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  Structure of monomeric transthyretin carrying the clinically important T119M mutation.

Kim, J. H., Oroz, J., & Zweckstetter, M. (2016). Structure of monomeric transthyretin carrying the clinically important T119M mutation. Angewandte Chemie International Edition, 55(52), 16168-16171. doi:10.1002/anie.201608516.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-A696-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-A69B-6
Genre: Journal Article

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2407599.pdf (Publisher version), 2MB
 
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 Creators:
Kim, J. H., Author
Oroz, J.1, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              

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Free keywords: NMR spectroscopy; protein structures; transthyretin
 Abstract: Mutations in the protein transthyretin can cause as well as protect individuals from transthyretin amyloidosis, an incurable fatal inherited disease. Little is known, however, about the structural basis of pathogenic and clinically protective transthyretin mutants. Here we determined the solution structure of a transthyretin monomer that carries the clinically important T119M mutation. The structure displays a non-native arrangement that is distinct from all known structures of transthyretin and highlights the importance of high-resolution studies in solution for understanding molecular processes that lead to amyloid diseases.

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Language(s): eng - English
 Dates: 2016-11-252016-12-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201608516
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 55 (52) Sequence Number: - Start / End Page: 16168 - 16171 Identifier: -