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Citation: F. Chiti et al., Solution conditions can promote formation of either amyloid protofilamentsor mature fibrils from the HypF N-terminal domain, PROTEIN SCI, 10(12), 2001, pp. 2541-2547

Authors: Chiti, F Taddei, N Bucciantini, M White, P Ramponi, G Dobson, CM

Citation: F. Chiti et al., Mutational analysis of the propensity for amyloid formation by a globular protein, EMBO J, 19(7), 2000, pp. 1441-1449

Authors: Taddei, N Chiti, F Fiaschi, T Bucciantini, M Capanni, C Stefani, M Serrano, L Dobson, CM Ramponi, G

Citation: N. Taddei et al., Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatasefolding, J MOL BIOL, 300(3), 2000, pp. 633-647

Authors: Chiti, F Taddei, N White, PM Bucciantini, M Magherini, F Stefani, M Dobson, CM

Citation: F. Chiti et al., Mutational analysis of acylphosphatase suggests the importance of topologyand contact order in protein folding, NAT ST BIOL, 6(11), 1999, pp. 1005-1009

Authors: Bucciantini, M Chiarugi, P Cirri, P Taddei, L Stefani, M Raugei, G Nordlund, P Ramponi, G

Citation: M. Bucciantini et al., The low M-r phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr(131) or Tyr(132) by Src kinase, FEBS LETTER, 456(1), 1999, pp. 73-78

Authors: Taddei, N Chiti, F Paoli, P Fiaschi, T Bucciantini, M Stefani, M Dobson, CM Ramponi, G

Citation: N. Taddei et al., Thermodynamics and kinetics of folding of common-type acylphosphatase: Comparison to the highly homologous muscle isoenzyme, BIOCHEM, 38(7), 1999, pp. 2135-2142