David K. Stammers

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• DNA

David K. Stammers mainly focuses on Reverse transcriptase, Drug resistance, Stereochemistry, Biochemistry and Binding site. His Reverse transcriptase study combines topics in areas such as Protein subunit, Molecular biology, Hydrogen bond, Nucleoside and Nucleotidyltransferase. His studies deal with areas such as Transferase and Virology as well as Drug resistance.

His work carried out in the field of Stereochemistry brings together such families of science as Protein structure, Hydroxylation, Polymerase and Active site. His work in Protein structure addresses issues such as Crystallography, which are connected to fields such as Beta sheet and Triosephosphate isomerase. Much of his study explores Biochemistry relationship to Cell biology.

His most cited work include:

• Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. (393 citations)
• Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. (377 citations)
• Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors (278 citations)

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

His primary areas of investigation include Biochemistry, Reverse transcriptase, Stereochemistry, Virology and Binding site. His Reverse transcriptase research is multidisciplinary, incorporating elements of Mutation, Molecular biology, Nucleoside, Drug resistance and Nucleotidyltransferase. His work deals with themes such as Drug and Reverse-transcriptase inhibitor, which intersect with Drug resistance.

His work carried out in the field of Stereochemistry brings together such families of science as Crystallography and Enzyme, Substrate, Dihydrofolate reductase, Active site. David K. Stammers combines subjects such as Mutant and Crystal structure with his study of Virology. His study on Binding site also encompasses disciplines like

• Plasma protein binding which is related to area like Potency,
• Oxidoreductase which is related to area like Oxygenase.

He most often published in these fields:

• Biochemistry (43.02%)
• Reverse transcriptase (37.79%)
• Stereochemistry (30.81%)

What were the highlights of his more recent work (between 2005-2013)?

• Biochemistry (43.02%)
• Binding site (22.67%)
• Protein structure (16.28%)

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

His main research concerns Biochemistry, Binding site, Protein structure, Virology and Stereochemistry. In his study, Transcription, Adenosine triphosphate and Threonine is strongly linked to Plasma protein binding, which falls under the umbrella field of Binding site. The Protein structure study combines topics in areas such as Amino acid, Transferase, Crystallography, Salmonella enterica and Neisseria.

His Virology research integrates issues from Wild type, Reverse transcriptase and Drug resistance. His work in Reverse transcriptase covers topics such as Nucleoside which are related to areas like Thymidine kinase and Molecular biology. His research integrates issues of Thymine, Tetramer and ACT domain in his study of Stereochemistry.

Between 2005 and 2013, his most popular works were:

• Structure-activity relationship studies of novel benzophenones leading to the discovery of a potent, next generation HIV nonnucleoside reverse transcriptase inhibitor. (136 citations)
• Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase. (120 citations)
• Calcium regulation of chloroplast protein translocation is mediated by calmodulin binding to Tic32 (105 citations)

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

• Enzyme
• Gene
• DNA

David K. Stammers mainly investigates Biochemistry, Drug resistance, Virology, Binding site and Reverse transcriptase. While the research belongs to areas of Drug resistance, David K. Stammers spends his time largely on the problem of Reverse-transcriptase inhibitor, intersecting his research to questions surrounding Wild type and Enzyme inhibitor. His research in Binding site tackles topics such as Plasma protein binding which are related to areas like Potency, Transport protein and Calmodulin.

His Reverse transcriptase study integrates concerns from other disciplines, such as Mutant and Nucleoside. His work in Mutant addresses subjects such as Protein subunit, which are connected to disciplines such as Mutation. His Protein structure research focuses on subjects like Biosynthesis, which are linked to Stereochemistry.