Evidence map›Paper›PMID 8704162›Full record

ArticlePlant molecular biology1996

A novel kinesin-like protein with a calmodulin-binding domain.

W Wang, D Takezawa, S B Narasimhulu, A S Reddy, B W Poovaiah

Abstract read
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In one paragraph

Article in Plant molecular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Microtubule-associated proteins in higher plants.Journal of plant research · 2007
    Review
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  7. Article
  8. Article
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  13. Review
  14. Article
  15. Article
  16. Neocentromere-mediated chromosome movement in maize.The Journal of cell biology · 1997
    Article
  17. In vitro motility of AtKCBP, a calmodulin-binding kinesin protein of Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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 at 2 institutions in 1 country.

W WangDepartment of Horticulture, Washington State University, Pullman 99164-6414, USA.
D Takezawa
S B Narasimhulu
A S Reddy
B W Poovaiah
Washington State University · USColorado State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium regulates diverse developmental processes in plants through the action of calmodulin. A cDNA expression library from developing anthers of tobacco was screened with 35S-labeled calmodulin to isolate cDNAs encoding calmodulin-binding proteins. Among several clones isolated, a kinesin-like gene (TCK1) that encodes a calmodulin-binding kinesin-like protein was obtained. The TCK1 cDNA encodes a protein with 1265 amino acid residues. Its structural features are very similar to those of known kinesin heavy chains and kinesin-like proteins from plants and animals, with one distinct exception. Unlike other known kinesin-like proteins, TCK1 contains a calmodulin-binding domain which distinguishes it from all other known kinesin genes. Escherichia coli-expressed TCK1 binds calmodulin in a Ca(2+)-dependent manner. In addition to the presence of a calmodulin-binding domain at the carboxyl terminal, it also has a leucine zipper motif in the stalk region. The amino acid sequence at the carboxyl terminal of TCK1 has striking homology with the mechanochemical motor domain of kinesins. The motor domain has ATPase activity that is stimulated by microtubules. Southern blot analysis revealed that TCK1 is coded by a single gene. Expression studies indicated that TCK1 is expressed in all of the tissues tested. Its expression is highest in the stigma and anther, especially during the early stages of anther development. Our results suggest that Ca2+/calmodulin may play an important role in the function of this microtubule-associated motor protein and may be involved in the regulation of microtubule-based intracellular transport.

Indexed as

Plants, ToxicAdenosine TriphosphatasesAmino Acid SequenceAnimalsBase SequenceCalciumCalmodulinCalmodulin-Binding ProteinsDNA, ComplementaryEscherichia coliKinesinsMolecular Sequence DataNicotianaPlant ProteinsProtein BindingProtein Structure, SecondaryAdenosine TriphosphatasesCalciumCalmodulinCalmodulin-Binding ProteinsDNA, ComplementaryKinesinsPlant ProteinsTCK1 protein, Nicotiana tabacumNASA Discipline Number 40-50NASA Discipline Plant BiologyNASA Program Space BiologyNon-NASA Center

Identifiers

PMID8704162
OpenAlexW1991829311

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.