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      GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours.

      Nature

      Adenylate Cyclase, metabolism, Amino Acid Sequence, Arginine, genetics, GTP Phosphohydrolases, antagonists & inhibitors, GTP-Binding Proteins, Glutamine, Humans, Mutation, Neoplasm Proteins, Phosphoric Monoester Hydrolases, Pituitary Neoplasms, enzymology, Proto-Oncogene Proteins

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          Abstract

          A subset of growth hormone-secreting human pituitary tumours carries somatic mutations that inhibit GTPase activity of a G protein alpha chain, alpha(s). The resulting activation of adenylyl cyclase bypasses the cells' normal requirement for trophic hormone. Amino acids substituted in the putative gsp oncogene identify a domain of G protein alpha-chains required for intrinsic ability to hydrolyse GTP. This domain may serve as a built-in counter-part of the separate GTPase-activating proteins required for GTP hydrolysis by small GTP-binding proteins such as p21ras.

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          Journal
          2549426
          10.1038/340692a0

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