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1 ity-modifying proteins (RAMPs) showed that a CRLR/RAMP receptor complex is required for intermedin si
2 tonin receptor-like receptor (CRLR), while a CRLR heterodimer with RAMP1 yields a calcitonin gene-rel
7 r in the regulation of peripheral tissues by CRLR and will allow development of new therapeutic agent
8 ing ligand specificity, we have co-expressed CRLR and RAMP proteins in the yeast Saccharomyces cerevi
11 etermined the transcriptional start of human CRLR cDNA by 5'-RACE and cloned the proximal 5'-flanking
12 we demonstrated that co-expression of human CRLR with rat RAMP1 produced rat receptor pharmacology,
13 ragment contains the basal promoter of human CRLR, including potential TATA-boxes and several GC boxe
15 igher affinity for the human receptor, human CRLR/human RAMP1, than for the rat receptor, rat CRLR/ra
17 n on NHERF-1 indicated that NHERF-1 inhibits CRLR/RAMP3 complex internalization by tethering the comp
19 r (NSF) with the CRLR-RAMP3 complex, but not CRLR-RAMP1 or CRLR-RAMP2 complex, altered receptor traff
21 e hypothesize that the Nt-domain of CRLR (Nt-CRLR) is an autonomously folded unit possessing a well-d
26 together, our data provide evidence that Nt-CRLR is structured and further that a significant part o
28 uctural and functional information on the Nt-CRLR, we cloned and expressed the Nt-CRLR as a fusion pr
31 s in yeast, indicating that glycosylation of CRLR is not the prime determinant of ligand specificity.
32 ons in mammalian cells, the glycosylation of CRLR was not affected by the presence of RAMPs in yeast,
33 imultaneous transcriptional up-regulation of CRLR and its ligand adrenomedullin in endothelial cells
36 hich exhibited a preferential stimulation of CRLR when co-expressed with RAMP1 and RAMP2 or RAMP3, re
37 he CRLR-RAMP3 complex, but not CRLR-RAMP1 or CRLR-RAMP2 complex, altered receptor trafficking to a re
40 kawa cells express the putative ADM-receptor CRLR-RAMP2 the production and secretion of ADM with the
41 esence of NHERF-1, although the AM receptor (CRLR/RAMP3) undergoes desensitization, the internalizati
42 ession of calcitonin receptor-like receptor (CRLR) and an accessory protein called receptor activity-
43 combinant calcitonin receptor-like receptor (CRLR) and one of the three receptor activity-modifying p
44 tor named calcitonin receptor-like receptor (CRLR) has been identified, and in this study RCP co-immu
46 on of the calcitonin receptor-like receptor (CRLR) with different members of the receptor activity mo
47 zation of calcitonin receptor-like receptor (CRLR) with receptor activity-modifying protein 1 (RAMP 1
48 or (GPCR) calcitonin receptor-like receptor (CRLR), and receptor activity modifying proteins (RAMPs)
49 ains, the calcitonin-receptor-like receptor (CRLR), can function as either a CGRP receptor or an adre
50 vely) and calcitonin receptor-like receptor (CRLR), while a CRLR heterodimer with RAMP1 yields a calc
51 receptor calcitonin receptor-like receptor (CRLR), with specificity being conferred by the receptor
54 ts of at least three proteins: the receptor (CRLR), the chaperone protein (RAMP), and RCP that couple
55 sing the CRLR-RAMP3 complex and NHERF-1, the CRLR-RAMP complex desensitizes but is unable to internal
56 oscopy, we observed that in HEK293 cells the CRLR-RAMP complex undergoes agonist-stimulated desensiti
57 mal tubule cells endogenously expressing the CRLR-RAMP3 complex and NHERF-1, the CRLR-RAMP complex de
60 hylmaleimide-sensitive factor (NSF) with the CRLR-RAMP3 complex, but not CRLR-RAMP1 or CRLR-RAMP2 com
62 P and adrenomedullin can both signal through CRLR, which has been previously shown to require a chape
63 peptide family capable of signaling through CRLR/RAMP receptor complexes provides an additional play
66 examined for their ability to associate with CRLR to effect CGRP-stimulated cAMP accumulation, CGRP b
67 l RAMP 1 mutants were able to associate with CRLR with full efficacy for CGRP-stimulated cAMP accumul
69 in this study RCP co-immunoprecipitated with CRLR indicating that these two proteins interact directl
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