Evidence map›Paper›PMID 7935353›Full record

ReviewMolecular and cellular biochemistry1993

Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains.

R S Moussavi, C A Kelley, R S Adelstein

Abstract readComparative StudyReview
PubMed Publisher
In one paragraph

Review in Molecular and cellular biochemistry, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
0.3field-weighted citation impact, top 56% 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

36 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  3. Article
  4. Changes in Myosin from Silver Carp (Foods (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. The PAR polarity complex and cerebellar granule neuron migration.Advances in experimental medicine and biology · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  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

3 authors at 2 institutions in 1 country.

R S MoussaviLaboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
C A Kelley
R S Adelstein
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this article we review the various amino acids present in vertebrate nonmuscle and smooth muscle myosin that can undergo phosphorylation. The sites for phosphorylation in the 20 kD myosin light chain include serine-19 and threonine-18 which are substrates for myosin light chain kinase and serine-1 and/or -2 and threonine-9 which are substrates for protein kinase C. The sites in vertebrate smooth muscle and nonmuscle myosin heavy chains that can be phosphorylated by protein kinase C and casein kinase II are also summarized. Original data indicating that treatment of human T-lymphocytes (Jurkat cell line) with phorbol 12-myristate 13-acetate results in phosphorylation of both the 20 kD myosin light chain as well as the 200 kD myosin heavy chain is presented. We identified the amino acids phosphorylated in the human T-lymphocytes myosin light chains as serine-1 or serine-2 and in the myosin heavy chains as serine-1917 by 1-dimensional isoelectric focusing of tryptic phosphopeptides. Untreated T-lymphocytes contain phosphate in the serine-19 residue of the myosin light chain, and in a residue tentatively identified as serine-1944 in the myosin heavy chain.

Indexed as

Amino Acid SequenceAnimalsAortaBrainCattleDrosophilaHumansMolecular Sequence DataMuscle, SmoothMuscle, Smooth, VascularMyosin-Light-Chain KinaseMyosinsOrgan SpecificityPeptide FragmentsPhosphorylationPhosphoserineMyosin-Light-Chain KinaseMyosinsPeptide FragmentsPhosphoserineProtein Kinase C

Identifiers

PMID7935353
OpenAlexW1995962514

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.