On the use of size exclusion chromatography for the resolution of mixed amyloid aggregate distributions: I. Equilibrium partition models-Reference-Cited by-同舟云学术

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On the use of size exclusion chromatography for the resolution of mixed amyloid aggregate distributions: I. Equilibrium partition models

Published:2012-07 Issue:1 Volume:426 Page:69-85
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Hall Damien,Huang Li

Funder

Young Scientists’ Independent Researc

Japanese Ministry of Education, Culture, Sports, Science, and Technology

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference107 articles.

1. β-Pleated sheet fibrils: a comparison of native amyloid with synthetic protein fibrils;Glenner;J. Histochem. Cytochem.,1974

2. The structural basis of protein folding and its links with human disease;Dobson;Philos. Trans. R Soc. Lond. B,2001

3. Amyloid fibril formation by an SH3 domain;Inaki Guijarro;Proc. Natl. Acad. Sci. USA,1998

4. Structure–activity relationship of amyloid fibrils;Maji;FEBS Lett.,2009

5. Prions and protein-folding diseases;Norrby;J. Intern. Med.,2011

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2. Biophysical Reviews’ “Meet the Editors Series”: a profile of Damien Hall;Biophysical Reviews;2023-12

3. A fortunate period of overlap with Prof. Haruki Nakamura;Biophysical Reviews;2022-12

4. Size exclusion chromatography (SEC);Particle Separation Techniques;2022

5. Synthesis and study of macrocyclic β-hairpin peptides for investigating amyloid oligomers;Synthetic and Enzymatic Modifications of the Peptide Backbone;2021

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