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
Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase.
TL;DR: The secondary structure elements identified in this study are consistent with previous chemical and mutagenesis studies of BHPTPase structure and are characteristic of the beta alpha beta structural motif.
Journal ArticleDOI
Identification and Optimization of Anthranilic Acid Based Inhibitors of Replication Protein A.
J.D. Patrone,J.D. Patrone,N.F. Pelz,Brittney S. Bates,Elaine M. Souza-Fagundes,Bhavatarini Vangamudi,DeMarco V. Camper,Alexey G. Kuznetsov,Carrie F. Browning,Michael D. Feldkamp,Andreas O. Frank,Benjamin A. Gilston,Edward T. Olejniczak,Olivia W. Rossanese,Alex G. Waterson,Walter J. Chazin,Stephen W. Fesik +16 more
TL;DR: An anthranilic acid based series was optimized by using a structure‐guided iterative medicinal chemistry approach to yield a cell‐penetrant compound that binds to RPA70N with an affinity of 812 nm, which is capable of inhibiting PPIs mediated by this domain.
Journal Article
Nuclear magnetic resonance studies on the interaction of avoparcin with model receptors of bacterial cell walls.
TL;DR: A significant affinity was measured for the tripeptide, indicating that the interactions with the NH2 terminus of the antibiotics provide binding energy for the antibiotic peptide complex but that the COOH-terminal end of the antibiotic also plays an important role in the binding interaction.
Journal ArticleDOI
Increased NOEs for small molecules using mixed solvents
TL;DR: In this article, a simple procedure is proposed for increasing the size of NOEs in NMR studies of small molecules, which involves the use of a mixed solvent (Me2SO-d6-D2O) to increase the viscosity of the solution such that ωtc > 1.
Journal ArticleDOI
Reply to Tran et al.: Dimeric KRAS protein-protein interaction stabilizers.
Dirk Kessler,Andreas Gollner,Michael Gmachl,Andreas Mantoulidis,Laetitia J. Martin,Andreas Zoephel,Moriz Mayer,David Covini,Silke Fischer,Thomas Gerstberger,Teresa Gmaschitz,Craig M. Goodwin,Peter Greb,Daniela Häring,Wolfgang Hela,Johann Hoffmann,Jale Karolyi-Oezguer,Petr Knesl,Stefan Kornigg,Manfred Koegl,Roland Kousek,Lyne Lamarre,Franziska Moser,Silvia Munico-Martinez,Christoph Peinsipp,Jason Phan,Jörg Rinnenthal,Jiqing Sai,Christian Salamon,Yvonne Scherbantin,Katharina Schipany,Renate Schnitzer,Andreas Schrenk,Bernadette Sharps,Gabriella Siszler,Qi Sun,Alex G. Waterson,Bernhard Wolkerstorfer,Markus Zeeb,Mark Pearson,Stephen W. Fesik,Darryl B. McConnell +41 more
TL;DR: It is proposed that BI-2852 exerts its cellular effects on the MAPK pathway at least in part through stabilization of a nonfunctional KRAS dimer, and inhibiting the protein–protein interactions between KRAS and its GEFs, GAPs, and downstream effectors is a more plausible explanation.