Evidence map›Paper›PMID 24630103›Full record

ArticleMethods in enzymology2014

Single-molecule studies of actin assembly and disassembly factors.

Benjamin A Smith, Jeff Gelles, Bruce L Goode

Abstract read
In one paragraph

Article in Methods in enzymology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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. Life science alliance · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Review
  11. Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017
    Review
  12. 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.

Benjamin A SmithDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts, USA; Present address: Biogen Idec, Cambridge, Massachusetts, USA.
Jeff GellesDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts, USA. Electronic address: gelles@brandeis.edu.
Bruce L GoodeDepartment of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, USA. Electronic address: goode@brandeis.edu.

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Molecular Mechanisms coordinating the actin and microtubule cytoskeletonsR01GM098143 · NIGMS · BRANDEIS UNIVERSITY · PI GELLES, JEFF, GOODE, BRUCE L · 2012 to 2019
$2.6M
Structure and mechanism of the dynein motorR01GM097312 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2011 to 2016
$1.5M
MICROTUBULE-BASED ORGANELLE TRANSPORTR01GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI VALE, RONALD D · 1988 to 2005
$1.2M
NIGMS NIH HHS GM063691NIGMS NIH HHS GM098143NIGMS NIH HHS R01 GM038499NIGMS NIH HHS R01 GM063691NIGMS NIH HHS R01 GM097312NIGMS NIH HHS R01 GM098143NIGMS NIH HHS R01GM098143
6 · The paper itself

Abstract

The actin cytoskeleton is very dynamic and highly regulated by multiple associated proteins in vivo. Understanding how this system of proteins functions in the processes of actin network assembly and disassembly requires methods to dissect the mechanisms of activity of individual factors and of multiple factors acting in concert. The advent of single-filament and single-molecule fluorescence imaging methods has provided a powerful new approach to discovering actin-regulatory activities and obtaining direct, quantitative insights into the pathways of molecular interactions that regulate actin network architecture and dynamics. Here we describe techniques for acquisition and analysis of single-molecule data, applied to the novel challenges of studying the filament assembly and disassembly activities of actin-associated proteins in vitro. We discuss the advantages of single-molecule analysis in directly visualizing the order of molecular events, measuring the kinetic rates of filament binding and dissociation, and studying the coordination among multiple factors. The methods described here complement traditional biochemical approaches in elucidating actin-regulatory mechanisms in reconstituted filamentous networks.

Indexed as

Actin CytoskeletonActinsEquipment DesignFluorescent DyesMicroscopy, FluorescenceOptical ImagingStaining and LabelingActinsFluorescent DyesArp2/3 complexBinding kineticsCofilinFilament nucleationForminPolymerizationSeveringTotal internal reflection fluorescence

Identifiers

PMID24630103
PMCPMC4037564

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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.