Evidence map›Paper›PMID 11606295›Full record

ArticleBiophysical journal2001

Motility of single one-headed kinesin molecules along microtubules.

Y Inoue, A H Iwane, T Miyai, E Muto, T Yanagida

Abstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Mechanism of processive movement of monomeric and dimeric kinesin molecules.International journal of biological sciences · 2010
    Review
  5. Article
  6. Article
  7. Article
  8. The diffusive interaction of microtubule binding proteins.Current opinion in cell biology · 2009
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  17. Article
  18. Coordination of kinesin's two heads studied with mutant heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

5 authors.

Y InoueSingle Molecule Processes Project, ICORP, Osaka 562-0035, Japan.
A H Iwane
T Miyai
E Muto
T Yanagida

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The motility of single one-headed kinesin molecules (K351 and K340), which were truncated fragments of Drosophila two-headed kinesin, has been tested using total internal reflection fluorescence microscopy. One-headed kinesin fragments moved continuously along the microtubules. The maximum distance traveled until the fragments dissociated from the microtubules for both K351 and K340 was approximately 600 nm. This value is considerably larger than the space resolution of the measurement system (SD approximately 30 nm). Although the movements of the fragments fluctuated in forward and backward directions, statistical analysis showed that the average movements for both K340 and K351 were toward the plus end of the microtubules, i.e., forward direction. When BDTC (a 1.3-S subunit of Propionibacterium shermanii transcarboxylase, which binds weakly to a microtubule), was fused to the tail (C-terminus) of K351, its movement was enhanced, smooth, and unidirectional, similar to that of the two-headed kinesin fragment, K411. However, the travel distance and velocity of K351BDTC molecules were approximately 3-fold smaller than that of K411. These observations suggest that a single kinesin head has basal motility, but coordination between the two heads is necessary for stabilizing the basal motility for the normal level of kinesin processivity.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsCarboxyl and Carbamoyl TransferasesDrosophilaKinesinsMicrotubulesMolecular Sequence DataMovementPeptide FragmentsPropionibacteriumAdenosine TriphosphatasesCarboxyl and Carbamoyl TransferasesKinesinsMethylmalonyl-CoA carboxytransferasePeptide Fragments

Identifiers

PMID11606295
PMCPMC1301749

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.