Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli.
Open Access
- 1 June 1994
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (23) , 16502-16507
- https://doi.org/10.1016/s0021-9258(17)34034-6
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Expression, purification, and characterization of the Drosophila kinesin motor domain produced in Escherichia coliBiochemistry, 1993
- Decoration of the microtubule surface by one kinesin head per tubulin heterodimerNature, 1993
- Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cellsThe Journal of cell biology, 1992
- Subcellular localization and sequence of sea urchin kinesin heavy chain: evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm [published erratum appears in J Cell Biol 1991 Aug;114(4):following 863]The Journal of cell biology, 1991
- The emerging kinesin family of microtubule motor proteinsTrends in Biochemical Sciences, 1991
- MOTOR PROTEINS OF CYTOPLASMIC MICROTUBULESAnnual Review of Biochemistry, 1990
- Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decorationCell, 1989
- The molecular structure of adrenal medulla kinesinCell Motility, 1989
- On the surface lattice of microtubules: helix starts, protofilament number, seam, and handedness.The Journal of cell biology, 1986
- Three-dimensional reconstruction of tubulin sheets and re-investigation of microtubule surface latticeJournal of Molecular Biology, 1983