Titlebook: Ras Superfamily Small G Proteins: Biology and Mechanisms 1; General Features, Si Alfred Wittinghofer Book 2014 Springer-Verlag Wien 2014 GT

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Bacterial Protein Toxins Acting on Small GTPasesate their switch functions. Frequent targets are Rho, Ras, and Rab proteins which are modified by ADP-ribosylation, adenylylation, mono-.-glycosylation, deamidation, transglutamination, phosphocholination, and proteolytic cleavage. Thereby, the GTPases are activated or inactivated. Other bacterial e

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Digitalis

Targeting the Raf-MEK-ERK Mitogen-Activated Protein Kinase Cascade for the Treatment of , Mutant Cankey driver roles in cancer development and growth. Consequently, there has been considerable interest and effort in developing therapeutic approaches for blocking aberrant Ras function for cancer treatment. Despite over three decades of intensive effort, to date no effective anti-Ras therapeutic app

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Detonate

Mouse Models of RAS-Induced Tumors and Developmental Disordersnoma, colorectal carcinoma, pancreatic ductal adenocarcinoma, and metastatic melanoma. In spite of the significant amount of knowledge accumulated over the last three decades regarding the molecular mechanisms by which RAS oncogenes induce malignant transformation, to date there are no efficacious t

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SOBER

The Coordinated Biology and Signaling Partners of Ral G-Proteinsdivergent roles in regulating distinct biological processes. As downstream signaling partners of oncogenic Ras, these two proteins have been described to be hyper-activated in tumors to support aberrant biology during oncogenic transformation. To regulate a varied collection of normal and oncogenic

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Structure and Function of the mTOR Activator Rhebsmall GTPase protein that is ubiquitously expressed from yeast to mammals. Rheb is most similar to Rap and Ras GTPases; however, it bears amino acid substitutions to key conserved residues in the G1 box. Rheb possesses a C-terminal CaaX box motif that is modified by attachment of a farnesyl isopreno