Evidence map›Paper›PMID 12879150›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2003

Tuning smooth muscle contraction by molecular motors.

Ingo Morano

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-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

19 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  10. Review
  11. Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  12. Article
  13. Direct association of calponin with specific domains of PKC-alpha.American journal of physiology. Gastrointestinal and liver physiology · 2008
    Article
  14. Article
  15. Review
  16. Regulation of the uterine contractile apparatus and cytoskeleton.Seminars in cell & developmental biology · 2007
    Review
  17. Article
  18. Article
  19. 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

1 author at 1 institution in 1 country.

Ingo MoranoMax Delbrück Centrum for Molecular Medicine and Humboldt University, Johannes Müller Institute for Physiology, Berlin, Germany. Imorano@mdc-berlin.de
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As in striated muscle, smooth muscle cells (SMC) contract by Ca2+ activated cyclic interaction between actin and type II myosin. However, smooth muscle maintains tone at basal activating Ca2+ and low energetic cost during sustained activation. This review analyzes the regulation of phasic and tonic contraction of SMC on the molecular level. Type II myosin is the molecular motor also of smooth muscle contraction. Six myosin heavy chain (MHC) isoenzymes (four smooth muscle, two nonmuscle) and five myosin light chain (MLC) isoforms (two 17 kDa, two 20 kDa, one 23 kDa) are expressed in SMC. These myosin subunits could be generated by alternative splicing or by differential gene expression. Thus different myosin isoenzymes are generated which may be modified posttranslationally by phosphorylation, affecting the contractile state of the SMC. Furthermore, they may be part of distinct contractile systems which are targeted by different second messenger cascades and are recruited differentially during activation, electromechanical, and pharmacomechanical coupling. Low energy consumption, shortening velocity, and MLC20 phosphorylation at low Ca2+ activation levels during tone maintenance ("latch") could be explained by a switch from smooth muscle myosin to nonmuscle myosin activation upon prolonged activation.

Indexed as

Alternative SplicingGene Expression RegulationHumansIsoenzymesMolecular Motor ProteinsMuscle ContractionMuscle, SmoothMyosin Heavy ChainsMyosin-Light-Chain KinaseMyosin Light ChainsIsoenzymesMolecular Motor ProteinsMyosin Heavy ChainsMyosin-Light-Chain KinaseMyosin Light Chains

Identifiers

PMID12879150
OpenAlexW2164379131

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.