Ronald J. Doyle
University of Louisville
147 Papers
2.4K Citations
Ronald J. Doyle is an academic researcher from University of Louisville. The author has contributed to research in topics: Bacillus subtilis & Cell wall. The author has an hindex of 40, co-authored 147 publications.
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Papers
•Book
Microbial cell surface hydrophobicity
Ronald J. Doyle,Mel Rosenberg +1 more
- 01 Jan 1990
TL;DR: The importance of hydrophobicity in the adhesiveness of pathogenic Gram-negative bacteria, especially Candida species, and the importance of surface free energy as a hydphobicity measure in bacterial adhesion to solid surfaces is studied.
462
Contribution of the hydrophobic effect to microbial infection.
TL;DR: The literature provides compelling evidence that a large number of bacterial and fungal pathogens depend on hydrophobic interactions for successful colonization of a host and several laboratories are now developing effective antiadhesins, based on inhibition of hydrophilic interactions between the host and the pathogen.
282
Diversity of the Escherichia coli type 1 fimbrial lectin. Differential binding to mannosides and uroepithelial cells.
TL;DR: Analysis of the ability of isogenic, recombinant strains of E. coli expressing fimH genes of the predominant fecal and UTI phenotypes to adhere to glycoproteins and to uroepithelial cells indicates that type 1 fimbriae differ in their ability to recognize various mannosides, utilizing at least two different mechanisms.
173
Hydrophobic interactions and the adherence of Streptococcus sanguis to hydroxylapatite.
TL;DR: The results suggest that the adherence of S. sanguis to saliva-coated smooth surfaces is at least partially dependent on the formation of hydrophobic bonds between the cell and adsorbed salivary proteins.
169
On the specificity of the D-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of D-galactose and thiogalactose.
TL;DR: The D-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests.
120