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  Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity

Miertzschke, M., Koerner, C., Vetter, I. R., Keilberg, D., Hot, E., Leonardy, S., et al. (2011). Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity. EMBO Journal, 30(20), 4185-4197.

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 Creators:
Miertzschke, M., Author
Koerner, C., Author
Vetter, I. R., Author
Keilberg, D.1, Author           
Hot, E.1, Author           
Leonardy, S.1, Author           
Sogaard-Andersen, L.1, Author           
Wittinghofer, A., Author
Affiliations:
1Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266305              

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Free keywords: bacterial Ras-like G protein; cell polarity; GTPase-activating protein; intrinsic arginine finger; Roadblock/LC7 domain
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Language(s): eng - English
 Dates: 2011-10-19
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 583318
ISI: 000296715800008
 Degree: -

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Title: EMBO Journal
  Alternative Title : Embo J.
Source Genre: Journal
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Publ. Info: NEW YORK : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 30 (20) Sequence Number: - Start / End Page: 4185 - 4197 Identifier: ISSN: 0261-4189