Philip D. Jeffrey mainly investigates Cell biology, Biochemistry, Ubiquitin ligase, Cyclin-dependent kinase and Protein structure. His biological study spans a wide range of topics, including Molecular biology and Genetics, DNA. His DNA research is multidisciplinary, incorporating perspectives in B3 domain, Binding domain, Binding site and HMG-box.
His work in Cyclin-dependent kinase covers topics such as Cyclin-dependent kinase 2 which are related to areas like Active site. His Protein structure study combines topics from a wide range of disciplines, such as Autophagy, Apoptosis, Bcl-xL and Function. He combines subjects such as Protein ubiquitination, Skp1 and F-box protein with his study of Ubiquitin-conjugating enzyme.
His main research concerns Cell biology, Biochemistry, Biophysics, Protein structure and Binding site. His Cell biology research is multidisciplinary, relying on both Quorum sensing, Molecular biology and Apoptosis. Philip D. Jeffrey combines topics linked to Ubiquitin ligase with his work on Biochemistry.
His Biophysics study combines topics in areas such as Endoplasmic reticulum, Vesicle and Lipid bilayer fusion. In his work, Enzyme activator is strongly intertwined with Active site, which is a subfield of Protein structure. His Binding site research is multidisciplinary, incorporating elements of Stereochemistry and Organelle.
His primary scientific interests are in Biophysics, Vesicle, Lipid bilayer fusion, Binding site and Linker. In his research, Philip D. Jeffrey performs multidisciplinary study on Biophysics and VPS45. His study in Vesicle is interdisciplinary in nature, drawing from both Golgi apparatus, Endoplasmic reticulum and USE1.
Philip D. Jeffrey performs multidisciplinary study in Binding site and Pyrenoid in his work. Linker and Carbon fixation are two areas of study in which Philip D. Jeffrey engages in interdisciplinary research. The SNARE complex assembly study combines topics in areas such as Structural biology and Molecular biophysics.
His primary areas of study are Biochemistry, Nucleotide excision repair, Base pair, Nucleotide-excision repair complex and Pyrimidone. His Biochemistry research includes elements of Bacterial adhesin and Streptococcus gordonii. His study in Nucleotide excision repair is interdisciplinary in nature, drawing from both Pyrimidine dimer and Stereochemistry.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
Yunje Cho;Svetlana Gorina;Philip D. Jeffrey;Nikola P. Pavletich.
Science (1994)
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Philip D. Jeffrey;Alicia A. Russo;Kornelia Polyak;Emma Gibbs.
Nature (1995)
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.
Nature (2002)
Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex.
Alicia A. Russo;Philip D. Jeffrey;Andrea K. Patten;Joan Massagué.
Nature (1996)
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.
Cancer Cell (2005)
Structure of a c-Cbl–UbcH7 Complex: RING Domain Function in Ubiquitin-Protein Ligases
Ning Zheng;Ping Wang;Philip D. Jeffrey;Nikola P. Pavletich.
Cell (2000)
Acquired Resistance to Imatinib in Gastrointestinal Stromal Tumor Occurs Through Secondary Gene Mutation
Cristina R. Antonescu;Peter Besmer;Tianhua Guo;Knarik Arkun.
Clinical Cancer Research (2005)
BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure
Haijuan Yang;Philip D. Jeffrey;Julie Miller;Elspeth Kinnucan.
Science (2002)
Structural basis of cyclin-dependent kinase activation by phosphorylation.
Alicia A. Russo;Philip D. Jeffrey;Nikola P. Pavletich.
Nature Structural & Molecular Biology (1996)
Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
Philip D. Jeffrey;Svetlana Gorina;Nikola P. Pavletich.
Science (1995)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
Tsinghua University
Princeton University
Memorial Sloan Kettering Cancer Center
Princeton University
Shanghai Medical College of Fudan University
Max Planck Society
University of Geneva
Princeton University
University of Cambridge
Chinese University of Hong Kong
University of Oulu
University of Seville
Zhejiang University
Chinese Academy of Sciences
Institute of Photonic Sciences
Yale University
University of Porto
National Institutes of Health
Japan Agency for Marine-Earth Science and Technology
University of Regensburg
Complutense University of Madrid
Uppsala University
University of Massachusetts Boston
University of Melbourne
Grenoble Alpes University
Vanderbilt University