The Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras
The first step of RAF activation involves binding to active RAS, resulting in the recruitment of RAF...
RGL2 [RalGDS (Ral guanine nucleotide dissociation stimulator)-like 2] is a member of the RalGDS fami...
Ras proteins function as molecular switches that are activated in response to signalling pathways in...
AbstractThe structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-...
The structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-RBD), th...
To identify proteins that bind to the Ras-related protein R-ras we performed a yeast two-hybrid cDNA...
AbstractThe RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identif...
Small GTPases of the Ras family are major players of signal transduction in eukaryotic cells. They r...
Small GTPases of the Ras family are major players of signal transduction in eukaryotic cells. They r...
AbstractThe three-dimensional structure of the complex between Rap and the ‘Ras-binding domain’ of R...
Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This pr...
Common domain databases contain sequence motifs which belong to the ubiquitin fold family and are ca...
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies ...
The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor Ral...
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies ...
The first step of RAF activation involves binding to active RAS, resulting in the recruitment of RAF...
RGL2 [RalGDS (Ral guanine nucleotide dissociation stimulator)-like 2] is a member of the RalGDS fami...
Ras proteins function as molecular switches that are activated in response to signalling pathways in...
AbstractThe structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-...
The structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-RBD), th...
To identify proteins that bind to the Ras-related protein R-ras we performed a yeast two-hybrid cDNA...
AbstractThe RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identif...
Small GTPases of the Ras family are major players of signal transduction in eukaryotic cells. They r...
Small GTPases of the Ras family are major players of signal transduction in eukaryotic cells. They r...
AbstractThe three-dimensional structure of the complex between Rap and the ‘Ras-binding domain’ of R...
Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This pr...
Common domain databases contain sequence motifs which belong to the ubiquitin fold family and are ca...
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies ...
The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor Ral...
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies ...
The first step of RAF activation involves binding to active RAS, resulting in the recruitment of RAF...
RGL2 [RalGDS (Ral guanine nucleotide dissociation stimulator)-like 2] is a member of the RalGDS fami...
Ras proteins function as molecular switches that are activated in response to signalling pathways in...