Evidence map›Paper›PMID 17200413›Full record

ArticleThe Journal of cell biology2007

Jump-starting kinesin.

David D Hackney

Abstract readComment
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The light chains of kinesin-1 are autoinhibited.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. On and around microtubules: an overview.Molecular biotechnology · 2009
    Review
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

David D HackneyDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA. ddh@andrew.cmu.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When it is not actively transporting cargo, conventional Kinesin-1 is present in the cytoplasm in a folded conformation that cannot interact effectively with microtubules (MTs). Two important and largely unexplored aspects of kinesin regulation are how it is converted to an active species when bound to cargo and the related issue of how kinesin discriminates among its many potential cargo molecules. Blasius et al. (see p. 11 of this issue) report that either binding of the cargo linker c-Jun N-terminal kinase-interacting protein 1 (JIP1) to the light chains (LCs) or binding of fasciculation and elongation protein zeta1 (FEZ1) to the heavy chains (HCs) is insufficient for activation but that activation occurs when both are present simultaneously. A related paper by Cai et al. (see p. 51 of this issue) provides structural insight into the conformation of the folded state in the cell obtained by fluorescence resonance energy transfer analysis.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsDNA-Binding ProteinsDrosophilaHumansKinesinsMicrotubule-Associated ProteinsNerve Tissue ProteinsProtein BindingProtein TransportRatsTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsFEZ1 protein, humanKinesinsLZTS1 protein, humanMAPK8IP1 protein, humanMicrotubule-Associated ProteinsNerve Tissue ProteinsTumor Suppressor Proteins

Identifiers

PMID17200413
PMCPMC2063616

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.