Literature DB >> 16981678

Sequence and structural determinants of amyloid fibril formation.

Francesco Bemporad1, Giulia Calloni, Silvia Campioni, Georgia Plakoutsi, Niccolo Taddei, Fabrizio Chiti.   

Abstract

Amyloid fibril formation is a process that represents an essential feature of the chemistry of proteins and plays a central role in human pathology and the biology of living organisms. In this Account, we shall describe some of the recent results on the sequence and structural determinants of protein aggregation. We shall describe the factors that govern aggregation of unfolded peptides and proteins. We shall then try to summarize the factors that pertain to the aggregation of partially structured states and will show that even fully folded states of proteins have an ability to aggregate into at least early oligomers with no need to undergo substantial conformational changes.

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Year:  2006        PMID: 16981678     DOI: 10.1021/ar050067x

Source DB:  PubMed          Journal:  Acc Chem Res        ISSN: 0001-4842            Impact factor:   22.384


  26 in total

1.  Characterizing intermolecular interactions that initiate native-like protein aggregation.

Authors:  Francesco Bemporad; Alfonso De Simone; Fabrizio Chiti; Christopher M Dobson
Journal:  Biophys J       Date:  2012-06-05       Impact factor: 4.033

2.  Dissecting the Structure-Function Relationship of a Fungicidal Peptide Derived from the Constant Region of Human Immunoglobulins.

Authors:  Tecla Ciociola; Thelma A Pertinhez; Laura Giovati; Martina Sperindè; Walter Magliani; Elena Ferrari; Rita Gatti; Tiziana D'Adda; Alberto Spisni; Stefania Conti; Luciano Polonelli
Journal:  Antimicrob Agents Chemother       Date:  2016-03-25       Impact factor: 5.191

3.  Structural and hydration properties of the partially unfolded states of the prion protein.

Authors:  Alfonso De Simone; Adriana Zagari; Philippe Derreumaux
Journal:  Biophys J       Date:  2007-05-04       Impact factor: 4.033

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

Authors:  Elodie Monsellier; Matteo Ramazzotti; Patrizia Polverino de Laureto; Gian-Gaetano Tartaglia; Niccolò Taddei; Angelo Fontana; Michele Vendruscolo; Fabrizio Chiti
Journal:  Biophys J       Date:  2007-08-31       Impact factor: 4.033

Review 5.  Amyloid formation by globular proteins under native conditions.

Authors:  Fabrizio Chiti; Christopher M Dobson
Journal:  Nat Chem Biol       Date:  2009-01       Impact factor: 15.040

6.  Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formation.

Authors:  Elisa A Waxman; Kristel L Emmer; Benoit I Giasson
Journal:  Biochem Biophys Res Commun       Date:  2009-12-21       Impact factor: 3.575

7.  The Effect of (-)-Epigallocatechin-3-Gallate on the Amyloid-β Secondary Structure.

Authors:  Atanu Acharya; Julia Stockmann; Léon Beyer; Till Rudack; Andreas Nabers; James C Gumbart; Klaus Gerwert; Victor S Batista
Journal:  Biophys J       Date:  2020-06-10       Impact factor: 4.033

Review 8.  Folding versus aggregation: polypeptide conformations on competing pathways.

Authors:  Thomas R Jahn; Sheena E Radford
Journal:  Arch Biochem Biophys       Date:  2007-06-08       Impact factor: 4.013

9.  Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.

Authors:  Rajamani Lakshminarayanan; Il Yoon; Balachandra G Hegde; Daming Fan; Chang Du; Janet Moradian-Oldak
Journal:  Proteins       Date:  2009-08-15

10.  Prediction of amyloid fibril-forming segments based on a support vector machine.

Authors:  Jian Tian; Ningfeng Wu; Jun Guo; Yunliu Fan
Journal:  BMC Bioinformatics       Date:  2009-01-30       Impact factor: 3.169

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