P
Philip D. Jeffrey
Researcher at Princeton University
Publications - 93
Citations - 20989
Philip D. Jeffrey is an academic researcher from Princeton University. The author has contributed to research in topics: Protein subunit & Quorum sensing. The author has an hindex of 51, co-authored 88 publications receiving 19428 citations. Previous affiliations of Philip D. Jeffrey include GlaxoSmithKline & University of Waikato.
Papers
More filters
Journal ArticleDOI
Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
TL;DR: The crystal structure of a complex containing the core domain of human p53 and a DNA binding site provides a framework for understanding how mutations inactivate it, and supports the hypothesis that DNA binding is critical for the biological activity of p53.
Journal ArticleDOI
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Philip D. Jeffrey,Alicia A. Russo,Kornelia Polyak,Emma Gibbs,Jerard Hurwitz,Joan Massagué,Nikola P. Pavletich +6 more
TL;DR: The crystal structure of the human cyclinA-cyclin-dependent kinase2-ATP complex has been determined at 2.3 A resolution and activates the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.
Journal ArticleDOI
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
Ning Zheng,Brenda A. Schulman,Brenda A. Schulman,Langzhou Song,Julie J. Miller,Philip D. Jeffrey,Ping Wang,Claire Chu,Deanna M. Koepp,Stephen J. Elledge,Stephen J. Elledge,Michele Pagano,Ronald C. Conaway,Joan W. Conaway,J. Wade Harper,Nikola P. Pavletich +15 more
TL;DR: The structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF complex suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold.
Journal ArticleDOI
Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
Shiqing Li,Karl R. Schmitz,Karl R. Schmitz,Philip D. Jeffrey,Jed J.W. Wiltzius,Paul Kussie,Kathryn M. Ferguson,Kathryn M. Ferguson +7 more
TL;DR: It is suggested that cetuximab interacts exclusively with domain III of sEGFR, partially occluding the ligand binding region on this domain and sterically preventing the receptor from adopting the extended conformation required for dimerization contribute to potent inhibition of EGFR activation.
Journal ArticleDOI
Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex.
TL;DR: The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A–cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 Å.