The DH and PH Domains of Trio Coordinately Engage Rho GTPases for their Efficient Activation
- 22 February 2007
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 368 (5) , 1307-1320
- https://doi.org/10.1016/j.jmb.2007.02.060
Abstract
No abstract availableKeywords
This publication has 70 references indexed in Scilit:
- The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activityBiochemical Journal, 2006
- GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factorsNature Reviews Molecular Cell Biology, 2005
- Developments in theCCP4 molecular-graphics projectActa Crystallographica Section D-Biological Crystallography, 2004
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Structural Analysis of Autoinhibition in the Ras Activator Son of SevenlessCell, 2004
- Structural basis for the selective activation of Rho GTPases by Dbl exchange factorsNature Structural & Molecular Biology, 2002
- The Guanine Nucleotide-Binding Switch in Three DimensionsScience, 2001
- Use of TLS parameters to model anisotropic displacements in macromolecular refinementActa Crystallographica Section D-Biological Crystallography, 2001
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983