Evidence map›Paper›PMID 27084718›Full record

ReviewEuropean biophysics journal : EBJ2016

Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives.

Haiyang Yu, Samya Chakravorty, Weihua Song, Michael A Ferenczi

Open access · hybridAbstract readReview
In one paragraph

Review in European biophysics journal : EBJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Cardiac muscle physiology.BJA education · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Regulatory Light Chains in Cardiac Development and Disease.International journal of molecular sciences · 2021
    Review
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Haiyang YuLee Kong Chian School of Medicine, Nanyang Technological University, Experimental Medicine Building, Level 3, 59 Nanyang Drive, Singapore, 636921, Singapore.
Samya ChakravortyLee Kong Chian School of Medicine, Nanyang Technological University, Experimental Medicine Building, Level 3, 59 Nanyang Drive, Singapore, 636921, Singapore.
Weihua SongLee Kong Chian School of Medicine, Nanyang Technological University, Experimental Medicine Building, Level 3, 59 Nanyang Drive, Singapore, 636921, Singapore.
Michael A FerencziLee Kong Chian School of Medicine, Nanyang Technological University, Experimental Medicine Building, Level 3, 59 Nanyang Drive, Singapore, 636921, Singapore. m.ferenczi@ntu.edu.sg.
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation of the regulatory light chain (RLC) of myosin modulates cellular functions such as muscle contraction, mitosis, and cytokinesis. Phosphorylation defects are implicated in a number of diseases. Here we focus on striated muscle where changes in RLC phosphorylation relate to diseases such as hypertrophic cardiomyopathy and muscular dystrophy, or age-related changes. RLC phosphorylation in smooth muscle and non-muscle cells are covered briefly where relevant. There is much scientific interest in controlling the phosphorylation levels of RLC in vivo and in vitro in order to understand its physiological function in striated muscles. A summary of available and emerging in vivo and in vitro methods is presented. The physiological role of RLC phosphorylation and novel pathways are discussed to highlight the differences between muscle types and to gain insights into disease processes.

Indexed as

Amino Acid SequenceAnimalsBinding SitesHumansMuscle, StriatedMyosin Light ChainsPhosphorylationProtein EngineeringProtein IsoformsMyosin Light ChainsProtein IsoformsCardiovascular diseaseMechanochemistryMuscle contractionMyosinPhosphorylationRegulatory light chain

Identifiers

PMID27084718
PMCPMC5101276
OpenAlexW2336162421

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.