Evidence map›Paper›PMID 23487037›Full record

ReviewJournal of cell science2013

Force generation by kinesin and myosin cytoskeletal motor proteins.

F Jon Kull, Sharyn A Endow

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  6. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  7. Article
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  14. Review
  15. Article
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  17. Article
  18. These motors were made for walking.Protein science : a publication of the Protein Society · 2020
    Review
  19. Review
  20. 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 at 2 institutions in 1 country.

F Jon KullDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, USA.
Sharyn A Endow
Dartmouth College · USDuke University · US

Funding

CHROMOSOME MOVEMENT IN MEIOSIS AND MITOSISR01GM046225 · NIGMS · DUKE UNIVERSITY · PI ENDOW, SHARYN A. · 1991 to 2011
$3.5M
Fine tuning the catalytic cycle of kinesin motorsR01GM097079 · NIGMS · DARTMOUTH COLLEGE · PI KULL, FREDRICK JON · 2011 to 2014
$1.2M
NIGMS NIH HHS GM046225NIGMS NIH HHS GM097079NIGMS NIH HHS R01 GM046225NIGMS NIH HHS R01 GM097079
6 · The paper itself

Abstract

Kinesins and myosins hydrolyze ATP, producing force that drives spindle assembly, vesicle transport and muscle contraction. How do motors do this? Here we discuss mechanisms of motor force transduction, based on their mechanochemical cycles and conformational changes observed in crystal structures. Distortion or twisting of the central β-sheet - proposed to trigger actin-induced Pi and ADP release by myosin, and microtubule-induced ADP release by kinesins - is shown in a movie depicting the transition between myosin ATP-like and nucleotide-free states. Structural changes in the switch I region form a tube that governs ATP hydrolysis and Pi release by the motors, explaining the essential role of switch I in hydrolysis. Comparison of the motor power strokes reveals that each stroke begins with the force-amplifying structure oriented opposite to the direction of rotation or swing. Motors undergo changes in their mechanochemical cycles in response to small-molecule inhibitors, several of which bind to kinesins by induced fit, trapping the motors in a state that resembles a force-producing conformation. An unusual motor activator specifically increases mechanical output by cardiac myosin, potentially providing valuable information about its mechanism of function. Further study is essential to understand motor mechanochemical coupling and energy transduction, and could lead to new therapies to treat human disease.

Indexed as

Adenosine TriphosphateAnimalsBiomechanical PhenomenaCytoskeletal ProteinsHumansKinesinsModels, BiologicalMolecular Motor ProteinsMyosinsAdenosine TriphosphateCytoskeletal ProteinsKinesinsMolecular Motor ProteinsMyosins

Identifiers

PMID23487037
PMCPMC3603507
OpenAlexW2042294339

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.