Literature DB >> 8696966

Alternative conformations of amyloidogenic proteins govern their behavior.

J W Kelly1.   

Abstract

Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.

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Year:  1996        PMID： 8696966     DOI： 10.1016/s0959-440x(96)80089-3

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  128 in total

1.  Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical.

Authors:  D T Downing; N D Lazo
Journal:  Biochem J       Date:  1999-10-15       Impact factor: 3.857

2.  Conformational propagation with prion-like characteristics in a simple model of protein folding.

Authors:  P M Harrison; H S Chan; S B Prusiner; F E Cohen
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

3.  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

4.  De novo amyloid proteins from designed combinatorial libraries.

Authors:  M W West; W Wang; J Patterson; J D Mancias; J R Beasley; M H Hecht
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

5.  Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution.

Authors:  S Goda; K Takano; Y Yamagata; R Nagata; H Akutsu; S Maki; K Namba; K Yutani
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

6.  Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments.

Authors:  J E Padilla; C Colovos; T O Yeates
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-20       Impact factor: 11.205

7.  An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid.

Authors:  M Balbirnie; R Grothe; D S Eisenberg
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-20       Impact factor: 11.205

8.  WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state.

Authors:  E K Koepf; H M Petrassi; M Sudol; J W Kelly
Journal:  Protein Sci       Date:  1999-04       Impact factor: 6.725

9.  A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro.

Authors:  M Ramirez-Alvarado; J S Merkel; L Regan
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-01       Impact factor: 11.205

10.  Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics.

Authors:  R I Dima; D Thirumalai
Journal:  Protein Sci       Date:  2002-05       Impact factor: 6.725
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