Evidence map›Paper›PMID 16873064›Full record

ArticleCell2006

Single-molecule analysis of dynein processivity and stepping behavior.

Samara L Reck-Peterson, Ahmet Yildiz, Andrew P Carter, Arne Gennerich, Nan Zhang, Ronald D Vale

Abstract readComparative Study
In one paragraph

Article in Cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 298 papers.

0numbers the graph read from it
0cells of the map it votes in
298citing 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

298 citing papers in PubMed.

  1. Article
  2. Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Programming DNA machines to move.Nature reviews. Chemistry · 2026
    Review
  8. Article
  9. Article
  10. Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025
    Article
  11. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Stepping dynamics of dynein characterized by MINFLUX.bioRxiv : the preprint server for biology · 2024
    Article
  20. Article

238 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Samara L Reck-PetersonDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.
Ahmet Yildiz
Andrew P Carter
Arne Gennerich
Nan Zhang
Ronald D Vale

Funding

STRUCTURE/FUNCTION OF MOLECULAR MOTORSP01AR042895 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FLETTERICK, ROBERT J · 1994 to 2008
$9.8M
Molecular Dissection of Cytoplasmic DyneinF32GM067403 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI RECK-PETERSON, SAMARA L · 2003 to 2005
$121k
Howard Hughes Medical InstituteNIAMS NIH HHS P01 AR042895NIAMS NIH HHS P01-AR42895NIGMS NIH HHS F32 GM067403NIGMS NIH HHS F32-GM67403-02
6 · The paper itself

Abstract

Cytoplasmic dynein, the 1.2 MDa motor driving minus-end-directed motility, has been reported to move processively along microtubules, but its mechanism of motility remains poorly understood. Here, using S. cerevisiae to produce recombinant dynein with a chemically controlled dimerization switch, we show by structural and single-molecule analysis that processivity requires two dynein motor domains but not dynein's tail domain or any associated subunits. Dynein advances most frequently in 8 nm steps, although longer as well as side and backward steps are observed. Individual motor domains show a different stepping pattern, which is best explained by the two motor domains shuffling in an alternating manner between rear and forward positions. Our results suggest that cytoplasmic dynein moves processively through the coordination of its two motor domains, but its variable step size and direction suggest a considerable diffusional component to its step, which differs from Kinesin-1 and is more akin to myosin VI.

Indexed as

Amino Acid SequenceCytoplasmDiffusionDimerizationDyneinsGlutathione TransferaseGreen Fluorescent ProteinsKinesinsMicrotubulesModels, BiologicalMolecular Motor ProteinsMolecular Sequence DataMyosin Heavy ChainsProtein Structure, TertiaryQuantum DotsRecombinant ProteinsDyneinsGlutathione TransferaseGreen Fluorescent ProteinsKinesinsMolecular Motor ProteinsMyosin Heavy Chainsmyosin VIRecombinant Proteins

Identifiers

PMID16873064
PMCPMC2851639

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.