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1 P321A was coexpressed with RAMP1, RAMP2, or RAMP3.
2 medullin receptors are comprised of RAMP2 or RAMP3 (AM1R and AM2R, respectively) and calcitonin recep
4 as to identify other interaction partners of RAMP3 and determine their role in CRLR-RAMP3 trafficking
5 ssays and mutational analysis indicated that RAMP3 and NHERF-1 interact via a PDZ type I domain on NH
7 mesangial cells, where RNA interference with RAMP3 and pharmacological inhibition of NSF both resulte
9 MP2 is required for survival, mice that lack RAMP3 appear normal until old age, at which point they h
10 g secretin receptor expression competing for RAMP3 association with the calcitonin receptor-like rece
12 Z type I domain present in the C terminus of RAMP3, but not in RAMP1 or RAMP2, leads to protein-prote
15 ubule cells endogenously expressing the CRLR-RAMP3 complex and NHERF-1, the CRLR-RAMP complex desensi
16 NHERF-1 indicated that NHERF-1 inhibits CRLR/RAMP3 complex internalization by tethering the complex t
17 leimide-sensitive factor (NSF) with the CRLR-RAMP3 complex, but not CRLR-RAMP1 or CRLR-RAMP2 complex,
20 replaced with the corresponding region from RAMP3, dual topology was retained but MRAP was inactive.
23 Therefore, to determine whether RAMP2 and RAMP3 have distinct functions in vivo, we generated mice
24 ertheless, our studies reveal that RAMP2 and RAMP3 have distinct physiological functions throughout e
25 on in mice results in elevated expression of Ramp3 in mammary tissue through augmented promoter-enhan
26 s, indicate a novel function for NHERF-1 and RAMP3 in the internalization of the AM receptor and sugg
27 These results indicate a novel function for RAMP3 in the post-endocytic sorting of the AM-R and sugg
28 GPCR interaction map suggests that RAMP1 and RAMP3 interact with the same set of GPCRs, which implies
29 t new insights into the structural basis for RAMP3 interaction with a family B G protein-coupled rece
30 t mutations, indicated that the PDZ motif of RAMP3 interacts with NSF to cause the change in traffick
31 ed on combined expression level of HN1, RAN, RAMP3, KRT19, and TAF9, was associated with disease-spec
36 LR when co-expressed with RAMP1 and RAMP2 or RAMP3, respectively, intermedin represents a nonselectiv
38 f HAECs with CRLR or RAMP2, but not RAMP1 or RAMP3, siRNAs abolished protection by IMD (1 nmol l(-)(1
39 ) and receptor activity modifying protein 3 (RAMP3) to inhibit glycolysis and induce reactive oxygen
41 e of NHERF-1, although the AM receptor (CRLR/RAMP3) undergoes desensitization, the internalization of
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