Evidence map›Paper›PMID 18480297›Full record

ArticleAmerican journal of physiology. Cell physiology2008

Effect of low pH on single skeletal muscle myosin mechanics and kinetics.

E P Debold, S E Beck, D M Warshaw

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 3 pooled it
2.1field-weighted citation impact, top 12% 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

55 citing papers in PubMed, 3 syntheses or guidelines pooled it, 109 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Trial
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  18. CaBiomolecules · 2025
    Review
  19. Lactic acidosis: implications for human exercise performance.European journal of applied physiology · 2025
    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

3 authors at 1 institution in 1 country.

E P DeboldDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA. ndebold@physiology.med.uvm.edu
S E Beck
D M Warshaw
University of Vermont · US

Funding

Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI ROBBINS, JEFFREY · 1999 to 2014
$26.4M
Smooth Muscle Myosin: Molecular Mechanics and Intramolecular CommunicationR01HL085489 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2006 to 2009
$1.5M
NHLBI NIH HHS HL 059408NHLBI NIH HHS HL 085489NHLBI NIH HHS P01 HL059408NHLBI NIH HHS R01 HL085489
6 · The paper itself

Abstract

Acidosis (low pH) is the oldest putative agent of muscular fatigue, but the molecular mechanism underlying its depressive effect on muscular performance remains unresolved. Therefore, the effect of low pH on the molecular mechanics and kinetics of chicken skeletal muscle myosin was studied using in vitro motility (IVM) and single molecule laser trap assays. Decreasing pH from 7.4 to 6.4 at saturating ATP slowed actin filament velocity (V(actin)) in the IVM by 36%. Single molecule experiments, at 1 microM ATP, decreased the average unitary step size of myosin (d) from 10 +/- 2 nm (pH 7.4) to 2 +/- 1 nm (pH 6.4). Individual binding events at low pH were consistent with the presence of a population of both productive (average d = 10 nm) and nonproductive (average d = 0 nm) actomyosin interactions. Raising the ATP concentration from 1 microM to 1 mM at pH 6.4 restored d (9 +/- 3 nm), suggesting that the lifetime of the nonproductive interactions is solely dependent on the [ATP]. V(actin), however, was not restored by raising the [ATP] (1-10 mM) in the IVM assay, suggesting that low pH also prolongs actin strong binding (t(on)). Measurement of t(on) as a function of the [ATP] in the single molecule assay suggested that acidosis prolongs t(on) by slowing the rate of ADP release. Thus, in a detachment limited model of motility (i.e., V(actin) approximately d/t(on)), a slowed rate of ADP release and the presence of nonproductive actomyosin interactions could account for the acidosis-induced decrease in V(actin), suggesting a molecular explanation for this component of muscular fatigue.

Indexed as

Actin CytoskeletonAdenosine TriphosphateAnimalsBiomechanical PhenomenaChickensComputer SimulationHydrogen-Ion ConcentrationKineticsSkeletal Muscle MyosinsAdenosine TriphosphateSkeletal Muscle Myosins

Identifiers

PMID18480297
PMCPMC2493560
OpenAlexW2108383149

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.