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Irene Weber

Regents' Professor

B.A., Physics, Cambridge University, Cambridge, UK 1974
M.A., Physics, Cambridge University, Cambridge, UK, 1978
D. Phil., Molecular Biophysics, Oxford University, Oxford, UK, 1978
Postdoc, Yale University, 1978-1984
Research Associate, National Bureau of Standards, 1985-1987
Staff Scientist, NCI-Frederick Cancer Research Facility, 1987-1991


Protein crystallography, enzyme structures, drug design, bioinformatics.


Research Interest:

Dr. Weber is conducting research on drug resistance in HIV and structure-guided design of new protease inhibitors for AIDS. The viral-encoded protease is an important drug target for HIV/AIDS therapy. We are studying how novel inhibitors bind to HIV protease, determining the molecular basis for drug resistance by X-ray crystallography and other biophysical and biochemical assays, and developing algorithms to predict resistance from genotype sequence data. In addition, her group carries out bioinformatics, crystallographic and biochemical studies of key proteins implicated in obesity, cancer, and infectious diseases.


Recent publications:
Agniswamy J, Louis JM, Roche J, Harrison RW, Weber IT. (2016) Structural studies of a rationally selected multi-drug resistant HIV-1 protease reveal synergistic effect of distal mutations on flap dynamics. Plos One, 11(12):e0168616.
Weber IT, Harrison RW. (2017) Decoding HIV Resistance: From Genotype to Therapy. Fut. Med. Chem. 9, 1529-1538.
Sachla AJ, Ouattara M, Romero E, Agniswamy J, Weber IT, Gadda G, Eichenbaum Z. In vitro heme biotransformation by the HupZ enzyme from Group A streptococcus. (2016) Biometals. 29, 593-609.
Ghosh AK, Rao KV, Nyalapatla PR, Osswald HL, Martyr CD, Aoki M, Takayama J, Hayashi H,, Agniswamy J, Wang YF, Bulut H, Das D, Weber, IT, Mitsuya M. Design and Development of Highly Potent HIV1 Protease Inhibitors with a Crownlike Oxotricyclic Core as the P2-Ligand To Combat Multidrug-Resistant HIV Variants. (2017) J. Med. Chem 60, 4267-4278.