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D D Hackney

Showing results (31-40 of 42) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|August 1, 1979
Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formationD D Hackney, G Rosen, P D Boyer
The Journal of Biological Chemistry|April 25, 1992
Kinesin undergoes a 9 S to 6 S conformational transitionD D Hackney, J D Levitt, J Suhan
The Journal of Biological Chemistry|June 10, 1994
Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coliT G Huang, J Suhan, D D Hackney
Biochemical and Biophysical Research Communications|January 31, 1991
Characterization of alpha 2 beta 2 and alpha 2 forms of kinesinD D Hackney, J D Levitt, D D Wagner
Methods in Enzymology|January 1, 1980
Oxygen-18 probes of enzymic reactions of phosphate compoundsD D Hackney, K E Stempel, P D Boyer
The Journal of Biological Chemistry|September 25, 1989
Nucleotide-free kinesin hydrolyzes ATP with burst kineticsD D Hackney, A S Malik, K W Wright
The Journal of Biological Chemistry|August 10, 1978
Characterization of phosphate oxygen exchange reactions catalyzed by myosin through measurement of the distribution of 18-O-labeled speciesJ A Sleep, D D Hackney, P D Boyer
The Journal of Biological Chemistry|May 10, 1980
The equivalence of phosphate oxygens for exchange and the hydrolysis characteristics revealed by the distribution of [18O]Pi species formed by myosin and actomyosin ATPaseJ A Sleep, D D Hackney, P D Boyer
The Journal of Biological Chemistry|March 21, 1997
Influence of the kinesin neck domain on dimerization and ATPase kineticsW Jiang, M F Stock, X Li, et al.
Biochemistry|January 11, 1977
Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphataseP D Boyer, L de Meis, M da Gloria Costa Carvalho, et al.
Pageof 5

Showing results (31-40 of 42) with videos related to

Sort By:
Pageof 5
Proceedings of the National Academy of Sciences of the United States of America|August 1, 1979
Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formationD D Hackney, G Rosen, P D Boyer
The Journal of Biological Chemistry|April 25, 1992
Kinesin undergoes a 9 S to 6 S conformational transitionD D Hackney, J D Levitt, J Suhan
The Journal of Biological Chemistry|June 10, 1994
Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coliT G Huang, J Suhan, D D Hackney
Biochemical and Biophysical Research Communications|January 31, 1991
Characterization of alpha 2 beta 2 and alpha 2 forms of kinesinD D Hackney, J D Levitt, D D Wagner
Methods in Enzymology|January 1, 1980
Oxygen-18 probes of enzymic reactions of phosphate compoundsD D Hackney, K E Stempel, P D Boyer
The Journal of Biological Chemistry|September 25, 1989
Nucleotide-free kinesin hydrolyzes ATP with burst kineticsD D Hackney, A S Malik, K W Wright
The Journal of Biological Chemistry|August 10, 1978
Characterization of phosphate oxygen exchange reactions catalyzed by myosin through measurement of the distribution of 18-O-labeled speciesJ A Sleep, D D Hackney, P D Boyer
The Journal of Biological Chemistry|May 10, 1980
The equivalence of phosphate oxygens for exchange and the hydrolysis characteristics revealed by the distribution of [18O]Pi species formed by myosin and actomyosin ATPaseJ A Sleep, D D Hackney, P D Boyer
The Journal of Biological Chemistry|March 21, 1997
Influence of the kinesin neck domain on dimerization and ATPase kineticsW Jiang, M F Stock, X Li, et al.
Biochemistry|January 11, 1977
Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphataseP D Boyer, L de Meis, M da Gloria Costa Carvalho, et al.
Pageof 5