S Gulnik

Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.

T. Bhat, S. Gulnik, B. Liu, 1995, Structure.

Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy.

C. Boucher, S. Gulnik, J. Erickson, 1999, AIDS.

Drug-resistant HIV-1 proteases identify enzyme residues important for substrate selection and catalytic rate.

A Wlodawer, A. Wlodawer, I. Weber, 1998, Biochemistry.

Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.

R E Cachau, T. Bhat, J. Collins, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Structure of human cathepsin D: comparison of inhibitor binding and subdomain displacement with other aspartic proteases.

T. Bhat, S. Gulnik, J. Erickson, 1995, Advances in experimental medicine and biology.