Evidence map›Paper›PMID 21565153›Full record

ReviewArchives of biochemistry and biophysics2011

Biochemistry of smooth muscle myosin light chain kinase.

Feng Hong, Brian D Haldeman, Del Jackson, Mike Carter, Jonathan E Baker, Christine R Cremo

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Molecular Insights into the MLCK Activation by CaM.Journal of chemical information and modeling · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
  17. Review
  18. Article
  19. Visceral myopathy: clinical syndromes, genetics, pathophysiology, and fall of the cytoskeleton.American journal of physiology. Gastrointestinal and liver physiology · 2021
    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

6 authors at 1 institution in 1 country.

Feng HongDepartment of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno, 89557, USA.
Brian D Haldeman
Del Jackson
Mike Carter
Jonathan E Baker
Christine R Cremo
University of Nevada, Reno · US

Funding

TOPOGRAPHICAL STUDIES OF SMOOTH AND NONMUSCLE MYOSINSR01AR040917 · NIAMS · WASHINGTON STATE UNIVERSITY · PI CREMO, CHRISTINE R · 1996 to 2009
$3.2M
A Multi-Scale Study of the Interplay Between Force Generating and Force Sensing MR01HL090938 · NHLBI · UNIVERSITY OF NEVADA RENO · PI BAKER, JONATHAN E. · 2008 to 2011
$1.3M
NHLBI NIH HHS R01 HL090938NIAMS NIH HHS R01 AR040917
6 · The paper itself

Abstract

The smooth muscle isoform of myosin light chain kinase (MLCK) is a Ca(2+)-calmodulin-activated kinase that is found in many tissues. It is particularly important for regulating smooth muscle contraction by phosphorylation of myosin. This review summarizes selected aspects of recent biochemical work on MLCK that pertains to its function in smooth muscle. In general, the focus of the review is on new findings, unresolved issues, and areas with the potential for high physiological significance that need further study. The review includes a concise summary of the structure, substrates, and enzyme activity, followed by a discussion of the factors that may limit the effective activity of MLCK in the muscle. The interactions of each of the many domains of MLCK with the proteins of the contractile apparatus, and the multi-domain interactions of MLCK that may control its behaviors in the cell are summarized. Finally, new in vitro approaches to studying the mechanism of phosphorylation of myosin are introduced.

Indexed as

Amino Acid SequenceAnimalsConserved SequenceHumansMolecular Sequence DataMuscle ProteinsMuscle, SmoothMyosin-Light-Chain KinaseProtein Structure, TertiaryMuscle ProteinsMyosin-Light-Chain Kinase

Identifiers

PMID21565153
PMCPMC3382066
OpenAlexW2088607946

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.