Biochemistry, Enzyme, ATP synthase, Biophysics and Oxidative phosphorylation are his primary areas of study. The concepts of his Enzyme study are interwoven with issues in Endoplasmic reticulum and Adenosine triphosphate. His study in ATP synthase is interdisciplinary in nature, drawing from both Protein subunit, ATP synthase alpha/beta subunits, ATP synthase gamma subunit, ATP Synthetase Complexes and Protein structure.
He interconnects ATPase and Photophosphorylation in the investigation of issues within ATP synthase alpha/beta subunits. In his study, which falls under the umbrella issue of ATP synthase gamma subunit, Chemiosmosis is strongly linked to Stereochemistry. His Biophysics study integrates concerns from other disciplines, such as Electrochemical gradient, Oxygen and Oligomycin.
His main research concerns Biochemistry, Enzyme, ATPase, ATP synthase and Biophysics. His work on Biochemistry deals in particular with Nucleotide, Adenosine triphosphate, Oxidative phosphorylation, ATP hydrolysis and Phosphorylation. As a member of one scientific family, Paul D. Boyer mostly works in the field of Enzyme, focusing on Binding site and, on occasion, Peptide sequence.
His ATPase research incorporates themes from Stereochemistry, Phosphate, Catalysis and Adenine nucleotide. His ATP synthase study incorporates themes from Photophosphorylation, ATP synthase alpha/beta subunits, ATP synthase gamma subunit, ATP Synthetase Complexes and Protein structure. His study explores the link between Biophysics and topics such as Oxygen that cross with problems in Photochemistry and Molecule.
Paul D. Boyer mostly deals with Biochemistry, ATPase, Enzyme, ATP synthase and Nucleotide. His Biochemistry research is multidisciplinary, incorporating perspectives in Molecular biology and Biophysics. His studies in ATPase integrate themes in fields like Cleavage, Stereochemistry and Phosphate.
The study incorporates disciplines such as Hydrolysis, Chloroplast and Escherichia coli in addition to Enzyme. His ATP synthase research is multidisciplinary, relying on both Photophosphorylation, ATP synthase alpha/beta subunits, ATP synthase gamma subunit, ATP Synthetase Complexes and Protein structure. His work in Nucleotide addresses issues such as GTP', which are connected to fields such as GTPase and Guanosine.
Biochemistry, ATP synthase, Enzyme, ATPase and ATP synthase alpha/beta subunits are his primary areas of study. His Biochemistry research is mostly focused on the topic Nucleotide. His ATP synthase study combines topics from a wide range of disciplines, such as Protein structure, Protein subunit and ATP Synthetase Complexes.
His Enzyme research is multidisciplinary, incorporating elements of Oxidative phosphorylation, Bioenergetics and Molecular machine. In his study, Chemiosmosis, V-ATPase and Thylakoid is strongly linked to Photophosphorylation, which falls under the umbrella field of ATPase. While the research belongs to areas of ATP synthase alpha/beta subunits, Paul D. Boyer spends his time largely on the problem of ATP hydrolysis, intersecting his research to questions surrounding Adenylate kinase.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
The ATP Synthase—A Splendid Molecular Machine
Paul D. Boyer.
Annual Review of Biochemistry (1997)
The binding change mechanism for ATP synthase — Some probabilities and possibilities
Paul D. Boyer.
Biochimica et Biophysica Acta (1993)
Oxidative phosphorylation and photophosphorylation
Paul D. Boyer;Britton Chance;Lars Ernster;Peter Mitchell.
Annual Review of Biochemistry (1977)
Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.
M J Gresser;J A Myers;P D Boyer.
Journal of Biological Chemistry (1982)
A New Concept for Energy Coupling in Oxidative Phosphorylation Based on a Molecular Explanation of the Oxygen Exchange Reactions
P. D. Boyer;R. L. Cross;W. Momsen.
Proceedings of the National Academy of Sciences of the United States of America (1973)
A perspective of the binding change mechanism for ATP synthesis.
Paul D. Boyer.
The FASEB Journal (1989)
A Borohydride Reduction Method for Characterization of the Acyl Phosphate Linkage in Proteins and Its Application to Sarcoplasmic Reticulum Adenosine Triphosphatase
Chemda Degani;Paul D. Boyer.
Journal of Biological Chemistry (1973)
An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions.
C Kayalar;J Rosing;P D Boyer.
Journal of Biological Chemistry (1977)
Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles
Tohru Kanazawa;Paul D. Boyer.
Journal of Biological Chemistry (1973)
A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport.
Paul D. Boyer.
FEBS Letters (1975)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
University of California, San Francisco
University of Pennsylvania
Stockholm University
Rockefeller University
University of Rochester Medical Center
University of California, Los Angeles
Cold Spring Harbor Laboratory
Stanford University
University of Toronto
California Institute of Technology
IBM (United States)
Federal University of Rio de Janeiro
National University of Defense Technology
Chinese Academy of Sciences
University of Arkansas for Medical Sciences
Chinese Academy of Sciences
KU Leuven
University of Florida
University of Alaska Fairbanks
National Research Council (CNR)
United States Naval Research Laboratory
University of Oxford
University of California, Davis
Sciences Po
Stanford University
University of Rochester