K. Mcginnis

The five cysteine residues located in the active site region of bovine aspartyl (asparaginyl) beta-hydroxylase are not essential for catalysis.

A. Stern, P. Friedman, J. Fu, 1998, Biochimica et biophysica acta.

Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+.

V. Garsky, A. Stern, P. Friedman, 1996, Biochemistry.

Unusually low dynamic surface tensions of aqueous solutions of sodium myristate

E. Franses, K. Mcginnis, Xinyun Wen, 1998 .

A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenases.

K. O. Elliston, P. Griffin, A. Stern, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Disulfide arrangement and functional domains of beta-1,4-endoglucanse E5 from Thermomonospora fusca.

D. Wilson, K. McGinnis, K. Mcginnis, 1993, Biochemistry.

Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2.

D. Wilson, K. McGinnis, C. Kroupis, 1993, Biochemistry.

Disulfide arrangement and chemical modification of beta-1,4-endoglucanase E2 from Thermomonospora fusca.

D. Wilson, K. Mcginnis, 1993, Biochemistry.

Higher Ploidy in Saccharomyces cerevisiae Supports Enhanced Hepatitis B Virus S Cloned Gene Expression at the Pilot Scale

D. Montgomery, L. Schultz, B. A. Arnold, 1996, Biotechnology progress.