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  The crystal structure of dipeptidyl peptidase IV(CD26) reveals its functional regulation and enzymatic mechanism

Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., et al. (2003). The crystal structure of dipeptidyl peptidase IV(CD26) reveals its functional regulation and enzymatic mechanism. Proceedings of the National Academy of Sciences of the United States of America, 100(9), 5063-5068.

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

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 Creators:
Engel, M.1, Author              
Hoffmann, T., Author
Wagner, L., Author
Wermann, M., Author
Heiser, U., Author
Kiefersauer, R.1, Author              
Huber, R.1, Author              
Bode, W.1, 2, 3, Author              
Demuth, H. U., Author
Brandstetter, H.1, Author              
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: serine protease, oxyanion hole, substrate channeling, drug design, diabetes mellitus
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Language(s): eng - English
 Dates: 2003-04-29
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 123110
ISI: 000182612600020
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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: 100 (9) Sequence Number: - Start / End Page: 5063 - 5068 Identifier: ISSN: 0027-8424