Evidence map›Paper›PMID 27729532›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.

Bert Nitzsche, Elzbieta Dudek, Lukasz Hajdo, Andrzej A Kasprzak, Andrej Vilfan, Stefan Diez

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  6. Torques within and outside the human spindle balance twist at anaphase.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Mechanisms underlying spindle assembly and robustness.Nature reviews. Molecular cell biology · 2023
    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

6 authors.

Bert NitzscheMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany; Center for Molecular Bioengineering (B CUBE), Technische Universität Dresden, 01069 Dresden, Germany.
Elzbieta DudekNencki Institute of Experimental Biology, 02-093 Warsaw, Poland.
Lukasz HajdoNencki Institute of Experimental Biology, 02-093 Warsaw, Poland.
Andrzej A KasprzakNencki Institute of Experimental Biology, 02-093 Warsaw, Poland.
Andrej VilfanJ. Stefan Institute, 1000 Ljubljana, Slovenia andrej.vilfan@ijs.si diez@bcube-dresden.de.ORCID 0000-0001-8985-6072
Stefan DiezMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany; Center for Molecular Bioengineering (B CUBE), Technische Universität Dresden, 01069 Dresden, Germany; andrej.vilfan@ijs.si diez@bcube-dresden.de.

Funding

European Research Council
6 · The paper itself

Abstract

Single-molecule experiments have been used with great success to explore the mechanochemical cycles of processive motor proteins such as kinesin-1, but it has proven difficult to apply these approaches to nonprocessive motors. Therefore, the mechanochemical cycle of kinesin-14 (ncd) is still under debate. Here, we use the readout from the collective activity of multiple motors to derive information about the mechanochemical cycle of individual ncd motors. In gliding motility assays we performed 3D imaging based on fluorescence interference contrast microscopy combined with nanometer tracking to simultaneously study the translation and rotation of microtubules. Microtubules gliding on ncd-coated surfaces rotated around their longitudinal axes in an [ATP]- and [ADP]-dependent manner. Combined with a simple mechanical model, these observations suggest that the working stroke of ncd consists of an initial small movement of its stalk in a lateral direction when ADP is released and a second, main component of the working stroke, in a longitudinal direction upon ATP binding.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBiological AssayBiomechanical PhenomenaCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsHumansKinesinsKineticsMicrotubulesModels, ChemicalOncogene ProteinsProtein BindingRecombinant Fusion ProteinsAdenosine DiphosphateAdenosine TriphosphateKIF14 protein, humanKinesinsOncogene ProteinsRecombinant Fusion Proteinsfluorescence interference contrast microscopygliding motility assaykinesinmathematical modelingmicrotubule

Identifiers

PMID27729532
PMCPMC5086986

What OpenQuestion holds

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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.