William R. Montfort

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Biochemistry
• Amino acid

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.

His most cited work include:

• Properties and Biological Activities of Thioredoxins (391 citations)
• The Three-dimensional Structure of Ricin at 2.8 A* (325 citations)
• Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. (308 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

• Stereochemistry (33.33%)
• Crystallography (31.01%)
• Crystal structure (26.36%)

What were the highlights of his more recent work (between 2010-2021)?

• Biochemistry (25.58%)
• Soluble guanylyl cyclase (9.30%)
• Heme (23.26%)

In recent papers he was focusing on the following fields of study:

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.

Between 2010 and 2021, his most popular works were:

• Evolution in an Ancient Detoxification Pathway Is Coupled with a Transition to Herbivory in the Drosophilidae (60 citations)
• Structure and Activation of Soluble Guanylyl Cyclase, the Nitric Oxide Sensor. (59 citations)
• Crystal Structures of Multicopper Oxidase CueO Bound to Copper(I) and Silver(I): FUNCTIONAL ROLE OF A METHIONINE-RICH SEQUENCE, (57 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• DNA
• Amino acid

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.