Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS)-Reference-Cited by-同舟云学术

Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS)

Published:2012-09-07 Issue:11 Volume:41 Page:931-938
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

de la Arada Igor,Seiler Christian,Mäntele Werner

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/s00249-012-0845-1.pdf

Reference34 articles.

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3. Bramanti E, Benedetti E (1996) Determination of the secondary structure of isomeric forms of human serum albumin by a particular frequency deconvolution procedure applied to Fourier-transform IR analysis. Biopolymers 38:639–653

4. Bucciantini M, Giannoni E, Chiti F et al (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416:507–511

5. Cerdà-Costa N, Esteras-Chopo A, Avilés FX et al (2007) Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J Mol Biol 366:1351–1363

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