Chiti F - Search Results

1

Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus.

Plakoutsi G, Bemporad F, Monti M, Pagnozzi D, Pucci P, Chiti F. Plakoutsi G, et al. Among authors: chiti f. Structure. 2006 Jun;14(6):993-1001. doi: 10.1016/j.str.2006.03.014. Structure. 2006. PMID: 16765892 Free article.

2

The contribution of acidic residues to the conformational stability of common-type acylphosphatase.

Paoli P, Taddei N, Fiaschi T, Veggi D, Camici G, Manao G, Raugei G, Chiti F, Ramponi G. Paoli P, et al. Among authors: chiti f. Arch Biochem Biophys. 1999 Mar 15;363(2):349-55. doi: 10.1006/abbi.1998.1097. Arch Biochem Biophys. 1999. PMID: 10068458

3

Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.

Taddei N, Chiti F, Fiaschi T, Bucciantini M, Capanni C, Stefani M, Serrano L, Dobson CM, Ramponi G. Taddei N, et al. Among authors: chiti f. J Mol Biol. 2000 Jul 14;300(3):633-47. doi: 10.1006/jmbi.2000.3870. J Mol Biol. 2000. PMID: 10884358

4

Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.

Chiti F, Taddei N, Stefani M, Dobson CM, Ramponi G. Chiti F, et al. Protein Sci. 2001 Apr;10(4):879-86. doi: 10.1110/ps.42401. Protein Sci. 2001. PMID: 11274479 Free PMC article.

5

Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.

Taddei N, Capanni C, Chiti F, Stefani M, Dobson CM, Ramponi G. Taddei N, et al. Among authors: chiti f. J Biol Chem. 2001 Oct 5;276(40):37149-54. doi: 10.1074/jbc.M105720200. Epub 2001 Jul 30. J Biol Chem. 2001. PMID: 11479314 Free article.

6

Kinetic partitioning of protein folding and aggregation.

Chiti F, Taddei N, Baroni F, Capanni C, Stefani M, Ramponi G, Dobson CM. Chiti F, et al. Nat Struct Biol. 2002 Feb;9(2):137-43. doi: 10.1038/nsb752. Nat Struct Biol. 2002. PMID: 11799398

7

Characterization of a novel Drosophila melanogaster acylphosphatase.

Degl'Innocenti D, Ramazzotti M, Marzocchini R, Chiti F, Raugei G, Ramponi G. Degl'Innocenti D, et al. Among authors: chiti f. FEBS Lett. 2003 Jan 30;535(1-3):171-4. doi: 10.1016/s0014-5793(02)03901-7. FEBS Lett. 2003. PMID: 12560098 Free article.

8

Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins.

Calamai M, Taddei N, Stefani M, Ramponi G, Chiti F. Calamai M, et al. Among authors: chiti f. Biochemistry. 2003 Dec 30;42(51):15078-83. doi: 10.1021/bi030135s. Biochemistry. 2003. PMID: 14690417

9

Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation.

Plakoutsi G, Taddei N, Stefani M, Chiti F. Plakoutsi G, et al. Among authors: chiti f. J Biol Chem. 2004 Apr 2;279(14):14111-9. doi: 10.1074/jbc.M312961200. Epub 2004 Jan 14. J Biol Chem. 2004. PMID: 14724277 Free article.

10

The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process.

Monti M, Garolla di Bard BL, Calloni G, Chiti F, Amoresano A, Ramponi G, Pucci P. Monti M, et al. Among authors: chiti f. J Mol Biol. 2004 Feb 6;336(1):253-62. doi: 10.1016/j.jmb.2003.10.082. J Mol Biol. 2004. PMID: 14741220 Free article.

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