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P D Boyer

Showing results (41-50 of 138) with videos related to

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Journal of Molecular Biology|March 14, 1972
Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coliS G Chaney, P D Boyer
The Journal of Biological Chemistry|February 25, 1972
Substrate binding and reaction intermediates of glutamine synthetase (Escherichia coli W) as studied by isotope exchangesF C Wedler, P D Boyer
The Journal of Biological Chemistry|October 25, 1979
Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphataseR L Hutton, P D Boyer
European Journal of Biochemistry|October 15, 1992
The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic siteM B Murataliev, P D Boyer
Journal of Molecular Biology|April 5, 1978
Integrity of parental DNA during replicationD R Strayer, P D Boyer
The Journal of Biological Chemistry|July 10, 1982
Subunit interaction in catalysis. Some experimental and theoretical approaches with glyceraldehyde-3-phosphate dehydrogenaseJ W Cardon, P D Boyer
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1976
Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP during ATP synthesis by chloroplastsD J Smith, P D Boyer
Biochemistry|January 28, 1975
The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylationR L Cross, P D Boyer
Biochimica Et Biophysica Acta|October 24, 1990
The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic siteY M Milgrom, P D Boyer
The Journal of Biological Chemistry|October 25, 1985
The role of tightly bound ADP on chloroplast ATPaseR I Feldman, P D Boyer
Pageof 14

Showing results (41-50 of 138) with videos related to

Sort By:
Pageof 14
Journal of Molecular Biology|March 14, 1972
Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coliS G Chaney, P D Boyer
The Journal of Biological Chemistry|February 25, 1972
Substrate binding and reaction intermediates of glutamine synthetase (Escherichia coli W) as studied by isotope exchangesF C Wedler, P D Boyer
The Journal of Biological Chemistry|October 25, 1979
Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphataseR L Hutton, P D Boyer
European Journal of Biochemistry|October 15, 1992
The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic siteM B Murataliev, P D Boyer
Journal of Molecular Biology|April 5, 1978
Integrity of parental DNA during replicationD R Strayer, P D Boyer
The Journal of Biological Chemistry|July 10, 1982
Subunit interaction in catalysis. Some experimental and theoretical approaches with glyceraldehyde-3-phosphate dehydrogenaseJ W Cardon, P D Boyer
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1976
Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP during ATP synthesis by chloroplastsD J Smith, P D Boyer
Biochemistry|January 28, 1975
The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylationR L Cross, P D Boyer
Biochimica Et Biophysica Acta|October 24, 1990
The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic siteY M Milgrom, P D Boyer
The Journal of Biological Chemistry|October 25, 1985
The role of tightly bound ADP on chloroplast ATPaseR I Feldman, P D Boyer
Pageof 14