Evidence map›Paper›PMID 8580344›Full record

ArticleBiophysical journal1995

Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin.

Z Wang, S Khan, M P Sheetz

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

63 citing papers in PubMed, 186 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Motor Proteins.Cold Spring Harbor perspectives in biology · 2018
    Review
  10. Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Mechanism and regulation of cytoplasmic dynein.Annual review of cell and developmental biology · 2015
    Review
  17. Article
  18. Article
  19. Article
  20. Article

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

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 at 2 institutions in 1 country.

Z WangDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
S Khan
M P Sheetz
Albert Einstein College of Medicine · USDuke Medical Center · US

Funding

MOTILITY AND CHEMOSENSING IN BACTERIAR01GM036936 · NIGMS · YESHIVA UNIVERSITY · PI KHAN, SHAHID M · 1986 to 2004
$1.1M
MOLECULAR BASIS OF ORGANELLE MOVEMENT IN AXONSR01NS023345 · NINDS · WASHINGTON UNIVERSITY · PI SHEETZ, MICHAEL P · 1986 to 2002
$651k
NIGMS NIH HHS GM36936NINDS NIH HHS NS23345
6 · The paper itself

Abstract

Cytoplasmic dynein is a major microtubule motor for minus-end directed movements including retrograde axonal transport. To better understand the mechanism by which cytoplasmic dynein converts ATP energy into motility, we have analyzed the nanometer-level displacements of latex beads coated with low numbers of cytoplasmic dynein molecules. Cytoplasmic dynein-coated beads exhibited greater lateral movements among microtubule protofilaments (ave. 5.1 times/microns of displacement) compared with kinesin (ave. 0.9 times/micron). In addition, dynein moved rearward up to 100 nm over several hundred milliseconds, often in correlation with off-axis movements from one protofilament to another. We suggest that single molecules of cytoplasmic dynein move the beads because 1) there is a linear dependence of bead motility on dynein/bead ratio, 2) the binding of beads to microtubules studied by laser tweezers is best fit by a first-order Poisson, and 3) the run length histogram of dynein beads follows a first-order decay. At the cellular level, the greater disorder of cytoplasmic dynein movements may facilitate transport by decreasing the duration of collisions between kinesin and cytoplasmic dynein-powered vesicles.

Indexed as

Adenosine TriphosphateAnimalsAxonal TransportBiophysical PhenomenaBiophysicsChick EmbryoCytoplasmDyneinsEnergy MetabolismIn Vitro TechniquesKinesinsLatexMicrospheresMovementAdenosine TriphosphateDyneinsKinesinsLatex

Identifiers

PMID8580344
PMCPMC1236434
OpenAlexW2000479770

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.