J
James P. Griffith
Researcher at Vertex Pharmaceuticals
Publications - 17
Citations - 3593
James P. Griffith is an academic researcher from Vertex Pharmaceuticals. The author has contributed to research in topics: Binding site & Thermolysin. The author has an hindex of 13, co-authored 17 publications receiving 3444 citations.
Papers
More filters
Journal ArticleDOI
Structure and mechanism of interleukin-1 beta converting enzyme.
Wilson Keith P,J.A Black,John A. Thomson,Eunice E. Kim,James P. Griffith,Manuel A. Navia,Murcko Mark A,Stephen P. Chambers,R A Aldape,Scott A. Raybuck +9 more
TL;DR: The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction and confirms the relationship between human ICE and cell-death proteins in other organisms.
Journal ArticleDOI
X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex
James P. Griffith,Joseph L. Kim,Eunice E. Kim,Michael D. Sintchak,John A. Thomson,Matthew J. Fitzgibbon,Mark A. Fleming,Paul R. Caron,Kathy Hsiao,Manuel A. Navia +9 more
TL;DR: The ternary complex described here represents the three-dimensional structure of a Ser/Thr protein phosphatase and provides a structural basis for understanding calcineurin inhibition by FKBP12-FK506.
Journal ArticleDOI
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding
Joseph L. Kim,Morgenstern Kurt A,James P. Griffith,Maureen D. Dwyer,John A. Thomson,Murcko Mark A,Chao Lin,Paul R. Caron +7 more
TL;DR: The structure of the HCV NS3 RNA helicase domain complexed with a single-stranded DNA oligonucleotide has been solved to 2.2 A resolution and is a member of a superfamily of helicases, termed superfamily II.
Journal ArticleDOI
The Structural Basis for Autoinhibition of FLT3 by the Juxtamembrane Domain
James P. Griffith,James Black,Carlos H. Faerman,Lora Swenson,Michael Wynn,Fan Lu,Judith A. Lippke,Kumkum Saxena +7 more
TL;DR: The crystal structure of the autoinhibited form of FLT3 is determined and the detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine kinases.
Journal ArticleDOI
Crystal structure of p38 mitogen-activated protein kinase.
Wilson Keith P,Matthew J. Fitzgibbon,Paul R. Caron,James P. Griffith,Wenyong Chen,Patricia G. McCaffrey,Stephen P. Chambers,Michael S.-S. Su +7 more
TL;DR: The crystal structure of the apo, unphosphorylated form of p38 kinase has been solved at 2.3 Å resolution and the relative orientation of the two domains of p 38 kinase is different from that observed in the active form of cAMP-dependent protein kinase.