Evidence map›Paper›PMID 23528086›Full record

ArticleBiophysical journal2013

Tilting and wobble of myosin V by high-speed single-molecule polarized fluorescence microscopy.

John F Beausang, Deborah Y Shroder, Philip C Nelson, Yale E Goldman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
8.8field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Volumetric imaging of the 3D orientation of cellular structures with a polarized fluorescence light-sheet microscope.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. No hype in hyperspace.Biophysical journal · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. STEAM: Using the Arts to Train Well-Rounded and Creative Scientists.Journal of microbiology & biology education · 2018
    Article
  20. Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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 1 institution in 1 country.

John F BeausangDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA, USA.
Deborah Y Shroder
Philip C Nelson
Yale E Goldman
University of Pennsylvania · US

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
StructuraL Dynamics of Actomyosin MotilityR01GM086352 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GOLDMAN, YALE E · 2008 to 2016
$3.8M
STRUCTURAL DYNAMICS OF ACTOMYOSIN MOTILITYR01AR026846 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI GOLDMAN, YALE E · 1986 to 2007
$2.3M
NIAMS NIH HHS R01 AR026846NIGMS NIH HHS R01 GM086352NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Myosin V is biomolecular motor with two actin-binding domains (heads) that take multiple steps along actin by a hand-over-hand mechanism. We used high-speed polarized total internal reflection fluorescence (polTIRF) microscopy to study the structural dynamics of single myosin V molecules that had been labeled with bifunctional rhodamine linked to one of the calmodulins along the lever arm. With the use of time-correlated single-photon counting technology, the temporal resolution of the polTIRF microscope was improved ~50-fold relative to earlier studies, and a maximum-likelihood, multitrace change-point algorithm was used to objectively determine the times when structural changes occurred. Short-lived substeps that displayed an abrupt increase in rotational mobility were detected during stepping, likely corresponding to random thermal fluctuations of the stepping head while it searched for its next actin-binding site. Thus, myosin V harnesses its fluctuating environment to extend its reach. Additional, less frequent angle changes, probably not directly associated with steps, were detected in both leading and trailing heads. The high-speed polTIRF method and change-point analysis may be applicable to single-molecule studies of other biological systems.

Indexed as

Microscopy, FluorescenceAnimalsMovementMyosin Type VRhodaminesRotationTime FactorsMyosin Type VRhodamines

Identifiers

PMID23528086
PMCPMC3602762
OpenAlexW1976138338

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.