Evidence map›Paper›PMID 16450053›Full record

ReviewJournal of muscle research and cell motility2006

Review: regulation mechanisms of Kinesin-1.

Sarah Adio, Jolante Reth, Friederike Bathe, Günther Woehlke

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Dynein-Powered Cell Locomotion Guides Metastasis of Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  2. Dynein-Powered Cell Locomotion Guides Metastasis of Breast Cancer.bioRxiv : the preprint server for biology · 2023
    Article
  3. The physiological cargo adaptor of kinesin-2 functions as an evolutionary conserved lockpick.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022
    Review
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  14. Subpixel colocalization reveals amyloid precursor protein-dependent kinesin-1 and dynein association with axonal vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2012
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  20. Single molecule mechanics of the kinesin neck.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

4 authors at 3 institutions in 1 country.

Sarah AdioInstitute for Cell Biology, University of Munich, Schillerstr. 42, D-80336, Munich, Germany.
Jolante Reth
Friederike Bathe
Günther Woehlke
München Klinik · DEInstitut für Urheber- und Medienrecht · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin-1 microtubule motors are common kinesin motors from protozoa, fungi and animals. They transport vesicular or particle cargo in a strictly regulated manner. The relatively well-studied tail inhibition mechanism is based on a conformational change that leads to an interaction of Kinesin-1's tail with the junction of neck and hinge regions. This folding causes a decrease in microtubule binding and motor activity. In fungal Kinesin-1 motors several lines of evidence suggest that a conserved tyrosine in the neck coiled-coil mediates this inhibition. In the active state, a region surrounding a conserved tryptophan in the hinge stabilises the neck coiled-coil, and prevents the tyrosine from inhibiting. Although animal and fungal Kinesin-1 motors are clearly homologous and function according to the same chemo-mechanical mechanism, they differ in their regulation. Unlike fungal Kinesin-1s, animal kinesins associate with light chains that are important for regulation and cargo interaction. Several proteins interacting with animal Kinesin-1 heavy or light chains are known, among them typical scaffolding proteins that seem to link Kinesin-1 to signalling pathways.

Indexed as

AnimalsCell MovementFungiHumansKinesinsMicrotubulesSignal TransductionKinesins

Identifiers

PMID16450053
OpenAlexW1978222165

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.