Taddei N - Search Results

1

Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions.

Sicorello A, Torrassa S, Soldi G, Gianni S, Travaglini-Allocatelli C, Taddei N, Relini A, Chiti F. Sicorello A, et al. Among authors: taddei n. Biophys J. 2009 Mar 18;96(6):2289-98. doi: 10.1016/j.bpj.2008.11.042. Biophys J. 2009. PMID: 19289055 Free PMC article.

2

Amyloid formation from HypF-N under conditions in which the protein is initially in its native state.

Marcon G, Plakoutsi G, Canale C, Relini A, Taddei N, Dobson CM, Ramponi G, Chiti F. Marcon G, et al. Among authors: taddei n. J Mol Biol. 2005 Mar 25;347(2):323-35. doi: 10.1016/j.jmb.2005.01.034. Epub 2005 Jan 27. J Mol Biol. 2005. PMID: 15740744

3

Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state.

Soldi G, Bemporad F, Torrassa S, Relini A, Ramazzotti M, Taddei N, Chiti F. Soldi G, et al. Among authors: taddei n. Biophys J. 2005 Dec;89(6):4234-44. doi: 10.1529/biophysj.105.067538. Epub 2005 Sep 16. Biophys J. 2005. PMID: 16169977 Free PMC article.

4

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. Among authors: taddei n. Nat Struct Biol. 2002 Feb;9(2):137-43. doi: 10.1038/nsb752. Nat Struct Biol. 2002. PMID: 11799398

5

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: taddei n. 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.

6

Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates.

Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F. Plakoutsi G, et al. Among authors: taddei n. J Mol Biol. 2005 Aug 26;351(4):910-22. doi: 10.1016/j.jmb.2005.06.043. J Mol Biol. 2005. PMID: 16024042

7

Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.

Bemporad F, Taddei N, Stefani M, Chiti F. Bemporad F, et al. Among authors: taddei n. Protein Sci. 2006 Apr;15(4):862-70. doi: 10.1110/ps.051915806. Protein Sci. 2006. PMID: 16600970 Free PMC article.

8

Sequence and structural determinants of amyloid fibril formation.

Bemporad F, Calloni G, Campioni S, Plakoutsi G, Taddei N, Chiti F. Bemporad F, et al. Among authors: taddei n. Acc Chem Res. 2006 Sep;39(9):620-7. doi: 10.1021/ar050067x. Acc Chem Res. 2006. PMID: 16981678 Review.

9

Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway.

Soldi G, Plakoutsi G, Taddei N, Chiti F. Soldi G, et al. Among authors: taddei n. J Med Chem. 2006 Oct 5;49(20):6057-64. doi: 10.1021/jm0606488. J Med Chem. 2006. PMID: 17004719

10

The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.

Monsellier E, Ramazzotti M, de Laureto PP, Tartaglia GG, Taddei N, Fontana A, Vendruscolo M, Chiti F. Monsellier E, et al. Among authors: taddei n. Biophys J. 2007 Dec 15;93(12):4382-91. doi: 10.1529/biophysj.107.111336. Epub 2007 Aug 31. Biophys J. 2007. PMID: 17766358 Free PMC article.

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