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研究领域

David Fernig is a North West Cancer Research Fund Professor of Biological Chemistry whose research focuses on understanding the regulation of cell fate by growth factors. The regulation of cell fate lies at the heart of the development of animals from a single cell, the fertilised egg, to the mature organism. Many human diseases, ranging from developmental defects affecting neonates to cancers result from incorrect cell fate decisions. At the molecular level, cell fate is regulated by the assembly of complexes of proteins, polysaccharides, lipids and nucleic acids that are dynamic in time, location and composition. The molecular focus of research are the fibroblast growth factors (FGF) and hepatocyte growth factor/scatter factor (HGF/SF), their cognate receptor tyrosine kinases and heparan sulfate co-receptors since molecules are central players in normal development and in diseases whose basis is incorrect cell fate decisions. The complexity of the biological problem at the molecular level necessitates a highly interdisciplinary approach, in which analytical techniques from the physical sciences are applied to solve biological problems. The foundation for this approach is the major central facilities of the School of Biological Sciences and the collegiate character of the University, and indispensable ingredient for interdisciplinary research. ÊResearch projects flow freely within the Facilities of the School of Biological Sciences and within the orbit of the virtual Liverpool Centre for Nanoscale Science. Particularly strong links exist with the Departments of Chemistry, Physics, and within the Faculty of Medicine with the Schools of Clinical Laboratory Sciences, and of Health Sciences, Reproductive and Developmental Medicine. Further afield, Proteoglycans NorthWest (PgsNoW) groups seventeen major research groups in the North West of England and provides a major forum for collaboration between the major research Universities in the region.

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Differential sub-nuclear distribution of hypoxia-inducible factors (HIF)-1 and-2 alpha impacts on their stability and mobility. OPEN BIOLOGY, 6(9). doi:10.1098/rsob.160195 Fibroblast growth factors as tissue repair and regeneration therapeutics. PEERJ, 4. doi:10.7717/peerj.1535 Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification. OPEN BIOLOGY, 6(3). doi:10.1098/rsob.150275 High colloidal stability of gold nanorods coated with a peptide-ethylene glycol: Analysis by cyanide-mediated etching and nanoparticle tracking analysis. COLLOIDS AND SURFACES B-BIOINTERFACES, 146, 871-878. doi:10.1016/j.colsurfb.2016.07.006 High production in E. coli of biologically active recombinant human fibroblast growth factor 20 and its neuroprotective effects.. Applied microbiology and biotechnology, 100(7), 3023-3034. doi:10.1007/s00253-015-7168-y In silico analyses of heparin binding proteins expression in human periodontal tissues.. BMC research notes, 9, 53. doi:10.1186/s13104-016-1857-1 Selectivity in glycosaminoglycan binding dictates the distribution and diffusion of fibroblast growth factors in the pericellular matrix. OPEN BIOLOGY, 6(3). doi:10.1098/rsob.150277 Specific Internalisation of Gold Nanoparticles into Engineered Porous Protein Cages via Affinity Binding. PLOS ONE, 11(9). doi:10.1371/journal.pone.0162848 The Heparin-Binding Proteome in Murine Experimental Acute Pancreatitis. Cytokines and growth factors cross-link heparan sulfate. Detection of interaction between protein trytophan residues and small or macromolecular ligands by synchrotron radiation magnetic circular dichroism. HaloTag is an effective expression and solubilisation fusion partner for a range of fibroblast growth factors. Photothermal raster image correlation spectroscopy of gold nanoparticles in solution and on live cells. Structural determinants of heparin-transforming growth factor-beta 1 interactions and their effects on signaling. Targeting Cell Membrane Lipid Rafts by Stoichiometric Functionalization of Gold Nanoparticles with a Sphingolipid-Binding Domain Peptide.

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