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Biochemistry|May 2, 1989
Isolation and preliminary characterization of wild-type OmpC porin dimers from Escherichia coli K-12W J Rocque, E J McGroartyBiochemistry|June 5, 1990
Structure and function of an OmpC deletion mutant porin from Escherichia coli K-12W J Rocque, E J McGroartyBiochemistry|November 3, 1992
Effects of pH on bacterial porin functionJ C Todt, W J Rocque, E J McGroartyJournal of Bacteriology|September 1, 1987
Lipopolysaccharide tightly bound to porin monomers and trimers from Escherichia coli K-12W J Rocque, R T Coughlin, E J McGroartyAntimicrobial Agents and Chemotherapy|March 1, 1988
Polycation binding to isolated lipopolysaccharide from antibiotic-hypersusceptible mutant strains of Escherichia coliW J Rocque, S W Fesik, A Haug, et al.The Journal of Biological Chemistry|May 15, 1993
A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferaseW J Rocque, C A McWherter, D C Wood, et al.Protein Expression and Purification|April 3, 2001
Solution studies of recombinant human stromal-cell-derived factor-1W D Holmes, T G Consler, W S Dallas, et al.Biochemistry|April 9, 1999
Subunit affinities and stoichiometries of the human papillomavirus type 11 E1:E2:DNA complexS F Chao, W J Rocque, S Daniel, et al.Proceedings of the National Academy of Sciences of the United States of America|February 1, 1993
Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanismD A Rudnick, W J Rocque, C A McWherter, et al.The Journal of Biological Chemistry|May 25, 1991
Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferaseD A Rudnick, C A McWherter, W J Rocque, et al.Pageof 3