Chiti F - Search Results

1

Full-length TDP-43 and its C-terminal domain form filaments in vitro having non-amyloid properties.

Capitini C, Fani G, Vivoli Vega M, Penco A, Canale C, Cabrita LD, Calamai M, Christodoulou J, Relini A, Chiti F. Capitini C, et al. Among authors: chiti f. Amyloid. 2021 Mar;28(1):56-65. doi: 10.1080/13506129.2020.1826425. Epub 2020 Oct 7. Amyloid. 2021. PMID: 33026249 Free PMC article.

2

Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM. Chiti F, et al. Proc Natl Acad Sci U S A. 2002 Dec 10;99 Suppl 4(Suppl 4):16419-26. doi: 10.1073/pnas.212527999. Epub 2002 Oct 8. Proc Natl Acad Sci U S A. 2002. PMID: 12374855 Free PMC article.

3

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

4

Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils.

Relini A, Torrassa S, Rolandi R, Gliozzi A, Rosano C, Canale C, Bolognesi M, Plakoutsi G, Bucciantini M, Chiti F, Stefani M. Relini A, et al. Among authors: chiti f. J Mol Biol. 2004 May 14;338(5):943-57. doi: 10.1016/j.jmb.2004.03.054. J Mol Biol. 2004. PMID: 15111058

5

Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily.

Bemporad F, Capanni C, Calamai M, Tutino ML, Stefani M, Chiti F. Bemporad F, et al. Among authors: chiti f. Biochemistry. 2004 Jul 20;43(28):9116-26. doi: 10.1021/bi030238a. Biochemistry. 2004. PMID: 15248769

6

Reversal of protein aggregation provides evidence for multiple aggregated States.

Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM. Calamai M, et al. Among authors: chiti f. J Mol Biol. 2005 Feb 18;346(2):603-16. doi: 10.1016/j.jmb.2004.11.067. Epub 2004 Dec 30. J Mol Biol. 2005. PMID: 15670608

7

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: chiti f. 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

8

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: chiti f. J Mol Biol. 2005 Aug 26;351(4):910-22. doi: 10.1016/j.jmb.2005.06.043. J Mol Biol. 2005. PMID: 16024042

9

Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

Calamai M, Chiti F, Dobson CM. Calamai M, et al. Among authors: chiti f. Biophys J. 2005 Dec;89(6):4201-10. doi: 10.1529/biophysj.105.068726. Epub 2005 Sep 16. Biophys J. 2005. PMID: 16169975 Free PMC article.

10

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: chiti f. 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.

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