个人简介
I have a BSc in Biochemistry and Genetics from the University of Nottingham and gained my PhD from Birkbeck College, University of London under the supervision of Sir Tom Blundell.
I was awarded a Fellowship from the Wellcome Trust and appointed to a lectureship at the University of Leicester Biochemistry Department in 2000. I was promoted to Reader in 2004 and moved to the University of Nottingham to found the Crystallography Laboratory which is within the Medicinal Chemistry and Structural Biology Research Division of the School of Pharmacy.
研究领域
Research interests include determining protein structures and studying the structure/function of complexes formed with drugs and natural ligands. Key developments in recent years includes (i) Determination of the first structure of an integrin/collagen complex. This structure revealed the molecular basis of the contacts formed between cells and the extracellular matrix. (ii) Determination of the platelet receptor glycoprotein Ib extracellular domain and von Willebrand factor A1 domain structures (iii) determination of the coagulation factor xi structure. These proteins are vital to normal platelet adhesion and hemostatic function. We also have collaborative interests in determining structures of protein complexes formed with anti-cancer and anti-thrombosis inhibitors. These structures provide scaffolds which can pave the way for design of improved therapeutic agents.
近期论文
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DREES SL, LI C, PRASETYA F, SALEEM M, DREVENY I, WILLIAMS P, HENNECKE U, EMSLEY J and FETZNER S, 2016. PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM. J Biol Chem. 291(13), 6610-24
WONG, SZU S, OSTERGAARD, SOREN, HALL, GARETH, LI, CHAN, WILLIAMS, PHILIP M, STENNICKE, HENNING and EMSLEY, JONAS, 2016. A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain. Blood. 127(23), 2915-23
WONG SS, ØSTERGAARD S, HALL G, LI C, WILLIAMS PM, STENNICKE H and EMSLEY J, 2016. A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain. Blood. 127(23), 2915-23
DREES SL, LI C, PRASETYA F, SALEEM M, DREVENY I, WILLIAMS P, HENNECKE U, EMSLEY J and FETZNER S, 2016. PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM. The Journal of biological chemistry. 291(13), 6610-24