Evidence map›Paper›PMID 18037705›Full record

ArticleThe Journal of biological chemistry2008

Getting in sync with dimeric Eg5. Initiation and regulation of the processive run.

Troy C Krzysiak, Michael Grabe, Susan P Gilbert

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Kinesin-2 KIF3AB exhibits novel ATPase characteristics.The Journal of biological chemistry · 2014
    Article
  12. Prime movers: the mechanochemistry of mitotic kinesins.Nature reviews. Molecular cell biology · 2014
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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.

Troy C KrzysiakDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Michael Grabe
Susan P Gilbert

Funding

Mechanistic Analysis Of Microtubule Based MotorsR01GM054141 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GILBERT, SUSAN P. · 1996 to 2012
$3.8M
Mechanistic Analysis of Microtubule-Based MotorsK02AR047841 · NIAMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GILBERT, SUSAN P. · 2002 to 2006
$509k
NIAMS NIH HHS K02 AR047841NIAMS NIH HHS K02-AR47841NIGMS NIH HHS R01 GM054141NIGMS NIH HHS R01-GM54141
6 · The paper itself

Abstract

Eg5/KSP is the kinesin-related motor protein that generates the major plus-end directed force for mitotic spindle assembly and dynamics. Recent work using a dimeric form of Eg5 has found it to be a processive motor; however, its mechanochemical cycle is different from that of conventional Kinesin-1. Dimeric Eg5 appears to undergo a conformational change shortly after collision with the microtubule that primes the motor for its characteristically short processive runs. To better understand this conformational change as well as head-head communication during processive stepping, equilibrium and transient kinetic approaches have been used. By contrast to the mechanism of Kinesin-1, microtubule association triggers ADP release from both motor domains of Eg5. One motor domain releases ADP rapidly, whereas ADP release from the other occurs after a slow conformational change at approximately 1 s(-1). Therefore, dimeric Eg5 begins its processive run with both motor domains associated with the microtubule and in the nucleotide-free state. During processive stepping however, ATP binding and potentially ATP hydrolysis signals rearward head advancement 16 nm forward to the next microtubule-binding site. This alternating cycle of processive stepping is proposed to terminate after a few steps because the head-head communication does not sufficiently control the timing to prevent both motor domains from entering the ADP-bound state simultaneously.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateDimerizationHumansHydrolysisKinesinsProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsSpindle ApparatusTime FactorsTubulinAdenosine DiphosphateAdenosine TriphosphateKIF11 protein, humanKinesinsRecombinant ProteinsTubulin

Identifiers

PMID18037705
PMCPMC2265775

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.