Evidence map›Paper›PMID 34777614›Full record

ReviewBiophysical reviews2021

Striated muscle proteins are regulated both by mechanical deformation and by chemical post-translational modification.

Christopher Solís, Brenda Russell

Open access · greenAbstract readReview
In one paragraph

Review in Biophysical reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Cardiac CapZ Regulation During Acute Exercise in Female Mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  3. The role of mechanosignaling in the control of myocardial mass.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Role of Muscle LIM Protein in Mechanotransduction Process.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Article
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

2 authors at 1 institution in 1 country.

Christopher SolísDepartment of Physiology and Biophysics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612 USA.ORCID https://orcid.org/0000-0003-4584-7363
Brenda RussellDepartment of Physiology and Biophysics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612 USA.ORCID 0000-0002-4847-5836
University of Illinois Chicago · US

Funding

Sarcomeric Modifications and Progressive Cardiac MaladaptationP01HL062426 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI DE TOMBE, PIETER P. · 2000 to 2020
$42.4M
Post-translational mechanisms of cardiac adaptation during unloadingR00HL151825 · NHLBI · FLORIDA STATE UNIVERSITY · PI SOLIS OCAMPO, CHRISTOPHER · 2023 to 2025
$747k
Post-translational mechanisms of cardiac adaptation during unloadingK99HL151825 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLIS OCAMPO, CHRISTOPHER · 2020 to 2021
$210k
NHLBI NIH HHS K99 HL151825NHLBI NIH HHS P01 HL062426NHLBI NIH HHS R00 HL151825
6 · The paper itself

Abstract

All cells sense force and build their cytoskeleton to optimize function. How is this achieved? Two major systems are involved. The first is that load deforms specific protein structures in a proportional and orientation-dependent manner. The second is post-translational modification of proteins as a consequence of signaling pathway activation. These two processes work together in a complex way so that local subcellular assembly as well as overall cell function are controlled. This review discusses many cell types but focuses on striated muscle. Detailed information is provided on how load deforms the structure of proteins in the focal adhesions and filaments, using α-actinin, vinculin, talin, focal adhesion kinase, LIM domain-containing proteins, filamin, myosin, titin, and telethonin as examples. Second messenger signals arising from external triggers are distributed throughout the cell causing post-translational or chemical modifications of protein structures, with the actin capping protein CapZ and troponin as examples. There are numerous unanswered questions of how mechanical and chemical signals are integrated by muscle proteins to regulate sarcomere structure and function yet to be studied. Therefore, more research is needed to see how external triggers are integrated with local tension generated within the cell. Nonetheless, maintenance of tension in the sarcomere is the essential and dominant mechanism, leading to the well-known phrase in exercise physiology: "use it or lose it."

Indexed as

AdhesomeCostamereIntegrinMechanobiologyMechanotransductionSarcomere

Identifiers

PMID34777614
PMCPMC8555064
OpenAlexW3198278026

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.