Evidence map›Paper›PMID 29190034›Full record

ReviewCell stress & chaperones2018

The role of αB-crystallin in skeletal and cardiac muscle tissues.

Ivan Dimauro, Ambra Antonioni, Neri Mercatelli, Daniela Caporossi

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell stress & chaperones, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

46 citing papers in PubMed, 81 citations in OpenAlex.

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  16. Human MutatedInternational journal of molecular sciences · 2023
    Article
  17. Review
  18. Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

4 authors at 1 institution in 1 country.

Ivan DimauroDepartment of Movement, Human and Health Sciences, University of Rome "Foro Italico", Rome, Italy. ivan.dimauro@uniroma4.it.ORCID http://orcid.org/0000-0003-0577-3144
Ambra AntonioniDepartment of Movement, Human and Health Sciences, University of Rome "Foro Italico", Rome, Italy.
Neri MercatelliDepartment of Movement, Human and Health Sciences, University of Rome "Foro Italico", Rome, Italy.
Daniela CaporossiDepartment of Movement, Human and Health Sciences, University of Rome "Foro Italico", Rome, Italy. daniela.caporossi@uniroma4.it.
Foro Italico University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

All organisms and cells respond to various stress conditions such as environmental, metabolic, or pathophysiological stress by generally upregulating, among others, the expression and/or activation of a group of proteins called heat shock proteins (HSPs). Among the HSPs, special attention has been devoted to the mutations affecting the function of the αB-crystallin (HSPB5), a small heat shock protein (sHsp) playing a critical role in the modulation of several cellular processes related to survival and stress recovery, such as protein degradation, cytoskeletal stabilization, and apoptosis. Because of the emerging role in general health and disease conditions, the main objective of this mini-review is to provide a brief account on the role of HSPB5 in mammalian muscle physiopathology. Here, we report the current known state of the regulation and localization of HSPB5 in skeletal and cardiac tissue, making also a critical summary of all human HSPB5 mutations known to be strictly associated to specific skeletal and cardiac diseases, such as desmin-related myopathies (DRM), dilated (DCM) and restrictive (RCM) cardiomyopathy. Finally, pointing to putative strategies for HSPB5-based therapy to prevent or counteract these forms of human muscular disorders.

Indexed as

alpha-Crystallin B ChainAnimalsAutophagyHumansMuscle, SkeletalMyocardiumOxidation-ReductionProteasome Endopeptidase Complexalpha-Crystallin B ChainProteasome Endopeptidase ComplexChaperonesCrystallinopathiesDiseaseHeat shock proteinsPhysical activity

Identifiers

PMID29190034
PMCPMC6045558
OpenAlexW2775276675

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.