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  Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein

Wolschner, C., Giese, A., Kretzschmar, H. A., Huber, R., Moroder, L., & Budisa, N. (2009). Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proceedings of the National Academy of Sciences of the United States of America, 106(19), 7756-7761.

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Genre: Journal Article
Alternative Title : Proc. Natl. Acad. Sci. U. S. A.

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 Creators:
Wolschner, C.1, Author           
Giese, A., Author
Kretzschmar, H. A., Author
Huber, R.2, Author           
Moroder, L.3, Author           
Budisa, N.1, Author           
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
3Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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Free keywords: conformational switch; expanded genetic code; methionine sulfoxide reductase; noncanonical analogs; unnatural amino acid sequence
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Language(s): eng - English
 Dates: 2009-05-12
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 432118
ISI: 000266208900017
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 106 (19) Sequence Number: - Start / End Page: 7756 - 7761 Identifier: ISSN: 0027-8424