What is she best known for?
The fields of study she is best known for:
Irene T. Weber mainly focuses on Protease, HIV-1 protease, Stereochemistry, Binding site and HIV Protease Inhibitor.
Her Protease research focuses on Proteases and how it connects with Homology modeling, Rous sarcoma virus and Wild type.
The various areas that Irene T. Weber examines in her HIV-1 protease study include Mutant and Enzyme inhibitor.
The Stereochemistry study combines topics in areas such as Crystallography, Beta sheet and Hydrogen bond.
Her Binding site research is under the purview of Biochemistry.
The concepts of her HIV Protease Inhibitor study are interwoven with issues in Darunavir and Saquinavir.
Her most cited work include:
- Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro (305 citations)
- Predicted structures of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites. (112 citations)
- Geometric criteria of hydrogen bonds in proteins and identification of "bifurcated" hydrogen bonds. (109 citations)
What are the main themes of her work throughout her whole career to date?
Her main research concerns Protease, HIV-1 protease, Stereochemistry, Biochemistry and HIV Protease Inhibitor.
Her Protease research includes themes of Darunavir, Mutant and Virology.
Her Darunavir research focuses on Saquinavir and how it relates to Protease inhibitor.
In her study, Protein structure and Dissociation constant is strongly linked to Crystallography, which falls under the umbrella field of HIV-1 protease.
Her biological study spans a wide range of topics, including Hydrolase, Active site, Substrate, Hydrogen bond and Binding site.
Irene T. Weber combines subjects such as Potency and Enzyme inhibitor with her study of HIV Protease Inhibitor.
She most often published in these fields:
- Protease (47.57%)
- HIV-1 protease (38.92%)
- Stereochemistry (37.84%)
What were the highlights of her more recent work (between 2013-2021)?
- Protease (47.57%)
- HIV-1 protease (38.92%)
- Stereochemistry (37.84%)
In recent papers she was focusing on the following fields of study:
Irene T. Weber mostly deals with Protease, HIV-1 protease, Stereochemistry, HIV Protease Inhibitor and Active site.
Her Protease research is classified as research in Biochemistry.
Irene T. Weber has included themes like Hydrolase, Darunavir and Hydrogen bond in her HIV-1 protease study.
Her Stereochemistry research is multidisciplinary, incorporating elements of Design synthesis, Protein structure, Biological evaluation, Structure–activity relationship and Binding site.
Her research in HIV Protease Inhibitor intersects with topics in Proteases and Potency.
Her Active site study incorporates themes from Oxidoreductase, Cofactor, Flavin group and Molecular mechanics.
Between 2013 and 2021, her most popular works were:
- Design and Development of Highly Potent HIV-1 Protease Inhibitors with a Crown-Like Oxotricyclic Core as the P2-Ligand To Combat Multidrug-Resistant HIV Variants (36 citations)
- Highly resistant HIV-1 proteases and strategies for their inhibition (36 citations)
- Long-Range Electrostatics-Induced Two-Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site. (30 citations)
In her most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Protease, HIV-1 protease, Stereochemistry, Active site and HIV Protease Inhibitor.
Her Protease research is multidisciplinary, incorporating perspectives in Wild type, Aspartic acid and Virology.
Her HIV-1 protease research includes elements of Darunavir and Binding site.
As part of one scientific family, Irene T. Weber deals mainly with the area of Stereochemistry, narrowing it down to issues related to the Protein structure, and often Oxidoreductase, Substrate, Drug resistance, Crystallography and Amprenavir.
While the research belongs to areas of Active site, Irene T. Weber spends her time largely on the problem of Hydrolase, intersecting her research to questions surrounding Mutation and Hydrogen bond.
Her studies in HIV Protease Inhibitor integrate themes in fields like Proteases, Potency, Orders of magnitude, AIDS therapy and Drug target.
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.
