Evidence map›Paper›PMID 38001371›Full record

ArticleCell stress & chaperones2023

Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.

Milene N O Moritz, Paulo R Dores-Silva, Amanda L S Coto, Heloísa S Selistre-de-Araújo, Andrei Leitão, David M Cauvi, Antonio De Maio, Serena Carra, Júlio Cesar Borges

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell stress & chaperones, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 68% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 3 institutions in 5 countries.

Milene N O Moritz *São Carlos Institute of Chemistry, University of São Paulo - USP, P.O. Box 780, São Carlos, SP, 13560-970, Brazil.
Paulo R Dores-Silva *São Carlos Institute of Chemistry, University of São Paulo - USP, P.O. Box 780, São Carlos, SP, 13560-970, Brazil.
Amanda L S Coto *São Carlos Institute of Chemistry, University of São Paulo - USP, P.O. Box 780, São Carlos, SP, 13560-970, Brazil.
Heloísa S Selistre-de-AraújoDepartment of Physiological Sciences, Federal University of São Carlos, São Carlos, SP, Brazil.
Andrei LeitãoSão Carlos Institute of Chemistry, University of São Paulo - USP, P.O. Box 780, São Carlos, SP, 13560-970, Brazil.
David M CauviDivision of Trauma, Critical Care, Burns and Acute Care Surgery, Department of Surgery, School of Medicine, University of California San Diego, La Jolla, CA, 92093, USA.
Antonio De MaioDivision of Trauma, Critical Care, Burns and Acute Care Surgery, Department of Surgery, School of Medicine, University of California San Diego, La Jolla, CA, 92093, USA.
Serena CarraCentre for Neuroscience and Nanotechnology, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Júlio Cesar BorgesSão Carlos Institute of Chemistry, University of São Paulo - USP, P.O. Box 780, São Carlos, SP, 13560-970, Brazil. borgesjc@iqsc.usp.br.ORCID 0000-0003-4856-748X
Universidade Federal de São Carlos · BRUniversity of California San Diego · USUniversity of Modena and Reggio Emilia · IT

Funding

Contribution of Cholesterol Homeostasis for Injury ResolutionR01GM114473 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 2015 to 2018
$1.2M
Heat Shock Proteins and the Stress Observation SystemR01GM098455 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 2012 to 2015
$1.1M
NIGMS NIH HHS R01 GM098455NIGMS NIH HHS R01 GM114473NIH HHS R01 GM098455-04NIH HHS R01 GM114473-01
6 · The paper itself

Abstract

Human Hsp70-escort protein 1 (hHep1) is a cochaperone that assists in the function and stability of mitochondrial HSPA9. Similar to HSPA9, hHep1 is located outside the mitochondria and can interact with liposomes. In this study, we further investigated the structural and thermodynamic behavior of interactions between hHep1 and negatively charged liposomes, as well as interactions with cellular membranes. Our results showed that hHep1 interacts peripherally with liposomes formed by phosphatidylserine and cardiolipin and remains partially structured, exhibiting similar affinities for both. In addition, after being added to the cell membrane, recombinant hHep1 was incorporated by cells in a dose-dependent manner. Interestingly, the association of HSPA9 with hHep1 improved the incorporation of these proteins into the lipid bilayer. These results demonstrated that hHep1 can interact with lipids also present in the plasma membrane, indicating roles for this cochaperone outside of mitochondria.

Indexed as

Lipid BilayersLiposomesCell MembraneHumansMitochondriaMolecular ChaperonesDNLZ protein, humanLipid BilayersLiposomesMolecular ChaperonesCochaperoneHeat ShockHSP70sLiposomes and plasma membrane

Identifiers

PMID38001371
PMCPMC10746634
OpenAlexW4388990973

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.