Evidence map›Paper›PMID 25791537›Full record

ArticleScientific reports2015

Functional diversification and specialization of cytosolic 70-kDa heat shock proteins.

Chelsea McCallister, Matthew C Siracusa, Farzaneh Shirazi, Dimitra Chalkia, Nikolas Nikolaidis

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

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  11. Origin and Evolution of the Human Bcl2-Associated Athanogene-1 (BAG-1).International journal of molecular sciences · 2020
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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 2 institutions in 1 country.

Chelsea McCallisterDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University, Fullerton, Fullerton, CA 92834.
Matthew C SiracusaDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University, Fullerton, Fullerton, CA 92834.
Farzaneh ShiraziDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University, Fullerton, Fullerton, CA 92834.
Dimitra ChalkiaCenter for Mitochondrial and Epigenomic Medicine, The Children's Hospital of Philadelphia Research Institute, Philadelphia, PA.
Nikolas NikolaidisDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University, Fullerton, Fullerton, CA 92834.
California State University, Fullerton · USChildren's Hospital of Philadelphia · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

A fundamental question in molecular evolution is how protein functional differentiation alters the ability of cells and organisms to cope with stress and survive. To answer this question we used two paralogous Hsp70s from mouse and explored whether these highly similar cytosolic molecular chaperones, which apart their temporal expression have been considered functionally interchangeable, are differentiated with respect to their lipid-binding function. We demonstrate that the two proteins bind to diverse lipids with different affinities and therefore are functionally specialized. The observed lipid-binding patterns may be related with the ability of both Hsp70s to induce cell death by binding to a particular plasma-membrane lipid, and the potential of only one of them to promote cell survival by binding to a specific lysosomal-membrane lipid. These observations reveal that two seemingly identical proteins differentially modulate cellular adaptation and survival by having acquired specialized functions via sequence divergence. Therefore, this study provides an evolutionary paradigm, where promiscuity, specificity, sub- and neo-functionalization orchestrate one of the most conserved systems in nature, the cellular stress-response.

Indexed as

Amino Acid SequenceAnimalsCytosolHeat-Shock ProteinsMiceMolecular Sequence DataPhylogenySequence Homology, Amino AcidHeat-Shock Proteins

Identifiers

PMID25791537
PMCPMC4366816
OpenAlexW2036109896

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.