Evidence map›Paper›PMID 9755154›Full record

ArticleThe EMBO journal1998

Importance of a flexible hinge near the motor domain in kinesin-driven motility.

M Grummt, G Woehlke, U Henningsen, S Fuchs, M Schleicher, M Schliwa

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review: regulation mechanisms of Kinesin-1.Journal of muscle research and cell motility · 2006
    Review
  9. Article
  10. Article
  11. Article
  12. Breathing down the neck of Unc104.The Journal of cell biology · 2003
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Kinetic equilibrium of forces and molecular events in muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

6 authors.

M GrummtAdolf-Butenandt-Institut, Zellbiologie, University of Munich, Schillerstrasse 42, 80336 Munich, Germany.
G Woehlke
U Henningsen
S Fuchs
M Schleicher
M Schliwa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional kinesin is a molecular motor consisting of an N-terminal catalytic motor domain, an extended stalk and a small globular C-terminus. Whereas the structure and function of the catalytic motor domain has been investigated, little is known about the function of domains outside the globular head. A short coiled-coil region adjacent to the motor domain, termed the neck, is known to be important for dimerization and may be required for kinesin processivity. We now provide evidence that a helix-disrupting hinge region (hinge 1) that separates the neck from the first extended coiled-coil of the stalk plays an essential role in basic motor activity. A fast fungal kinesin from Syncephalastrum racemosum was used for these studies. Deletion, substitution by a coiled-coil and truncation of the hinge 1 region all reduce motor speed and uncouple ATP turnover from gliding velocity. Insertion of hinge 1 regions from two conventional kinesins, Nkin and DmKHC, fully restores motor activity, whereas insertion of putative flexible linkers of other proteins does not, suggesting that hinge 1 regions of conventional kinesins can functionally replace each other. We suggest that this region is essential for kinesin movement in its promotion of chemo-mechanical coupling of the two heads and therefore the functional motor domain should be redefined to include not only the catalytic head but also the adjacent neck and hinge 1 domains.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceDimerizationFungal ProteinsKinesinsMicrotubulesMolecular Motor ProteinsMolecular Sequence DataMovementMucoralesMutagenesis, InsertionalPliabilityProtein ConformationSequence DeletionAdenosine TriphosphatasesFungal ProteinsKinesinsMolecular Motor Proteins

Identifiers

PMID9755154
PMCPMC1170882

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.