Evidence map›Paper›PMID 26385864›Full record

ReviewJournal of muscle research and cell motility2015

Molecular mechanisms of cardiomyopathy phenotypes associated with myosin light chain mutations.

Wenrui Huang, Danuta Szczesna-Cordary

Open access · greenAbstract readReview
In one paragraph

Review in Journal of muscle research and cell motility, 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
3.2field-weighted citation impact, top 8% 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, 37 citations in OpenAlex.

  1. Article
  2. Fine tuning contractility: atrial sarcomere function in health and disease.American journal of physiology. Heart and circulatory physiology · 2024
    Review
  3. Article
  4. Cryo-EM structure of the folded-back state of human β-cardiac myosin.bioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Dysfunctional sarcomeric relaxation in the heart.Current opinion in physiology · 2022
    Article
  7. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  8. Article
  9. Article
  10. Regulatory Light Chains in Cardiac Development and Disease.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Actin-Myosin Interaction: Structure, Function and Drug Discovery.International journal of molecular sciences · 2018
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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.

Wenrui HuangDepartment of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL, 33136, USA.
Danuta Szczesna-CordaryDepartment of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL, 33136, USA. dszczesna@med.miami.edu.
University of Miami · US

Funding

Novel cardioskeletal myopathy associated with MYL2R01HL123255 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SZCZESNA-CORDARY, DANUTA · 2015 to 2018
$2.0M
Myosin ELC, a novel therapeutic target for FHCR01HL108343 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SZCZESNA-CORDARY, DANUTA · 2012 to 2015
$1.5M
NHLBI NIH HHS HL108343NHLBI NIH HHS HL123255NHLBI NIH HHS R01 HL108343NHLBI NIH HHS R01 HL123255
6 · The paper itself

Abstract

We discuss here the potential mechanisms of action associated with hypertrophic (HCM) or dilated (DCM) cardiomyopathy causing mutations in the myosin regulatory (RLC) and essential (ELC) light chains. Specifically, we focus on four HCM mutations: RLC-A13T, RLC-K104E, ELC-A57G and ELC-M173V, and one DCM RLC-D94A mutation shown by population studies to cause different cardiomyopathy phenotypes in humans. Our studies indicate that RLC and ELC mutations lead to heart disease through different mechanisms with RLC mutations triggering alterations of the secondary structure of the RLC which further affect the structure and function of the lever arm domain and impose changes in the cross bridge cycling rates and myosin force generation ability. The ELC mutations exert their detrimental effects through changes in the interaction of the N-terminus of ELC with actin altering the cross talk between the thick and thin filaments and ultimately resulting in an altered force-pCa relationship. We also discuss the effect of mutations on myosin light chain phosphorylation. Exogenous myosin light chain phosphorylation and/or pseudo-phosphorylation were explored as potential rescue tools to treat hypertrophy-related cardiac phenotypes.

Indexed as

AnimalsCardiomyopathy, Hypertrophic, FamilialHumansMutationMyosin Light ChainsPhenotypePhosphorylationMyosin Light ChainsCardiomyopathyFunctionMutationMyosin light chainsPhosphorylationStructure

Identifiers

PMID26385864
PMCPMC4764388
OpenAlexW1695363803

What OpenQuestion holds

Textmetadata
LicenceTDM
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.