Evidence map›Paper›PMID 9634584›Full record

ArticleThe Plant cell1998

Characterization of microtubule binding domains in the Arabidopsis kinesin-like calmodulin binding protein.

S B Narasimhulu, A S Reddy

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. A New Allele of theFrontiers in plant science · 2019
    Article
  3. Article
  4. Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Characterization of a myosin VII MyTH/FERM domain.Journal of molecular biology · 2011
    Article
  11. An unconventional myosin required for cell polarization and chemotaxis.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  12. Article
  13. Structure of the complex of a mitotic kinesin with its calcium binding regulator.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Article
  16. Article
  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

2 authors at 1 institution in 1 country.

S B NarasimhuluDepartment of Biology and Program in Cell and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523, USA.
A S Reddy
Colorado State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kinesin-like calmodulin binding protein (KCBP) is a new member of the kinesin superfamily that appears to be present only in plants. The KCBP is unique in its ability to interact with calmodulin in a Ca2+-dependent manner. To study the interaction of the KCBP with microtubules, we expressed different regions of the Arabidopsis KCBP and used the purified proteins in cosedimentation assays with microtubules. The motor domain with or without the calmodulin binding domain bound to microtubules. The binding of the motor domain containing the calmodulin binding region to microtubules was inhibited by Ca2+-calmodulin. This Ca2+-calmodulin regulation of motor domain interactions with microtubules was abolished in the presence of antibodies specific to the calmodulin binding region. In addition, the binding of the motor domain lacking the calmodulin binding region to microtubules was not inhibited in the presence of Ca2+-calmodulin, suggesting an essential role for the calmodulin binding region in Ca2+-calmodulin modulation. Results of the cosedimentation assays with the N-terminal tail suggest the presence of a second microtubule binding site on the KCBP. However, the interaction of the N-terminal tail region of the KCBP with microtubules was insensitive to ATP. These data on the interaction of the KCBP with microtubules provide new insights into the functioning of the KCBP in plants.

Indexed as

Arabidopsis ProteinsAnimalsArabidopsisBinding SitesBrainCalciumCalmodulinCalmodulin-Binding ProteinsCattleKinesinsMicrotubulesPlant ProteinsRecombinant ProteinsTubulinArabidopsis ProteinsCalciumCalmodulinCalmodulin-Binding ProteinsKCBP protein, ArabidopsisKinesinsPlant ProteinsRecombinant ProteinsTubulin

Identifiers

PMID9634584
PMCPMC144043
OpenAlexW2143472220

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.