Evidence map›Paper›PMID 19751671›Full record

ArticleBiophysical journal2009

On the origin of kinesin limping.

Adrian N Fehr, Braulio Gutiérrez-Medina, Charles L Asbury, Steven M Block

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. 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
1.6field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. 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
  2. Article
  3. Kinesin rotates unidirectionally and generates torque while walking on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Coiled-coils: The long and short of it.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  5. Article
  6. Article
  7. Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  13. FRET measurements of kinesin neck orientation reveal a structural basis for processivity and asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

4 authors at 2 institutions in 1 country.

Adrian N FehrDepartment of Applied Physics, Stanford University, Stanford, California, USA.
Braulio Gutiérrez-Medina
Charles L Asbury
Steven M Block
Stanford University · USUniversity of Washington · US

Funding

MICROTUBULE MOTORS STUDIES ON A MOLECULAR SCALER01GM051453 · NIGMS · STANFORD UNIVERSITY · PI BLOCK, STEVEN M · 1994 to 2010
$4.3M
NIGMS NIH HHS R01 GM051453NIGMS NIH HHS R01-GM51453
6 · The paper itself

Abstract

Kinesin is a dimeric motor with twin catalytic heads joined to a common stalk. Kinesin molecules move processively along microtubules in a hand-over-hand walk, with the two heads advancing alternately. Recombinant kinesin constructs with short stalks have been found to "limp", i.e., exhibit alternation in the dwell times of successive steps. Limping behavior implies that the molecular rearrangements underlying even- and odd-numbered steps must differ, but the mechanism by which such rearrangements lead to limping remains unsolved. Here, we used an optical force clamp to measure individual, recombinant dimers and test candidate explanations for limping. Introducing a covalent cross-link into the stalk region near the heads had no effect on limping, ruling out possible stalk misregistration during coiled-coil formation as a cause. Limping was equally unaffected by mutations that produced 50-fold changes in stalk stiffness, ruling out models where limping arises from an asymmetry in torsional strain. However, limping was enhanced by perturbations that increased the vertical component of load on the motor, including increases in bead size or net load, and decreases in the stalk length. These results suggest that kinesin heads take different vertical trajectories during alternate steps, and that the rates for these motions are differentially sensitive to load.

Indexed as

MovementAmino Acid SequenceAnimalsDrosophila melanogasterHumansKinesinsMicrospheresMicrotubulesModels, BiologicalMolecular Sequence DataProtein Structure, SecondaryTemperatureKinesins

Identifiers

PMID19751671
PMCPMC2749785
OpenAlexW2163652921

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.