Evidence map›Paper›PMID 18552179›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Characterization of the pre-force-generation state in the actomyosin cross-bridge cycle.

Mingxuan Sun, Michael B Rose, Shobana K Ananthanarayanan, Donald J Jacobs, Christopher M Yengo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
2.7field-weighted citation impact, top 9% 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, 43 citations in OpenAlex.

  1. Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
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  8. Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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  16. Characterizing protein motions from structure.Journal of molecular graphics & modelling · 2011
    Article
  17. Article
  18. Structural kinetics of myosin by transient time-resolved FRET.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Article
  20. Review
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

5 authors at 1 institution in 1 country.

Mingxuan SunDepartments of Biology and Physics and Optical Science, University of North Carolina, Charlotte, NC 28223, USA.
Michael B Rose
Shobana K Ananthanarayanan
Donald J Jacobs
Christopher M Yengo
University of North Carolina at Charlotte · US

Funding

Predicting protein flexibility and stabilityR01GM073082 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI JACOBS, DONALD · 2006 to 2010
$1.6M
NIGMS NIH HHS R01 GM073082NIGMS NIH HHS R01 GM073082-01A1
6 · The paper itself

Abstract

Myosin is an actin-based motor protein that generates force by cycling between actin-attached (strong binding: ADP or rigor) and actin-detached (weak binding: ATP or ADP.P(i)) states during its ATPase cycle. However, it remains unclear what specific conformational changes in the actin binding site take place on binding to actin, and how these structural changes lead to product release and the production of force and motion. We studied the dynamics of the actin binding region of myosin V by using fluorescence resonance energy transfer (FRET) to monitor conformational changes in the upper-50-kDa domain of the actin binding cleft in the weak and strong actin binding states. Steady-state and lifetime data monitoring the FRET signal suggest that the cleft is in a more open conformation in the weak actin binding states. Transient kinetic experiments suggest that a rapid conformational change occurs, which is consistent with cleft closure before actin-activated phosphate release. Our results have identified a pre-force-generation actomyosin ADP.P(i) state, and suggest force generation may occur from a state not yet seen by crystallography in which the actin binding cleft and the nucleotide binding pocket are closed. Computational modeling uncovers dramatic changes in the rigidity of the upper-50-kDa domain in different nucleotide states, which suggests that the intrinsic flexibility of this domain allows myosin motors to accomplish simultaneous tight nucleotide binding (closed nucleotide binding pocket) and high-affinity actin binding (closed actin binding cleft).

Indexed as

ActomyosinBinding SitesFluorescence Resonance Energy TransferKineticsModels, MolecularProtein ConformationStructure-Activity RelationshipTemperatureActomyosin

Identifiers

PMID18552179
PMCPMC2438420
OpenAlexW2099127313

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.