Evidence map›Paper›PMID 12426369›Full record

ArticleThe EMBO journal2002

Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd.

Thomas G Wendt, Niels Volkmann, Georgios Skiniotis, Kenneth N Goldie, Jens Müller, Eckhard Mandelkow, Andreas Hoenger

Abstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
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  7. Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Drosophila Ncd reveals an evolutionarily conserved powerstroke mechanism for homodimeric and heterodimeric kinesin-14s.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Review
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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

7 authors.

Thomas G WendtEuropean Molecular Biology Laboratory, Structure Programme, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
Niels Volkmann
Georgios Skiniotis
Kenneth N Goldie
Jens Müller
Eckhard Mandelkow
Andreas Hoenger

Funding

Three-dimensional Molecular Pattern RecognitionR01GM064473 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI VOLKMANN, NIELS · 2002 to 2006
$1.6M
NIGMS NIH HHS GM 64473NIGMS NIH HHS R01 GM064473
6 · The paper itself

Abstract

We used cryo-electron microscopy and image reconstruction to investigate the structure and microtubule-binding configurations of dimeric non-claret disjunctional (ncd) motor domains under various nucleotide conditions, and applied molecular docking using ncd's dimeric X-ray structure to generate a mechanistic model for force transduction. To visualize the alpha-helical coiled-coil neck better, we engineered an SH3 domain to the N-terminal end of our ncd construct (296-700). Ncd exhibits strikingly different nucleotide-dependent three-dimensional conformations and microtubule-binding patterns from those of conventional kinesin. In the absence of nucleotide, the neck adapts a configuration close to that found in the X-ray structure with stable interactions between the neck and motor core domain. Minus-end-directed movement is based mainly on two key events: (i) the stable neck-core interactions in ncd generate a binding geometry between motor and microtubule which places the motor ahead of its cargo in the minus-end direction; and (ii) after the uptake of ATP, the two heads rearrange their position relative to each other in a way that promotes a swing of the neck in the minus-end direction.

Indexed as

Cryoelectron MicroscopyAdenosine DiphosphateAdenosine TriphosphateAnimalsDrosophila ProteinsImage Processing, Computer-AssistedKinesinsMicrotubulesModels, MolecularMolecular Motor ProteinsMovementProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsSpindle ApparatusStructure-Activity RelationshipAdenosine DiphosphateAdenosine TriphosphateDrosophila ProteinsKinesinsMolecular Motor Proteinsncd protein, DrosophilaRecombinant Fusion ProteinsTubulin

Identifiers

PMID12426369
PMCPMC137211

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.