Evidence map›Paper›PMID 15345561›Full record

ArticleBiophysical journal2004

Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications.

Boris Gafurov, Yi-Der Chen, Joseph M Chalovich

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.

  1. Pooled it
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  5. Review
  6. Article
  7. Article
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  12. Mini-thin filaments regulated by troponin-tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  13. 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.

Boris GafurovLaboratory of Biological Modeling, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-5621, USA.
Yi-Der Chen
Joseph M Chalovich
East Carolina University · USNational Institutes of Health · US

Funding

Acting Based Regulation of Smooth Muscle ContractionR01AR035216 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1986 to 2007
$1.5M
WEAKLY BOUND CROSSBRIDGES AND MUSCLE CONTRACTIONR01AR040540 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1991 to 1994
–
NIAMS NIH HHS AR40540NIAMS NIH HHS R01 AR035216
6 · The paper itself

Abstract

Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin-troponin. Binding of Ca(2+) to troponin or binding of ATP-free myosin to actin reverses this inhibition. Ca(2+) and ATP-free myosin stabilize different tropomyosin-actin structural arrangements. The position of tropomyosin on actin affects the binding of ATP-free myosin to actin but does not greatly affect myosin-ATP binding. Ca(2+) and ATP-free myosin alter both the affinity of ATP-free myosin for actin and the kinetics of that binding. A parallel pathway model of regulation simulated the effects of Ca(2+) and ATP-free myosin binding on both equilibrium binding of myosin-nucleotide complexes to actin and the general features of ATPase activity. That model was recently shown to simulate the kinetics of myosin-S1 binding but the analysis was limited to a single condition because of the limited data available. We have now measured equilibrium binding and binding kinetics of myosin-S1-ADP to actin at a series of ionic strengths and free Ca(2+) concentrations. The parallel pathway model of regulation is consistent with those data. In that model the interaction between adjacent regulatory complexes fully saturated with Ca(2+) was destabilized and the inactive state of actin was stabilized at high ionic strength. These changes explain the previously observed change in binding kinetics with increasing ionic strength.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsCalciumDose-Response Relationship, DrugGene Expression RegulationHydrolysisIonsKineticsModels, MolecularMyosinsProtein BindingRabbitsSpectrometry, FluorescenceTropomyosinActinsAdenosine DiphosphateAdenosine TriphosphateCalciumIonsMyosinsTropomyosinTroponin

Identifiers

PMID15345561
PMCPMC1304587
OpenAlexW2154326967

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.