J
James P. Snyder
Researcher at Emory University
Publications - 263
Citations - 10988
James P. Snyder is an academic researcher from Emory University. The author has contributed to research in topics: Curcumin & Receptor. The author has an hindex of 58, co-authored 263 publications receiving 10280 citations. Previous affiliations of James P. Snyder include Yerkes National Primate Research Center & G. D. Searle & Company.
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Journal ArticleDOI
The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography
TL;DR: Comparison with Taxol shows that the longstanding expectation of a common pharmacophore is not met, because each ligand exploits the tubulin-binding pocket in a unique and independent manner.
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The binding conformation of Taxol in β-tubulin: A model based on electron crystallographic density
TL;DR: The crystallographic density is correlated with analysis of Taxol conformations and the unique solution is found to be a T-shaped Taxol structure, which is optimized within the β-tubulin site and exhibits functional similarity to a portion of the B9-B10 loop in the α- Tubulin subunit.
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Synthesis and biological evaluation of novel curcumin analogs as anti-cancer and anti-angiogenesis agents
Brian Adams,Eva M. Ferstl,Matthew C. Davis,Marike Herold,Serdar Kurtkaya,Richard F. Camalier,Melinda G. Hollingshead,Gurmeet Kaur,Edward A. Sausville,Frederick R. Rickles,James P. Snyder,Dennis C. Liotta,Mamoru Shoji +12 more
TL;DR: Compare analysis suggests the compound to be a possible RNA/DNA antimetabolite, but also implies that the compound's cytotoxicity may arise from a presently unknown mechanism.
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Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
Xing Zhang,John R. Horton,Anup K. Upadhyay,Astrid Spannhoff,Jin Liu,James P. Snyder,Mark T. Bedford,Xiaodong Cheng +7 more
TL;DR: The crystal structure of the catalytic SET domain of GLP in complex with BIX-01294 and S-adenosyl-L-homocysteine is presented and it is shown that the inhibitor resembles the bound conformation of histone H3 Lys4 to Arg8, and is positioned in place by residues specific for G9a and GLP through specific interactions.
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Facial symmetry in protein self-assembly.
Anil K. Mehta,Kun Lu,W. Seth Childers,Yan Liang,Steven N. Dublin,Jijun Dong,James P. Snyder,Sai Venkatesh Pingali,Pappannan Thiyagarajan,David G. Lynn +9 more
TL;DR: Spectroscopic and microscopy analyses are combined to reveal the subtle atomic-level differences that dictate assembly of two conformationally pure Abeta(16-22) assemblies, amyloid fibers and nanotubes, and define the minimal repeating unit for each assembly.