Gαi-αs chimeras define the function of α chain domains in control of G protein activation and βγ subunit complex interactions
- 1 November 1990
- Vol. 63 (4) , 697-706
- https://doi.org/10.1016/0092-8674(90)90136-3
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Mutation of the Gs protein alpha subunit NH2 terminus relieves an attenuator function, resulting in constitutive adenylyl cyclase stimulation.Molecular and Cellular Biology, 1990
- Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformationNature, 1989
- Mutations in the GTP-binding site of GSα alter stimulation of adenylyl cyclaseJournal of Biological Chemistry, 1989
- Synthesis in Escherichia coli of GTPase-deficient mutants of GsαJournal of Biological Chemistry, 1989
- The G-Protein Family and Their Interaction with Receptors*Endocrine Reviews, 1989
- GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumoursNature, 1989
- Carboxyl Rerminal Domain of G sα Specifies Coupling of Receptors to Stimulation of Adenylyl CyclaseScience, 1988
- Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H- ras P21Science, 1988
- ras GENESAnnual Review of Biochemistry, 1987
- G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALSAnnual Review of Biochemistry, 1987