Evidence map›Paper›PMID 29203715›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018

The role of heat shock proteins and co-chaperones in heart failure.

Mark J Ranek, Marisa J Stachowski, Jonathan A Kirk, Monte S Willis

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed, 1 pooled it
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

78 citing papers in PubMed, 1 synthesis or guideline pooled it, 118 citations in OpenAlex.

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18 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Mark J RanekDivision of Cardiology, Department of Medicine, Johns Hopkins Medical Institutions, Baltimore, MD 21205, USA.ORCID http://orcid.org/0000-0002-4970-8988
Marisa J StachowskiDepartment of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University, Chicago, IL 60302, USA.
Jonathan A KirkDepartment of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University, Chicago, IL 60302, USA.ORCID http://orcid.org/0000-0002-5192-2860
Monte S WillisDepartment of Pathology and Laboratory Medicine, McAllister Heart Institute, CB#7525, Chapel Hill, NC 27599-7525, USA monte_willis@med.unc.edu.ORCID http://orcid.org/0000-0002-0769-5816
Loyola University Chicago · USJohns Hopkins University · US

Funding

GSK-3β Localizes to the Myofilament and Modifies its Function in Ischemic CardiomyopathyR01HL136737 · NHLBI · UNIVERSITY OF CHICAGO · PI JONATHAN A KIRK · 2017 to 2026
$4.5M
Myocyte specific regulation of metabolism and the response to biomechanical forceR01HL104129 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WILLIS, MONTE S · 2010 to 2018
$3.3M
American Heart Association-American Stroke Association 14SDG20380148NHLBI NIH HHS R01 HL104129NHLBI NIH HHS R01 HL136737
6 · The paper itself

Abstract

The ongoing contractile and metabolic demands of the heart require a tight control over protein quality control, including the maintenance of protein folding, turnover and synthesis. In heart disease, increases in mechanical and oxidative stresses, post-translational modifications (e.g., phosphorylation), for example, decrease protein stability to favour misfolding in myocardial infarction, heart failure or ageing. These misfolded proteins are toxic to cardiomyocytes, directly contributing to the common accumulation found in human heart failure. One of the critical class of proteins involved in protecting the heart against these threats are molecular chaperones, including the heat shock protein70 (HSP70), HSP90 and co-chaperones CHIP (carboxy terminus of Hsp70-interacting protein, encoded by the

Indexed as

AnimalsHeart FailureHeat-Shock ProteinsHumansMiceMolecular ChaperonesMyocytes, CardiacRatsHeat-Shock ProteinsMolecular ChaperonesBAG-3carboxy terminus of HSP70-interacting proteinheart failureHSP70HSP90Stub1

Identifiers

PMID29203715
PMCPMC5717530
OpenAlexW2774870330

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.