S
Stephen W. Fesik
Researcher at Vanderbilt University
Publications - 298
Citations - 42613
Stephen W. Fesik is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Binding site. The author has an hindex of 95, co-authored 294 publications receiving 40006 citations. Previous affiliations of Stephen W. Fesik include Howard Hughes Medical Institute & Yale University.
Papers
More filters
Journal ArticleDOI
Survivin depletion preferentially reduces the survival of activated K-Ras-transformed cells
Aparna Sarthy,Susan Morgan-Lappe,Dorothy Zakula,Lawrence Vernetti,Mark Schurdak,Jeremy C.L. Packer,Mark G. Anderson,Senji Shirasawa,Takehiko Sasazuki,Stephen W. Fesik +9 more
TL;DR: Results indicate that tumors expressing the activated K-Ras oncogene may be particularly sensitive to inhibitors of the survivin protein.
Journal ArticleDOI
Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.
Liping Yu,Andrew M. Petros,Arndt Schnuchel,Ping Zhong,Jean M. Severin,Karl A. Walter,Thomas F. Holzman,Stephen W. Fesik +7 more
TL;DR: The three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy is described and it is shown that the catalytic domain is structurally similar to that found in other methyltransferases and the substrate binding domain is different from other methyl transferases and adopts a novel fold that consists of four α-helices.
Journal ArticleDOI
Decreased binding of antibiotics to lipopolysaccharides from polymyxin-resistant strains of Escherichia coli and Salmonella typhimurium.
TL;DR: The results suggested that esterification of the core-lipid A phosphates is responsible for increased resistance to polymyxin B and that this alteration is different from that previously proposed for the S. typhimurium and Escherichia coli strains.
Journal ArticleDOI
Solution structure of the amino-terminal fragment of urokinase-type plasminogen activator
Andrew P. Hansen,Andrew M. Petros,Robert P. Meadows,David G. Nettesheim,Andrew P. Mazar,Edward T. Olejniczak,Robert X. Xu,Terry M. Pederson,Jack Henkin,Stephen W. Fesik +9 more
TL;DR: Important structural differences between the growth factor and other homologous proteins were observed in the region which has been implicated in binding the urokinase receptor which may explain, in part, why other growth factors show no appreciable affinity for the uromycinase receptor.