Evidence map›Paper›PMID 18855423›Full record

ArticleBiochemistry2008

Changes in actin structural transitions associated with oxidative inhibition of muscle contraction.

Ewa Prochniewicz, Daniel Spakowicz, David D Thomas

Abstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Unique methionine-aromatic interactions govern the calmodulin redox sensor.Biochemical and biophysical research communications · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Dystrophin and utrophin have distinct effects on the structural dynamics of actin.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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.

Ewa ProchniewiczDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Daniel Spakowicz
David D Thomas
University of Minnesota · US

Funding

Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
Site-Directed Oxidative Modification of Muscle Protein Structural DynamicsR37AG026160 · NIA · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2011 to 2020
$4.5M
Protein Oxidation, Structure, &Function in Aging MuscleR01AG026160 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 2004 to 2008
$2.2M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
NIAMS NIH HHS AR32961NIAMS NIH HHS R01 AR032961NIAMS NIH HHS R37 AR032961NIA NIH HHS AG26160NIA NIH HHS R01 AG026160NIA NIH HHS R37 AG026160
6 · The paper itself

Abstract

We have used transient phosphorescence anisotropy (TPA) to detect changes in actin structural dynamics associated with oxidative inhibition of muscle contraction. Contractility of skinned rabbit psoas muscle fibers was inhibited by treatment with 50 mM H 2O 2, which induced oxidative modifications in the myosin head and in actin, as previously reported. Using proteins purified from oxidized and unoxidized muscle, we used TPA to measure the effects of weakly (+ATP) and strongly (no ATP) bound myosin heads (S1) on the microsecond dynamics of actin labeled at Cys374 with erythrosine iodoacetamide. Oxidative modification of S1 had no effect on actin dynamics in the absence of ATP (strong binding complex), but restricted the dynamics in the presence of ATP (weakly bound complex). In contrast, oxidative modification of actin did not have a significant effect on the weak-to-strong transitions. Thus, we concluded that (1) the effects of oxidation on the dynamics of actin in the actomyosin complex are predominantly determined by oxidation-induced changes in S1, and (2) changes in weak-to-strong structural transitions in actin and myosin are coupled to each other and are associated with oxidative inhibition of muscle contractility.

Indexed as

ActinsAdenosine TriphosphateAnimalsHydrogen PeroxideModels, MolecularMuscle ContractionMuscle, SkeletalMyosinsOxidation-ReductionProtein BindingRabbitsActinsAdenosine TriphosphateHydrogen PeroxideMyosins

Identifiers

PMID18855423
PMCPMC3253347
OpenAlexW2135639069

What OpenQuestion holds

Textmetadata
LicenceTDM
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.