Thioflavin T Hydroxylation at Basic pH and Its Effect on Amyloid Fibril Detection-Reference-Cited by-同舟云学术

Thioflavin T Hydroxylation at Basic pH and Its Effect on Amyloid Fibril Detection

Published:2008-10-29 Issue:47 Volume:112 Page:15174-15181
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Foderà Vito¹,Groenning Minna¹,Vetri Valeria¹,Librizzi Fabio¹,Spagnolo Salvatore¹,Cornett Claus¹,Olsen Lars¹,van de Weert Marco¹,Leone Maurizio¹

Affiliation:

1. Dipartimento di Scienze Fisiche e Astronomiche, Università degli Studi di Palermo, Via Archirafi 36, 90123 Palermo, Italy, CNR - Istituto di Biofisica, U.O. Via U. La Malfa 153, 90146 Palermo, Italy, Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen Ø, Denmark, and Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100...

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp805560c

Reference56 articles.

1. Protein misfolding, evolution and disease

2. Designing conditions for in vitro formation of amyloid protofilaments and fibrils

3. Effects of intermediates on aggregation of native bovine serum albumin

4. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases

5. Conformational changes involved in thermal aggregation processes of bovine serum albumin

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