Evidence map›Paper›PMID 16698919›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

On the hand-over-hand mechanism of kinesin.

Qiang Shao, Yi Qin Gao

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanistic basis of propofol-induced disruption of kinesin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Structural consequences of hereditary spastic paraplegia disease-related mutations in kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Review
  7. Mechanism of processive movement of monomeric and dimeric kinesin molecules.International journal of biological sciences · 2010
    Review
  8. Article
  9. Article
  10. Mechanical control of the directional stepping dynamics of the kinesin motor.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  11. 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

2 authors.

Qiang ShaoDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Yi Qin Gao

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present here a simple theoretical model for conventional kinesin. The model reproduces the hand-over-hand mechanism for kinesin walking to the plus end of a microtubule. A large hindering force induces kinesin to walk slowly to the minus end, again by a hand-over-hand mechanism. Good agreement is obtained between the calculated and experimental results on the external force dependence of the walking speed, the forward/backward step ratio, and dwell times for both forward and backward steps. The model predicts that both forward and backward motions of kinesin take place at the same chemical state of the motor heads, with the front head being occupied by an ATP (or ADP,Pi) and the rear being occupied by an ADP. The direction of motion is a result of the competition between the power stroke produced by the front head and the external load. The other predictions include the external force dependence of the chemomechanical coupling ratio (e.g., the stepping distance/ATP ratio) and the walking speed of kinesin at force ranges that have not been tested by experiments. The model predicts that the chemomechanical coupling remains tight in a large force range. However, when the external force is very large (e.g., approximately 18 pN), kinesin slides in an inchworm fashion, and the translocation of kinesin becomes loosely coupled to ATP turnovers.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsBiophysicsDyneinsHydrolysisKinesinsModels, BiologicalMolecular Motor ProteinsAdenosine DiphosphateAdenosine TriphosphateDyneinsKinesinsMolecular Motor Proteins

Identifiers

PMID16698919
PMCPMC1472431

What OpenQuestion holds

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Registered trials

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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.