Evidence map›Paper›PMID 10430903›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Allele-specific activators and inhibitors for kinesin.

T M Kapoor, T J Mitchison

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Allocating dissipation across a molecular machine cycle to maximize flux.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Article
  7. Analog sensitive chemical inhibition of the DEAD-box protein DDX3.Protein science : a publication of the Protein Society · 2016
    Article
  8. Article
  9. Article
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  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Article
  18. Chemical-genetic inhibition of a sensitized mutant myosin Vb demonstrates a role in peripheral-pericentriolar membrane traffic.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  19. 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

2 authors at 2 institutions in 1 country.

T M KapoorDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. Tarun_Kapoor@hms.harvard.edu
T J Mitchison
Harvard University · USSalk Institute for Biological Studies · US

Funding

MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR37GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1997 to 2006
$3.2M
NIGMS NIH HHS GM39565NIGMS NIH HHS R01 GM039565NIGMS NIH HHS R37 GM039565
6 · The paper itself

Abstract

Members of the kinesin superfamily are force-generating ATPases that drive movement and influence cytoskeleton organization in cells. Often, more than one kinesin is implicated in a cellular process, and many kinesins are proposed to have overlapping functions. By using conventional kinesin as a model system, we have developed an approach to activate or inhibit a specific kinesin allele in the presence of other similar motor proteins. Modified ATP analogs are described that do not activate either conventional kinesin or another superfamily member, Eg5. However, a kinesin allele with Arg-14 in its nucleotide binding pocket mutated to alanine can use a subset of these nucleotide analogs to drive microtubule gliding. Cyclopentyl-ATP is one such analog. Cyclopentyl-adenylylimidodiphosphate, a nonhydrolyzable form of this analog, inhibits the mutant allele in microtubule-gliding assays, but not wild-type kinesin or Eg5. We anticipate that the incorporation of kinesin mutants and allele-specific activators and inhibitors in in vitro assays should clarify the role of individual motor proteins in complex cellular processes.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAdenylyl ImidodiphosphateBinding SitesDimerizationHumansKinesinsKineticsMacromolecular SubstancesModels, MolecularMutagenesis, Site-DirectedRecombinant ProteinsStructure-Activity RelationshipAdenosine DiphosphateAdenosine TriphosphateAdenylyl ImidodiphosphateKinesinsMacromolecular SubstancesRecombinant Proteins

Identifiers

PMID10430903
PMCPMC17740
OpenAlexW2131518505

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.