Evidence map›Paper›PMID 10961838›Full record

ReviewJournal of muscle research and cell motility2000

Variable surface loops and myosin activity: accessories to a motor.

C T Murphy, J A Spudich

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Loop 2 of myosin is a force-dependent inhibitor of the rigor bond.Journal of muscle research and cell motility · 2014
    Article
  7. Article
  8. Article
  9. Functional diversity among a family of human skeletal muscle myosin motors.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Molecular engineering of myosin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  15. 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.

C T MurphyDepartment of Biochemistry, Stanford University School of Medicine, CA 94305, USA.
J A Spudich
Stanford University · US

Funding

PHS HHS 33289
6 · The paper itself

Abstract

The catalytic head of myosin is a globular structure that has historically been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed, proteolytically-sensitive surface loops of myosin that join these three segments are highly variable in their sequences. While surface loops have not traditionally been thought to affect enzymatic activities, these loops lie near the ATP and actin-binding sites and have been implicated in the modulation of myosin's kinetic activities. In this work we review the wealth of data regarding the loops that has accumulated over the years and discuss the roles of the loops in contributing to the different activities displayed by different myosin isoforms.

Indexed as

ActinsAmino Acid SequenceAnimalsHumansMuscle, SkeletalMuscle, SmoothMyosinsActinsMyosins

Identifiers

PMID10961838
OpenAlexW160463979

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.