Evidence map›Paper›PMID 27402829›Full record

ArticleThe Journal of biological chemistry2016

The Kinesin-5 Chemomechanical Cycle Is Dominated by a Two-heads-bound State.

Geng-Yuan Chen, Keith J Mickolajczyk, William O Hancock

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

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  17. Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Review
  19. KIF15 nanomechanics and kinesin inhibitors, with implications for cancer chemotherapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

3 authors at 1 institution in 1 country.

Geng-Yuan ChenFrom the Department of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania 16802.ORCID 0000-0002-0103-4494
Keith J MickolajczykFrom the Department of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania 16802.
William O HancockFrom the Department of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania 16802 wohbio@engr.psu.edu.ORCID 0000-0001-5547-8755
Pennsylvania State University · US

Funding

Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
NIGMS NIH HHS R01 GM076476
6 · The paper itself

Abstract

Single-molecule microscopy and stopped-flow kinetics assays were carried out to understand the microtubule polymerase activity of kinesin-5 (Eg5). Four lines of evidence argue that the motor primarily resides in a two-heads-bound (2HB) state. First, upon microtubule binding, dimeric Eg5 releases both bound ADPs. Second, microtubule dissociation in saturating ADP is 20-fold slower for the dimer than for the monomer. Third, ATP-triggered mant-ADP release is 5-fold faster than the stepping rate. Fourth, ATP binding is relatively fast when the motor is locked in a 2HB state. Shortening the neck-linker does not facilitate rear-head detachment, suggesting a minimal role for rear-head-gating. This 2HB state may enable Eg5 to stabilize incoming tubulin at the growing microtubule plus-end. The finding that slowly hydrolyzable ATP analogs trigger slower nucleotide release than ATP suggests that ATP hydrolysis in the bound head precedes stepping by the tethered head, leading to a mechanochemical cycle in which processivity is determined by the race between unbinding of the bound head and attachment of the tethered head.

Indexed as

Adenosine TriphosphateAnimalsDrosophila melanogasterDrosophila ProteinsHydrolysisKinesinsMicrotubule-Associated ProteinsProtein DomainsXenopus laevisXenopus ProteinsAdenosine TriphosphateDrosophila ProteinsKIF11 protein, XenopusKinesinsKlp61F protein, DrosophilaMicrotubule-Associated ProteinsXenopus Proteinscytoskeletonkinesinmicrotubulemitotic spindlemolecular motorsingle-molecule biophysics

Identifiers

PMID27402829
PMCPMC5034029
OpenAlexW2464687182

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.