Evidence map›Paper›PMID 1830666›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro.

R Urrutia, M A McNiven, J P Albanesi, D B Murphy, B Kachar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Article
  3. A small-molecule activator of kinesin-1 drives remodeling of the microtubule network.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Filament rigidity and connectivity tune the deformation modes of active biopolymer networks.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Biophysics of mitosis.Quarterly reviews of biophysics · 2012
    Review
  11. Active multistage coarsening of actin networks driven by myosin motors.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Article
  13. Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Collective alignment of polar filaments by molecular motors.The European physical journal. E, Soft matter · 2009
    Article
  16. Instabilities in a two-dimensional polar-filament--motor system.The European physical journal. E, Soft matter · 2008
    Article
  17. Article
  18. Article
  19. Nonlinear competition between asters and stripes in filament-motor systems.The European physical journal. E, Soft matter · 2005
    Article
  20. 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

5 authors at 3 institutions in 1 country.

R UrrutiaLaboratory of Cellular Biology, National Institute on Deafness and other Communication Disorders, Bethesda, MD 20892.
M A McNiven
J P Albanesi
D B Murphy
B Kachar
Johns Hopkins University · USMayo Clinic · USThe University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined the ability of kinesin to support the movement of adrenal medullary chromaffin granules on microtubules in a defined in vitro system. We found that kinesin and ATP are all that is required to support efficient (33% vesicle motility) and rapid (0.4-0.6 micron/s) translocation of secretory granule membranes on microtubules in the presence of a low-salt motility buffer. Kinesin also induced the formation of microtubule asters in this buffer, with the plus ends of microtubules located at the center of each aster. This observation indicates that kinesin is capable of promoting active sliding between microtubules toward their respective plus ends, a movement analogous to that of anaphase b in the mitotic spindle. The fact that vesicle translocation, microtubule sliding, and microtubule-dependent kinesin ATPase activities are all enhanced in low-salt buffer establishes a functional parallel between this translocator and other motility ATPases, myosin, and dynein.

Indexed as

Adenosine TriphosphatasesAdrenal MedullaAnimalsBrainCa(2+) Mg(2+)-ATPaseCattleChromaffin GranulesKinesinsKineticsMicrotubule ProteinsMicrotubulesOsmolar ConcentrationAdenosine TriphosphatasesCa(2+) Mg(2+)-ATPaseKinesinsMicrotubule Proteins

Identifiers

PMID1830666
PMCPMC52156
OpenAlexW2012810011

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.