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Results: 1-14 |
Results: 14
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation
Authors: Chiti, F Taddei, N Stefani, M Dobson, CM Ramponi, G
Citation: F. Chiti et al., Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation, PROTEIN SCI, 10(4), 2001, pp. 879-886
Solution conditions can promote formation of either amyloid protofilamentsor mature fibrils from the HypF N-terminal domain
Authors: Chiti, F Bucciantini, M Capanni, C Taddei, N Dobson, CM Stefani, M
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
Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin
Authors: Chiti, F Mangione, P Andreola, A Giorgetti, S Stefani, M Dobson, CM Bellottl, V Taddei, N
Citation: F. Chiti et al., Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin, J MOL BIOL, 307(1), 2001, pp. 379-391
Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase
Authors: Taddei, N Capanni, C Chiti, F Stefani, M Dobson, CM Ramponi, G
Citation: N. Taddei et al., Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase, J BIOL CHEM, 276(40), 2001, pp. 37149-37154
Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol
Authors: Hamada, D Chiti, F Guijarro, JI Kataoka, M Taddei, N Dobson, CM
Citation: D. Hamada et al., Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol, NAT ST BIOL, 7(1), 2000, pp. 58-61
Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization
Authors: Pertinhez, TA Hamada, D Smith, LJ Chiti, F Taddei, N Stefani, M Dobson, CM
Citation: Ta. Pertinhez et al., Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization, PROTEIN SCI, 9(8), 2000, pp. 1466-1473
Mutational analysis of the propensity for amyloid formation by a globular protein
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
Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatasefolding
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
Acceleration of the folding of acylphosphatase by stabilization of local secondary structure
Authors: Chiti, F Taddei, N Webster, P Hamada, D Fiaschi, T Ramponi, G Dobson, CM
Citation: F. Chiti et al., Acceleration of the folding of acylphosphatase by stabilization of local secondary structure, NAT ST BIOL, 6(4), 1999, pp. 380-387
Mutational analysis of acylphosphatase suggests the importance of topologyand contact order in protein folding
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
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
Authors: Chiti, F Webster, P Taddei, N Clark, A Stefani, M Ramponi, G Dobson, CM
Citation: F. Chiti et al., Designing conditions for in vitro formation of amyloid protofilaments and fibrils, P NAS US, 96(7), 1999, pp. 3590-3594
Development of enzymatic activity during protein folding - Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase
Authors: Chiti, F Taddei, N Giannoni, E van Nuland, NAJ Ramponi, G Dobson, CM
Citation: F. Chiti et al., Development of enzymatic activity during protein folding - Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase, J BIOL CHEM, 274(29), 1999, pp. 20151-20158
Thermodynamics and kinetics of folding of common-type acylphosphatase: Comparison to the highly homologous muscle isoenzyme
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
The contribution of acidic residues to the conformational stability of common-type acylphosphatase
Authors: Paoli, P Taddei, N Fiaschi, T Veggi, D Camici, G Manao, G Raugei, G Chiti, F Ramponi, G
Citation: P. Paoli et al., The contribution of acidic residues to the conformational stability of common-type acylphosphatase, ARCH BIOCH, 363(2), 1999, pp. 349-355
Risultati: 1-14 |