Dr Giorgio Favrin

Giorgio  Favrin

University position

Senior Research Associate

Dr Giorgio Favrin is pleased to consider applications from prospective PhD students.


Department of Biochemistry


Cambridge Systems Biology Centre

Home page

http://www.favrin.sysbiol.cam.ac.uk/ (personal home page)

Research Theme

Systems and Computational Neuroscience


The focus of my research is to build and analyze the network of pathways associated with Alzheimer’s disease. We are currently measuring these interaction data in the yeast S. cerevisiae (baker’s yeast). We use these data, in conjunction with freely available databases, to build the network of disease associated genetic pathways. As many genes are differentially expressed at different ages, it is crucial to study the temporal evolution of such a network, or, in other words, how the cascade of events that leads from the healthy to the diseased state changes with time and with the age of the organism.

The power of such a network/system approach is that we will be able to verify a large number of hypothesis regarding the downstream pathways of AD, not only the ones in which a single effector pathway is present, but, importantly, the ones in which several
(even very distinct) pathways contribute to the disease.

Research Focus





Systems Biology


Clinical conditions

Amyotrophic Latyeral Sclerosis

Movement disorders


No equipment indicated



Peter St George-Hyslop


Justin Yerbury Web: http://www.uow.edu.au/science...

Associated News Items

    Key publications

    Favrin G, Bean DM, Bilsland E, Boyer H, Fischer BE, Russell S, Crowther DC, Baylis HA, Oliver SG, Giannakou ME (2013), “Identification of novel modifiers of Aβ toxicity by transcriptomic analysis in the fruitfly.” Sci Rep 3:3512 Details

    Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, Vendruscolo M, Favrin G (2007), “Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.” PLoS Comput Biol 3(9):1727-38 Details



    Bean DM, Heimbach J, Ficorella L, Micklem G, Oliver SG, Favrin G (2014), “esyN: network building, sharing and publishing.” PLoS One 9(9):e106035 Details

    Khabirova E, Moloney A, Marciniak SJ, Williams J, Lomas DA, Oliver SG, Favrin G, Sattelle DB, Crowther DC (2014), “The TRiC/CCT Chaperone Is Implicated in Alzheimer's Disease Based on Patient GWAS and an RNAi Screen in Aβ-Expressing Caenorhabditis elegans.” PLoS One 9(7):e102985 Details


    Speretta E, Jahn TR, Tartaglia GG, Favrin G, Barros TP, Imarisio S, Lomas DA, Luheshi LM, Crowther DC, Dobson CM (2012), “Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity.” J Biol Chem 287(24):20748-54 Details


    Bolognesi B, Kumita JR, Barros TP, Esbjorner EK, Luheshi LM, Crowther DC, Wilson MR, Dobson CM, Favrin G, Yerbury JJ (2010), “ANS binding reveals common features of cytotoxic amyloid species.” ACS Chem Biol 5(8):735-40 Details

    Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM (2010), “Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.” Biophys J 98(8):1677-84 Details


    Cheon M, Favrin G, Chang I, Dobson CM, Vendruscolo M (2008), “Calculation of the free energy barriers in the oligomerisation of Abeta peptide fragments.” Front Biosci 13:5614-22 Details

    Pawar A, Favrin G (2008), “Finite size effects in simulations of protein aggregation.” PLoS One 3(7):e2641 Details


    Favrin G, Irbäck A, Mohanty S (2004), “Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.” Biophys J 87(6):3657-64 Details

    Favrin G, Irbäck A, Wallin S (2004), “Sequence-based study of two related proteins with different folding behaviors.” Proteins 54(1):8-12 Details


    Favrin G, Irbäck A, Samuelsson B, Wallin S (2003), “Two-state folding over a weak free-energy barrier.” Biophys J 85(3):1457-65 Details


    Favrin G, Irbäck A, Wallin S (2002), “Folding of a small helical protein using hydrogen bonds and hydrophobicity forces.” Proteins 47(2):99-105 Details