Evidence map›Paper›PMID 23663840›Full record

ArticleBiophysical journal2013

Modular aspects of kinesin force generation machinery.

William R Hesse, Miriam Steiner, Matthew L Wohlever, Roger D Kamm, Wonmuk Hwang, Matthew J Lang

Abstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. These motors were made for walking.Protein science : a publication of the Protein Society · 2020
    Review
  5. The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Frontiers in cellular and infection microbiology · 2020
    Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. New approach to capture and characterize synaptic proteome.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

William R HesseMechanical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Miriam Steiner
Matthew L Wohlever
Roger D Kamm
Wonmuk Hwang
Matthew J Lang

Funding

Computational and single molecule analysis of kinesin's atomistic machineryR01GM087677 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI HWANG, WONMUK, LANG, MATTHEW J. · 2009 to 2012
$911k
NIGMS NIH HHS R01 GM087677NIGMS NIH HHS R01GM087677
6 · The paper itself

Abstract

The motor head of kinesin carries out microtubule binding, ATP hydrolysis, and force generation. Despite a high level of sequence and structural conservation, subtle variations in subdomains of the motor head determine family-specific properties. In particular, both Kinesin-1 (Kin-1) and Kinesin-5 (Kin-5) walk processively to the microtubule plus-end, yet show distinct motility characteristics suitable for their functions. We studied chimeric Kin-1/Kin-5 constructs with a combination of single molecule motility assays and molecular dynamics simulations to demonstrate that Kin-5 possesses a force-generating element similar to Kin-1, i.e., the cover-neck bundle. Furthermore, the Kin-5 neck linker makes additional contacts with the core of the motor head via loop L13, which putatively compensates for the shorter cover-neck bundle of Kin-5. Our results indicate that Kin-1 is mechanically optimized for individual cargo transport, whereas Kin-5 does not necessarily maximize its mechanical performance. Its biochemical rates and enhanced force sensitivity may instead be beneficial for operation in a group of motors. Such variations in subdomains would be a strategy for achieving diversity in motility with the conserved motor head.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceAnimalsDrosophila melanogasterHumansKinesinsMolecular Sequence DataMutationOptical TweezersProtein Structure, TertiaryKinesins

Identifiers

PMID23663840
PMCPMC3647194

What OpenQuestion holds

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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.