Evidence map›Paper›PMID 17382876›Full record

ArticleCell2007

Kinesin Kar3 and Vik1 go head to head.

Günther Woehlke, Manfred Schliwa

Abstract readComment
PubMed Publisher
In one paragraph

Article in Cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Günther WoehlkeDepartment of Physics E22, Technical University Munich, Garching, Germany. guenther.woehlke@lrz.uni-muenchen.de
Manfred Schliwa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast kinesin motor protein Kar3 forms a heterodimer with a nonmotor protein Vik1. A study in this issue by Allingham et al. (2007) reveals that Vik1 unexpectedly has a structure similar to a kinesin motor domain yet lacks a nucleotide-binding site and is thus catalytically inactive. However, this does not hinder movement of the heterodimer because other features of the remarkably divergent Vik1 motor domain are retained, including the ability to bind microtubules.

Indexed as

AnimalsFungal ProteinsKinesinsMicrotubule-Associated ProteinsMicrotubulesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFungal ProteinsKAR3 protein, S cerevisiaeKinesinsMicrotubule-Associated ProteinsSaccharomyces cerevisiae ProteinsVIK1 protein, S cerevisiae

Identifiers

PMID17382876

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.