Evidence map›Paper›PMID 19805111›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Direct measurements of kinesin torsional properties reveal flexible domains and occasional stalk reversals during stepping.

Braulio Gutiérrez-Medina, Adrian N Fehr, Steven M Block

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Molecular mechanisms of the interhead coordination by interhead tension in cytoplasmic dyneins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. 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
  8. Article
  9. Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Torque measurement at the single-molecule level.Annual review of biophysics · 2013
    Review
  14. Article
  15. A universal pathway for kinesin stepping.Nature structural & molecular biology · 2011
    Article
  16. Review
  17. 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

3 authors.

Braulio Gutiérrez-MedinaDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Adrian N Fehr
Steven M Block

Funding

MICROTUBULE MOTORS STUDIES ON A MOLECULAR SCALER01GM051453 · NIGMS · STANFORD UNIVERSITY · PI BLOCK, STEVEN M · 1994 to 2010
$4.3M
NIGMS NIH HHS R01 GM051453
6 · The paper itself

Abstract

Kinesin is a homodimeric motor with two catalytic heads joined to a stalk via short neck linkers (NLs). We measured the torsional properties of single recombinant molecules by tracking the thermal angular motions of fluorescently labeled beads bound to the C terminus of the stalk. When kinesin heads were immobilized on microtubules (MTs) under varied nucleotide conditions, we observed bounded or unbounded angular diffusion, depending on whether one or both heads were attached to the MT. Free rotation implies that NLs act as swivels. From data on constrained diffusion, we conclude that the coiled-coil stalk domains are approximately 30-fold stiffer than its flexible "hinge" regions. Surprisingly, while tracking processive kinesin motion at low ATP concentrations, we observed occasional abrupt reversals in the directional orientations of the stalk. Our results impose constraints on kinesin walking models and suggest a role for rotational freedom in cargo transport.

Indexed as

Protein Structure, TertiaryAdenosine TriphosphateAnimalsBinding SitesDrosophila melanogasterDrosophila ProteinsKinesinsKineticsMicrotubulesModels, MolecularMolecular Motor ProteinsProtein BindingProtein MultimerizationRotationAdenosine TriphosphateDrosophila ProteinsKinesinsMolecular Motor Proteins

Identifiers

PMID19805111
PMCPMC2761353

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.