William R. Montfort focuses on Biochemistry, Stereochemistry, Crystallography, Nitrophorin and Thioredoxin. In general Biochemistry, his work in Enzyme is often linked to Copper toxicity linking many areas of study. The study incorporates disciplines such as Hydrogen bond, Binding site and Active site in addition to Stereochemistry.
His work focuses on many connections between Crystallography and other disciplines, such as Amino acid, that overlap with his field of interest in Crystal structure and Resolution. His Nitrophorin study is concerned with the larger field of Heme. His Thioredoxin reductase research includes themes of Cell growth and Cytosol.
The scientist’s investigation covers issues in Stereochemistry, Crystallography, Crystal structure, Biochemistry and Nitrophorin. His work is dedicated to discovering how Stereochemistry, Active site are connected with Cofactor and other disciplines. His Crystallography research includes elements of Protein structure, Conformational isomerism and Conformational change.
His biological study spans a wide range of topics, including Nitrophorin 4, Rhodnius prolixus and Resolution. His Biochemistry study frequently involves adjacent topics like Manduca sexta. His Nitrophorin research incorporates themes from Nitric oxide transport, Nitric oxide binding and Inorganic chemistry.
His primary areas of study are Biochemistry, Soluble guanylyl cyclase, Heme, Cimex lectularius and Cyclase activity. In general Biochemistry study, his work on Guanylate cyclase 2C and Hemeprotein often relates to the realm of Energy transfer, thereby connecting several areas of interest. Specifically, his work in Hemeprotein is concerned with the study of Nitrophorin.
William R. Montfort interconnects Biophysics, Shewanella oneidensis, Binding site and Histidine in the investigation of issues within Heme. His Cyclase research is multidisciplinary, relying on both Protein structure, Stereochemistry and Active site. His research in Stereochemistry intersects with topics in Protein engineering and Aldol reaction.
William R. Montfort mainly focuses on Stereochemistry, Heme, Soluble guanylyl cyclase, Cyclase and Histidine. His Stereochemistry study incorporates themes from Protein structure, Protein engineering and Serine. His Protein structure research is multidisciplinary, incorporating perspectives in Aldol reaction, GTP', Lactone and Active site.
Heme is the subject of his research, which falls under Biochemistry. His work in the fields of Biochemistry, such as Myoglobin and Guanylate cyclase 2C, overlaps with other areas such as Peroxynitrite and Ferrous. His Histidine study integrates concerns from other disciplines, such as Oxidoreductase, Oxidase test, Enzyme kinetics and Methionine.
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Properties and Biological Activities of Thioredoxins
Garth Powis;William R Montfort.
Annual Review of Pharmacology and Toxicology (2001)
The Three-dimensional Structure of Ricin at 2.8 A*
W. Montfort;J.E. Villafranca;A.F. Monzingo;S.R. Ernst.
Journal of Biological Chemistry (1987)
Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.
Andrzej Weichsel;John R Gasdaska;Garth Powis;William R Montfort.
Structure (1996)
Atomic structure of thymidylate synthase: target for rational drug design
Larry W. Hardy;Janet S. Finer-Moore;William R. Montfort;Melvin O. Jones.
Science (1987)
Crystal Structure and Electron Transfer Kinetics of CueO, a Multicopper Oxidase Required for Copper Homeostasis in Escherichia coli
Sue A. Roberts;Andrzej Weichsel;Gregor Grass;Keshari Thakali.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif.
Walter H. Watson;Jan Pohl;William R. Montfort;Olga Stuchlik.
Journal of Biological Chemistry (2003)
Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate.
William R. Montfort;Kathy M. Perry;Eric B. Fauman;Janet S. Finer-Moore.
Biochemistry (1990)
Cuprous oxidase activity of CueO from Escherichia coli.
Satish K. Singh;Gregor Grass;Christopher Rensing;William R. Montfort.
Journal of Bacteriology (2004)
Crystal structures of a nitric oxide transport protein from a blood-sucking insect
A. Weichsel;J.F. Andersen;D.E. Champagne;F.A. Walker.
Nature Structural & Molecular Biology (1998)
Plastic adaptation toward mutations in proteins: Structural comparison of thymidylate synthases
Kathy M. Perry;Eric B. Fauman;Janet S. Finer-Moore;William R. Montfort.
Proteins (1990)
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