English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Files

show Files
hide Files
:
2407599.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
2407599.pdf
Description:
-
OA-Status:
Visibility:
Restricted (UNKNOWN id 303; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2407599_Suppl.pdf (Supplementary material), 286KB
Name:
2407599_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 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              

Content

show
hide
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.

Details

show
hide
Language(s): eng - English
 Dates: 2016-11-252016-12-23
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201608516
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 55 (52) Sequence Number: - Start / End Page: 16168 - 16171 Identifier: -