The structural switch of nucleotide-free kinesin
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep42558.pdf
Reference34 articles.
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2. Coy, D. L., Wagenbach, M. & Howard, J. Kinesin takes one 8-nm step for each ATP that it hydrolyzes. J Biol Chem 274, 3667–3671 (1999).
3. Hackney, D. D. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc Natl Acad Sci USA 91, 6865–6869 (1994).
4. Kaseda, K., Higuchi, H. & Hirose, K. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat Cell Biol 5, 1079–1082 (2003).
5. Hackney, D. D. Kinesin ATPase: rate-limiting ADP release. Proc Natl Acad Sci USA 85, 6314–6318 (1988).
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