Dissecting the Structure, Thermodynamic Stability, and Aggregation Properties of the A25T Transthyretin (A25T-TTR) Variant Involved in Leptomeningeal Amyloidosis: Identifying Protein Partners That Co-Aggregate during A25T-TTR Fibrillogenesis in Cerebrospinal Fluid-Reference-Cited by-同舟云学术

Dissecting the Structure, Thermodynamic Stability, and Aggregation Properties of the A25T Transthyretin (A25T-TTR) Variant Involved in Leptomeningeal Amyloidosis: Identifying Protein Partners That Co-Aggregate during A25T-TTR Fibrillogenesis in Cerebrospinal Fluid

Published:2011-11-30 Issue:51 Volume:50 Page:11070-11083
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Azevedo Estefania P. C.¹,Pereira Humberto M.²,Garratt Richard C.²,Kelly Jeffery W.³,Foguel Debora¹,Palhano Fernando L.¹³

Affiliation:

1. Instituto de Bioquímica Médica, Programa de Biologia Estrutural, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941-590 Brazil

2. Centro de Biotecnologia Molecular Estrutural, Instituto de Física de São Carlos, Universidade de São Paulo, São Paulo, 13560-970 Brazil

3. Departments of Chemistry and Molecular and Experimental Medicine and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201365r

Reference69 articles.

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4. 3D structure of Alzheimer's amyloid- (1-42) fibrils

5. A structural model for Alzheimer's -amyloid fibrils based on experimental constraints from solid state NMR

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