Evidence map›Paper›PMID 32581848›Full record

ReviewFrontiers in physiology2020

Come Together: Protein Assemblies, Aggregates and the Sarcostat at the Heart of Cardiac Myocyte Homeostasis.

Moydul Islam, Abhinav Diwan, Kartik Mani

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
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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

3 authors at 1 institution in 1 country.

Moydul IslamDivision of Cardiology, Washington University School of Medicine, St. Louis, MO, United States.
Abhinav DiwanDivision of Cardiology, Washington University School of Medicine, St. Louis, MO, United States.
Kartik ManiDivision of Cardiology, Washington University School of Medicine, St. Louis, MO, United States.
Washington University in St. Louis · US

Funding

ROLE OF AUTOPHAGIC FLUX IN CARDIAC MYOCYTE VIABILITYR01HL107594 · NHLBI · WASHINGTON UNIVERSITY · PI Abhinav Diwan · 2011 to 2026
$5.9M
Maternal obesity and cardiometabolic health in the offspringR01HL143431 · NHLBI · WASHINGTON UNIVERSITY · PI DIWAN, ABHINAV · 2018 to 2021
$2.5M
Targeting Macrophage Lysosome Biogenesis Program in Cardiomyopathy and Heart FailureI01BX004235 · VA · ST. LOUIS VA MEDICAL CENTER · PI DIWAN, ABHINAV · 2018 to 2021
–
BLRD VA I01 BX004235NHLBI NIH HHS R01 HL107594NHLBI NIH HHS R01 HL143431
6 · The paper itself

Abstract

Homeostasis in vertebrate systems is contingent on normal cardiac function. This, in turn, depends on intricate protein-based cellular machinery, both for contractile function, as well as, durability of cardiac myocytes. The cardiac small heat shock protein (csHsp) chaperone system, highlighted by αB-crystallin (CRYAB), a small heat shock protein (sHsp) that forms ∼3-5% of total cardiac mass, plays critical roles in maintaining proteostatic function via formation of self-assembled multimeric chaperones. In this work, we review these ancient proteins, from the evolutionarily preserved role of homologs in protists, fungi and invertebrate systems, as well as, the role of sHsps and chaperones in maintaining cardiac myocyte structure and function. We propose the concept of the "sarcostat" as a protein quality control mechanism in the sarcomere. The roles of the proteasomal and lysosomal proteostatic network, as well as, the roles of the aggresome, self-assembling protein complexes and protein aggregation are discussed in the context of cardiac myocyte homeostasis. Finally, we will review the potential for targeting the csHsp system as a novel therapeutic approach to prevent and treat cardiomyopathy and heart failure.

Indexed as

aggregatesautophagyheat shock proteinslysosomeubiquitin 26S-proteasome system

Identifiers

PMID32581848
PMCPMC7287178
OpenAlexW3032947922

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.