R. De Gori

Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries.

P. Hudson, S. Nuttall, U. Krishnan, 2001, Molecular immunology.

Three-dimensional Structure of the Barley β-d-Glucan Glucohydrolase in Complex with a Transition State Mimic*

Brian J. Smith, J. Varghese, A. Vasella, 2004, Journal of Biological Chemistry.

Structural Basis for Broad Substrate Specificity in Higher Plant β-d-Glucan Glucohydrolases Article, publication date, and citation information can be found at www.plantcell.org/cgi/doi/10.1105/tpc.010442.

Brian J. Smith, J. Varghese, G. Fincher, 2002, The Plant Cell Online.

Single-chain Fv multimers of the anti-neuraminidase antibody NC10: the residue at position 15 in the V(L) domain of the scFv-0 (V(L)-V(H)) molecule is primarily responsible for formation of a tetramer-trimer equilibrium.

Olan Dolezal, Mark Walter, A. Kortt, 2003, Protein engineering.

Structural Basis for Broad Substrate Specificity in Higher Plant β-d-Glucan Glucohydrolases Article, publication date, and citation information can be found at www.plantcell.org/cgi/doi/10.1105/tpc.010442.

Brian J. Smith, J. Varghese, G. Fincher, 2002, The Plant Cell Online.

Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase.

Brian J. Smith, J. Varghese, G. Fincher, 2001, Structure.

Comparative modeling of the three‐dimensional structures of family 3 glycoside hydrolases

J. Varghese, G. Fincher, M. Hrmova, 2000, Proteins.