Literature DB >> 9195890

Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases.

J W Kelly1.   

Abstract

The assembly and misassembly of normally soluble proteins into fibrilar structures is thought to be a causative agent in a variety of human amyloid and prion diseases. Structural and mechanistic studies of this process are beginning to elucidate the conformational changes required for the conversion of a normally soluble and functional protein into a defined quaternary structure.

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Year:  1997        PMID： 9195890     DOI： 10.1016/s0969-2126(97)00215-3

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  43 in total

1.  Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB.

Authors:  M Gross; D K Wilkins; M C Pitkeathly; E W Chung; C Higham; A Clark; C M Dobson
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

2.  Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type.

Authors:  R L Isaacson; A G Weeds; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

3.  Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the lipid bilayer.

Authors:  A S Ulrich; W Tichelaar; G Förster; O Zschörnig; S Weinkauf; H W Meyer
Journal:  Biophys J       Date:  1999-08       Impact factor: 4.033

4.  Protein engineering as a strategy to avoid formation of amyloid fibrils.

Authors:  V Villegas; J Zurdo; V V Filimonov; F X Avilés; C M Dobson; L Serrano
Journal:  Protein Sci       Date:  2000-09       Impact factor: 6.725

5.  Conformational behavior of ionic self-complementary peptides.

Authors:  M Altman; P Lee; A Rich; S Zhang
Journal:  Protein Sci       Date:  2000-06       Impact factor: 6.725

6.  Self-assembly properties of a model RING domain.

Authors:  Alex Kentsis; Ronald E Gordon; Katherine L B Borden
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-15       Impact factor: 11.205

7.  The pH-dependent stability of wild-type and mutant transthyretin oligomers.

Authors:  S Skoulakis; J M Goodfellow
Journal:  Biophys J       Date:  2003-05       Impact factor: 4.033

8.  Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation: a mechanistic study.

Authors:  Giorgio Colombo; Giacomo M S De Mori; Danilo Roccatano
Journal:  Protein Sci       Date:  2003-03       Impact factor: 6.725

9.  Competing intrachain interactions regulate the formation of beta-sheet fibrils in bovine PrP peptides.

Authors:  Abdessamad Tahiri-Alaoui; Mario Bouchard; Jesús Zurdo; William James
Journal:  Protein Sci       Date:  2003-03       Impact factor: 6.725

10.  Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.

Authors:  Bishwajit Kundu; Nilesh R Maiti; Eric M Jones; Krystyna A Surewicz; David L Vanik; Witold K Surewicz
Journal:  Proc Natl Acad Sci U S A       Date:  2003-09-30       Impact factor: 11.205
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