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The Journal of Biological Chemistry|February 28, 1997
Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubuleW Jiang, D D HackneyBiochemistry International|December 1, 1991
The mechanism of ATP hydrolysis by smooth muscle myosin and subfragments using steady state titration and 18O exchangeP K Dash, D D HackneyArchives of Biochemistry and Biophysics|August 31, 2016
Nucleotide-free kinesin motor domains reversibly convert to an inactive conformation with characteristics of a molten globuleDavid D Hackney, Marshall S McGoffThe Biochemical Journal|April 1, 1987
A residence-time analysis of enzyme kineticsJ J Sines, D D HackneyBiochemistry|December 15, 1987
Analysis of positional isotope exchange in ATP by cleavage of the beta P-O gamma P bond. Demonstration of negligible positional isotope exchange by myosinM P Dale, D D HackneyBiochemistry|June 27, 2008
Kinesin tail domains and Mg2+ directly inhibit release of ADP from head domains in the absence of microtubulesDavid D Hackney, Maryanne F StockProceedings of the National Academy of Sciences of the United States of America|July 1, 1978
Evaluation of the partitioning of bound inorganic phosphate during medium and intermediate phosphate in equilibrium water oxygen exchange reactions of yeast inorganic pyrophosphataseD D Hackney, P D BoyerThe Journal of Biological Chemistry|May 10, 1985
Steady state kinetics at high enzyme concentration. The myosin MgATPaseD D Hackney, P K ClarkProceedings of the National Academy of Sciences of the United States of America|September 1, 1984
Catalytic consequences of oligomeric organization: kinetic evidence for "tethered" acto-heavy meromyosin at low ATP concentrationsD D Hackney, P K ClarkThe Journal of Biological Chemistry|June 10, 1994
Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterizationT G Huang, D D HackneyPageof 413