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1 that human retina expressed all GRKs except GRK4.
2 46 codons in the carboxyl-terminal domain of GRK4.
3 s explaining the generally low expression of GRK4.
4 f the three GRK subgroups (GRK1, GRK2/3, and GRK4/5/6) shares even a single intron in common, indicat
10 -activated D1R is regulated by both SNX5 and GRK4, and that SNX5 is critical to the recycling of the
11 through G-protein-coupled receptor kinase 4 (GRK4), comparatively little is known about other aspects
12 n this article, we present data showing that GRK4 constitutively phosphorylates the D1 receptor in th
13 lation resulting from mutationally activated GRK4 contributes to the heritable component of human ess
14 least, the G protein-coupled receptor kinase GRK4 does not display a preference for the agonist-occup
23 conservation, whereas GRK1 and particularly GRK4 have accumulated amino acid changes at extremely ra
27 amily (GRKs 4, 5, and 6) suggests that mouse GRK4 is not alternatively spliced in a manner analogous
30 regions undergo alternative splicing in the GRK4 mRNA, resulting from the presence or absence of exo
31 the regulation of blood pressure, and three GRK4 polymorphisms (R65L, A142V, and A486V) are associat
38 and 6 genes reveals that all members of the GRK4 subfamily share an identical gene structure, in whi
39 mediated exclusively by the alpha isoform of GRK4; the beta, gamma, and delta isoforms are ineffectiv
40 pliced in a manner analogous to human or rat GRK4, whereas GRK6 undergoes extensive alternative splic
41 a system incorporating constitutively active GRK4 will be prone to dysregulation, perhaps explaining
42 arison of the deduced amino acid sequence of GRK4 with those of the closely related GRK5 and GRK6 sug
43 sion of G-protein-coupled receptor kinase 4 (GRK4) with wild type receptor resulted in an increase in
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