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  Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif

Messerschmidt, A., Macieira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., et al. (2005). Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. Journal of Molecular Biology, 352(4), 918-931.

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Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Messerschmidt, A.1, Author           
Macieira, Sofia1, Author           
Velarde, Milko1, Author           
Badeker, M., Author
Benda, C.2, Author           
Jestel, A., Author
Brandstetter, H.2, Author           
Neuefeind, T., Author
Blaesse, M., Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2External Organizations, ou_persistent22              

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Free keywords: AGC protein kinase; bis(indolyl)maleimide 1 inhibitor; atypical protein kinase C; turn motif phosphorylation; X-ray structure
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Language(s): eng - English
 Dates: 2005-09-30
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 256273
ISI: 000232188100012
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 352 (4) Sequence Number: - Start / End Page: 918 - 931 Identifier: ISSN: 0022-2836