T
Thomas L. James
Researcher at University of California, San Francisco
Publications - 366
Citations - 17557
Thomas L. James is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Nuclear Overhauser effect & RNA. The author has an hindex of 61, co-authored 366 publications receiving 17129 citations. Previous affiliations of Thomas L. James include St Mary's Hospital & Wake Forest University.
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Structure and mechanism
TL;DR: This chapter discusses enzyme modifications for Nuclear Magnetic Resonance Studies, which resulted in the determination of Three-Dimensional Protein Structures in Solution by Nuclear magnetic Resonance: An Overview, and the heuristic Refinement Method for Determination of Solution Structure of Proteins from Nuclear Magnetic resonance data.
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DOCK 6: Combining techniques to model RNA–small molecule complexes
P. Therese Lang,Scott R. Brozell,Sudipto Mukherjee,Eric F. Pettersen,Elaine C. Meng,Veena Thomas,Robert C. Rizzo,David A. Case,Thomas L. James,Irwin D. Kuntz +9 more
TL;DR: A test set of RNA-ligand complexes is compiled to validate the ability of the DOCK suite of programs to successfully recreate experimentally determined binding poses and indicates that DOCK can indeed be useful for structure-based drug design aimed at RNA.
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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.
David G. Donne,John H. Viles,Darlene Groth,Ingrid Mehlhorn,Thomas L. James,Fred E. Cohen,Stanley B. Prusiner,Peter E. Wright,H.J. Dyson +8 more
TL;DR: In this article, the secondary structure of the recombinant Syrian hamster PrP of residues 29-231 [PrP(29-231)] is investigated by multidimensional heteronuclear NMR.
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Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
Kiyotoshi Kaneko,Laurence Zulianello,Michael J. Scott,Carol M. Cooper,Wallace Andrew,Thomas L. James,Fred E. Cohen,Stanley B. Prusiner +7 more
TL;DR: The identification of the site at which protein X binds to the cellular isoform of PrP (PrPC) using scrapie-infected mouse (Mo) neuroblastoma cells transfected with chimeric Hu/MoPrP genes even though protein X has not yet been isolated is reported.
Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation (species barrieryCreutzfeldt-Jakob diseaseydominant negative)
Kiyotoshi Kaneko,Laurence Zulianello,Michael R. Scott,Carol M. Cooper,Wallace Andrew,Thomas L. James,Ezra E.W. Cohen,Stanley B. Prusiner +7 more
TL;DR: In this article, the authors identify the site at which protein X binds to the cellular isoform of PrP (PrP C ) using scrapie-infected mouse (Mo) neuroblastoma cells transfected with chimeric HuyMoPrP genes even though protein X has not yet been isolated.