Structural Study of Metastable Amyloidogenic Protein Oligomers by Photo‐Induced Cross‐Linking of Unmodified Proteins-Reference-Cited by-同舟云学术

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Structural Study of Metastable Amyloidogenic Protein Oligomers by Photo‐Induced Cross‐Linking of Unmodified Proteins

Published:2006 Issue: Volume: Page:217-236
ISSN:0076-6879
Container-title:Amyloid, Prions, and Other Protein Aggregates, Part C
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Author:

Bitan Gal

Publisher

Elsevier

Reference62 articles.

1. ETS‐1 transcription factor binds cooperatively to the palindromic head to head ETS‐binding sites of the stromelysin‐1 promoter by counteracting autoinhibition;Baillat;J. Biol. Chem.,2002

2. The uvsY recombination protein of bacteriophage T4 forms hexamers in the presence and absence of single‐stranded DNA;Beernink;Biochemistry,1998

3. Neurotoxic protein oligomers—what you see is not always what you get;Bitan;Amyloid,2005

4. Amyloid β‐protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways;Bitan;Proc. Natl. Acad. Sci. USA,2003

5. Amyloid β‐protein oligomerization: Prenucleation interactions revealed by photo‐induced cross‐linking of unmodified proteins;Bitan;J. Biol. Chem.,2001

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