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Amyloid Formation from HypF-N under Conditions in which the Protein is Initially in its Native State

  • Published:2005-03 Issue:2 Volume:347 Page:323-335
  • ISSN:0022-2836
  • Container-title:Journal of Molecular Biology
  • language:en
  • Short-container-title:Journal of Molecular Biology

Author:

Marcon Giordana,Plakoutsi Georgia,Canale Claudio,Relini Annalisa,Taddei Niccolò,Dobson Christopher M.,Ramponi Giampietro,Chiti Fabrizio

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference52 articles.

1. Protein folding and misfolding;Dobson;Nature,2003

2. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution;Stefani;J. Mol. Med.,2003

3. Conformational constraints for amyloid fibrillation: the importance of being unfolded;Uversky;Biochem. Biophys. Acta,2004

4. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration;Walsh;Protein Pept. Letters,2004

5. The structure of amyloid fibrils by electron microscopy and X-ray diffraction;Sunde;Advan. Protein Chem.,1997
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