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pro vyhledávání: '"D. J. Gawler"'
Autor:
Dennis Wray, D. J. Gawler, Hugh A. Pearson, V A Porter, Nigel Hodson, Carol J. Milligan, Lin-Hua Jiang
Publikováno v:
Journal of Biological Chemistry. 275:6135-6143
We have studied the effect of 8-bromo-cyclic GMP (8-Br-cGMP) on cloned cardiac L-type calcium channel currents to determine the site and mechanism of action underlying the functional effect. Rabbit cardiac alpha(1C) subunit, in the presence or absenc
Publikováno v:
The Journal of biological chemistry. 271(40)
The CaLB domain is a 43-amino acid sequence motif found in a number of functionally diverse signaling proteins including three Ras-specific GTPase activating proteins (GAPs). In the Ras GTPase activating protein, P120(GAP), this domain has the abilit
p120 GAP is a GTPase activating protein for p21 ras. It is a multidomain protein which exhibits sequence similarity with other GTPase-activating proteins, src, pleckstrin and a central portion of the protein kinase C conserved region 2 domain known a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45bd2b84b242527ff81490b888d67bf8
https://europepmc.org/articles/PMC1136674/
https://europepmc.org/articles/PMC1136674/
Publikováno v:
Oncogene. 10(5)
CaLB was originally observed as a conserved sequence motif in various calcium-responsive signalling proteins and also in p120 Ras GTPase activating protein (p120GAP) (Clark et al. Cell 65: 1043-1051, 1991). Here we show the 43 residue CaLB motif in p
Publikováno v:
Cellular signalling. 1(1)
Hepatocyte membranes from both lean and obese Zucker rats exhibited adenylate cyclase activity that could be stimulated by glucagon, forskolin, NaF and elevated concentrations of p[NH]ppG. In membranes from lean animals, functional Gi was detected by