN and BID. These fibers were characterized using several spectroscopic techniques, protease fragmentation with mass analysis, and EM. Enhanced fibrillation rates were detected with rising temperatures or pH values and the presence of a detergent. BID fibers are similar to those produced using BAX; however, the structures differ in final conformations of the BCL-2 proteins. BID fibers display both types of secondary structure in the fiber, whereas BAX was converted entirely to β-sheets. The data show that two distinct segments of BID are incorporated into the fiber structure, whereas other portions of BID remain solvent-exposed and retain helical structure. Similar analyses show that anti-apoptotic BCL-x

Indexed as

Amino Acid Sequencebcl-2-Associated X Proteinbcl-X ProteinBH3 Interacting Domain Death Agonist ProteinHumansIntracellular Signaling Peptides and ProteinsMitochondrial MembranesMutationProtein ConformationProto-Oncogene Proteins c-bcl-2BAX protein, humanbcl-2-Associated X ProteinBCL2L1 protein, humanBCL2 protein, humanbcl-X ProteinBH3 Interacting Domain Death Agonist ProteinBID protein, humanhumaninIntracellular Signaling Peptides and ProteinsProto-Oncogene Proteins c-bcl-2amyloidapoptosisB-cell lymphoma 2 (Bcl-2) familyBIDconformational changeelectron microscopy (EM)fibershumaninβ-sheet

Identifiers

PMID33106313
PMCPMC11843584
OpenAlexW3094023614

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.