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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. The EMBO Journal, 30(20): 1, pp. 4185-4197. Retrieved from http://dx.doi.org/10.1038/emboj.2011.291.

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 Creators:
Miertzschke, Mandy1, Author
Koerner, Carolin1, Author
Vetter, Ingrid R.2, Author           
Keilberg, Daniela1, Author
Hot, Edina1, Author
Leonardy, Simone1, Author
Søgaard-Andersen, Lotte1, Author
Wittinghofer, Alfred3, Author           
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              
3Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753294              

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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: 2011-08-16
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 571333
URI: http://dx.doi.org/10.1038/emboj.2011.291
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Title: The EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 30 (20) Sequence Number: 1 Start / End Page: 4185 - 4197 Identifier: -