Evidence map›Paper›PMID 7787085›Full record

ReviewBiophysical journal1995

The mechanics of force generation by kinesin.

J Howard

Abstract readComparative StudyReview
In one paragraph

Review in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  7. Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

1 author.

J HowardDepartment of Physiology and Biophysics, University of Washington, Seattle 98195, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several laboratories have developed highly sensitive mechanical techniques for studying the movement of purified motor proteins along their associated filaments. The aim of these experiments is to test models for force generation, such as the powerstroke model and "ratchet" or diffusional models, by 1) directly visualizing the path on the filament along which the motor moves, 2) measuring the force exerted by the motor against the filament, and 3) characterizing the passive mechanical properties (elasticity) of the motor. This paper focuses on recently published work on the microtubule-based motor kinesin taking this mechanical approach. Related work on myosin is mentioned for comparison.

Indexed as

Adenosine TriphosphateAnimalsBinding SitesBiomechanical PhenomenaBiophysical PhenomenaBiophysicsElasticityIn Vitro TechniquesKinesinsMicrotubulesModels, BiologicalMovementMyosinsViscosityAdenosine TriphosphateKinesinsMyosins

Identifiers

PMID7787085
PMCPMC1281936

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.