High-Resolution Structure of the Ra-Domain of Human Ralgds and a Dynamics Study of its Binding Loop to Ras
To be Published
PRIMARY
Three-dimensional structure of the Ras-interacting domain of RalGDS.
Nat.Struct.Biol. (1997)
Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling.
Nat.Struct.Biol. (1997)
;Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor.
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J.Biol.Chem. (1996)
;Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap.
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Proc.Natl.Acad.Sci.USA (1994)
Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.
Proc.Natl.Acad.Sci.USA (1994)
Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase.
Embo J. (1993)