A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
- 1 March 1989
- Vol. 56 (5) , 879-889
- https://doi.org/10.1016/0092-8674(89)90692-2
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extractsCell, 1988
- Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptideBiochemistry, 1988
- A non-AUG translational initiation in c-myc exon 1 generates an N-terminally distinct protein whose synthesis is disrupted in Burkitt's lymphomasCell, 1988
- Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail.The Journal of cell biology, 1987
- Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesinNature, 1987
- Comparison of the consensus sequence flanking translational start sites inDrosophilaand vertebratesNucleic Acids Research, 1987
- Identification of a MAP 2-like ATP-binding protein associated with axoplasmic vesicles that translocate on isolated microtubules.The Journal of cell biology, 1986
- A novel brain ATPase with properties expected for the fast axonal transport motorNature, 1985
- A comprehensive set of sequence analysis programs for the VAXNucleic Acids Research, 1984
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978