Jonathan L McMurry
Affiliation: Kennesaw State University
- Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machineryJonathan L McMurry
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 8114, USA
J Bacteriol 186:7586-92. 2004..Affinity blotting showed that FlhA interacts with several other export apparatus membrane proteins. The implications of these findings are discussed, and a model of FlhA within the export apparatus is presented...
- The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complexJonathan L McMurry
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 8114, USA
Biochemistry 45:11790-8. 2006..A model incorporating the present findings is presented...
- Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhBJohn S Van Arnam
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA
J Bacteriol 186:2495-8. 2004..We conclude that the FliR and FlhB proteins are physically associated in the wild-type Salmonella basal body, probably in a 1:1 ratio...
- Hydrodynamic surface interactions enable Escherichia coli to seek efficient routes to swim upstreamJane Hill
Yale University, Department of Chemical Engineering, Environmental Engineering Program, Mason Laboratory, Room 318, New Haven, Connecticut 06520 8286, USA
Phys Rev Lett 98:068101. 2007....
- Cannabinoid receptor-G protein interactions: G(alphai1)-bound structures of IC3 and a mutant with altered G protein specificityAmy L Ulfers
Department of Molecular Pharmacology, Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912, USA
Protein Sci 11:2526-31. 2002....
- Protein Interactions in the Flagellar Export MachineryJONATHAN MCMURRY; Fiscal Year: 2005..biophysical analysis of interactions with analytical ultracentrifugation and fluorescence resonance energy transfer studies; and reconstitution of complexes of export apparatus proteins and analysis of their concerted function. ..