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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
3 drenomedullin (AM), is comprised of RAMP2 or RAMP3 and calcitonin receptor-like receptor (CRLR).
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
6                                  The role of RAMP3 and NSF in AM2R recycling was confirmed in rat mes
7 mesangial cells, where RNA interference with RAMP3 and pharmacological inhibition of NSF both resulte
8                               Because RAMP2, RAMP3, and CLR transduce the signaling of the two potent
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
11                                              RAMP3 association with this receptor was shown to be cap
12 Z type I domain present in the C terminus of RAMP3, but not in RAMP1 or RAMP2, leads to protein-prote
13 cretin receptor associates specifically with RAMP3, but not with RAMP1 or RAMP2.
14                       Mutational analysis of RAMP3, by deletion and point mutations, indicated that t
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,
18 strates that the Wap super-enhancer controls Ramp3, despite three separating CTCF sites.
19 ce with reduced expression of RAMP2 (but not RAMP3) display remarkable subfertility.
20  replaced with the corresponding region from RAMP3, dual topology was retained but MRAP was inactive.
21  distal CTCF-binding site results in loss of Ramp3 expression in non-mammary tissues.
22 th targeted deletions of either the RAMP2 or RAMP3 gene.
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
32 AP residues 29-37 conferred dual topology to RAMP3, normally in an Nexo/Ccyt orientation.
33                         Knock-down of either RAMP3 or NHERF-1 by RNA interference technology enabled
34                         It is now known that RAMP3 protein-protein interactions regulate the recyclin
35 tivity-modifying proteins 2 and 3 (RAMP2 and RAMP3), respectively.
36 LR when co-expressed with RAMP1 and RAMP2 or RAMP3, respectively, intermedin represents a nonselectiv
37          Co-expression of CRLR with RAMP2 or RAMP3 resulted in a response with the pharmacological pr
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
40 rs of RAMP3 and determine their role in CRLR-RAMP3 trafficking.
41 e of NHERF-1, although the AM receptor (CRLR/RAMP3) undergoes desensitization, the internalization of
42             However, mRNA encoding RAMP2 and RAMP3 was also detected in the gastrointestinal tract, D
43               IMD and CRLR, RAMP1, RAMP2 and RAMP3 were expressed in all cell types.When cells were t
44                  The interaction of RAMP2 or RAMP3 with CLR induces conformational variation in the j

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