Prischi, Filippo - University of Essex - School of Biological Sciences

个人简介

Jun 2015 - Lecturer, University of Essex, School of Biological Sciences, Colchester, UK. May 2010 - Research Associate, Imperial College London, Centre for Structural Biology, London, UK. Oct 2009 - Research Assistant, National Institute for Medical Research - MRC (now The Francis Crick Institute), division of Molecular Structure, London, UK.

研究领域

My research programme focuses on unravelling the molecular mechanism of kinase signalling pathways, such as Ras/ERK/RSKs or S6Ks, in normal and cancer cells. In particular, I am interested in characterizing signal pathways that are unique of S6K2 and not redundant with S6K1. Recently, protein kinase C epsilon (PKCε) and B-Raf have been shown to activate S6K2, but not S6K1. Using a range of biophysical and structural techniques my aim is to characterize B-Raf-PKCε-S6K2 complex and its relationship with hnRNPA1. The information obtained from my studies will help the design of more specific inhibitors that could represent drug development candidates. In fact, these pathways are extremely relevant in cancer biology, since it has been shown that S6K2 mediates prosurvival/chemioresistence in patients with small cell lung cancer (SCLC). Around 41,000 people are diagnosed with lung cancer in the UK every year. Of these ~15% are SCLC and even with treatment the survival rate for 5 years is 5%. I have an active collaboration with Dr Marta Carroni (SciLife Laboratories, Stockholm), Dr Olivier Pardo (Imperial College London). Biochemistry & Enzymology & Biophysics Structural Biology - X-ray Crystallography and NMR Post-Translational modifications in Signaling Pathways Signaling Pathways in normal and cancer cell

近期论文

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Prischi F, Pastore A. Application of Nuclear Magnetic Resonance and Hybrid Methods to Structure Determination of Complex Systems. Adv. Exp. Med. Biol. 2016; 896:351-68. Carrara M, Prischi F, Nowak P, Ali MM. Crystal Structures of Perk Luminal Domains Reveal Transient Tetramer State Important for ER Stress Signaling. EMBO J, 20015; 34:1589-1600. Carrara M, Prischi F, Nowak P, Kopp MC, Ali MM. Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling. eLife. 2015; 4:e03522. Prischi F, Nowak P, Carrara M, Ali MM. Phosphoregulation of human Ire1 RNase splicing activity. Nat. Commun. 2014; 5:3554. Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A. Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat. Commun. 2010; 1:95. Prischi F, Pastore C, Carroni M, Iannuzzi C, Adinolfi S, Temussi P, Pastore A. Of the vulnerability of orphan complex proteins: the case study of the E. coli IscU and IscS proteins. Protein Expr Purif. 2010; 73:161-6. Prischi F, Giannini C, Adinolfi S, Pastore A. The N-Terminus of human frataxin is an intrinsically unfolded region. FEBS J. 2009; 276:6669-76. Adinolfi S, Iannuzzi C, Prischi F, Pastore C, Iametti S, Martin SR, Bonomi F, Pastore A. Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nat Struct Mol Biol. 2009; 16:390-6. Venditti V, Bernini A, De Simone A, Spiga O, Prischi F, Niccolai N. MD and NMR studies of alpha-bungarotoxin surface accessibility. Biochem Biophys Res Commun. 2007; 356:114-7. Bernini A, Spiga O, Venditti V, Prischi F, Bracci L, Tong AP, Wong WT, Niccolai N. NMR studies of lysozyme surface accessibility by using different paramagnetic relaxation probes. J Am Chem Soc. 2006; 128:9290-1.