Evidence map›Paper›PMID 23091026›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.

Bipasha Barua, Donald A Winkelmann, Howard D White, Sarah E Hitchcock-DeGregori

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.6field-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

41 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Case reports in genetics · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mutations Q93H and E97K inInternational journal of molecular sciences · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 3 institutions in 1 country.

Bipasha BaruaDepartment of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA. baruabi@umdnj.edu
Donald A Winkelmann
Howard D White
Sarah E Hitchcock-DeGregori
Johnson University · USEastern Virginia Medical School · USRutgers, The State University of New Jersey · US

Funding

Deciphering how tropomyosin regulates the actin filamentR01GM093065 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HITCHCOCK-DEGREGORI, SARAH ELLEN · 2010 to 2013
$1.2M
NIGMS NIH HHS GM093065NIGMS NIH HHS R01 GM093065
6 · The paper itself

Abstract

Cooperative activation of actin-myosin interaction by tropomyosin (Tm) is central to regulation of contraction in muscle cells and cellular and intracellular movements in nonmuscle cells. The steric blocking model of muscle regulation proposed 40 y ago has been substantiated at both the kinetic and structural levels. Even with atomic resolution structures of the major players, how Tm binds and is designed for regulatory function has remained a mystery. Here we show that a set of periodically distributed evolutionarily conserved surface residues of Tm is required for cooperative regulation of actomyosin. Based on our results, we propose a model of Tm on a structure of actin-Tm-myosin in the "open" (on) state showing potential electrostatic interactions of the residues with both actin and myosin. The sites alternate with a second set of conserved surface residues that are important for actin binding in the inhibitory state in the absence of myosin. The transition from the closed to open states requires the sites identified here, even when troponin + Ca(2+) is present. The evolutionarily conserved residues are important for actomyosin regulation, a universal function of Tm that has a common structural basis and mechanism.

Indexed as

Conserved SequenceActin CytoskeletonActinsAdenosine DiphosphateAmino Acid SequenceAnimalsBinding SitesCalciumEvolution, MolecularFluorescenceIodoacetamideKineticsModels, MolecularMolecular Sequence DataMutationMyosinsActinsAdenosine DiphosphateCalciumIodoacetamideMyosinsN-(1-pyrenyl)iodoacetamidePhosphatesTropomyosinTroponin

Identifiers

PMID23091026
PMCPMC3494946
OpenAlexW2004048009

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.