ArticlePlant molecular biology1996
Cell cycle-dependent accumulation of a kinesin-like protein, KatB/C in synchronized tobacco BY-2 cells.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 44 citations in OpenAlex.
- Function and Characteristic Analysis of Candidate PEAR Proteins inInternational journal of molecular sciences · 2023Article
- Localization of two homologous Arabidopsis kinesin-related proteins in the phragmoplast.Planta · 2004Article
- Genome-wide identification of Arabidopsis coiled-coil proteins and establishment of the ARABI-COIL database.Plant physiology · 2004Article
- The cotton kinesin-like calmodulin-binding protein associates with cortical microtubules in cotton fibers.Plant physiology · 2003Article
- A novel plant kinesin-related protein specifically associates with the phragmoplast organelles.The Plant cell · 2001Article
- Identification of a novel plant-specific kinesin-like protein that is highly expressed in interphase tobacco BY-2 cells.Protoplasma · 2001Article
- Identification and characterization of a novel microtubule-based motor associated with membranous organelles in tobacco pollen tubes.The Plant cell · 2000Article
- Genetic dissection of cytokinesis.Plant molecular biology · 2000Review
- Cell cycle regulation of the microtubular cytoskeleton.Plant molecular biology · 2000Review
- The kinesin-like calmodulin binding protein is differentially involved in cell division.The Plant cell · 2000Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoblot analysis with antibodies prepared against highly purified recombinant truncated kinesin-like proteins, KatB(5-249) and KatC(207-754), encoded by the katB and katC genes of Arabidopsis thaliana revealed the presence of a kinesin-like polypeptide, termed KatB/C, in cultured tobacco BY-2 cells. The KatB/C polypeptide cosedimented with microtubules in the presence of a nonhydrolyzable ATP analogue and was released from microtubules in the presence of ATP, both of which are characteristics of kinesin proteins. The amount of KatB/C polypeptide in synchronous BY-2 cells increased during M phase of the cell cycle. Microtubule-based structures present in cells at M phase, such as the spindle and phragmoplast, may be the site of action of the KatB/C protein.
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