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1 Calcitonin receptor-like receptor (CLR) and receptor activity modifying protein 1 (RAMP1) comprise a
3 on together with its two accessory proteins, receptor activity modifying protein 1 and CGRP-receptor
4 he calcitonin receptor-like receptor and the receptor activity modifying protein 1, within the area o
8 the calcitonin receptor (CTR) interact with receptor activity-modifying protein 1 (RAMP1) at the cel
9 citonin receptor-like receptor (CLR) and the receptor activity-modifying protein 1 (RAMP1) comprise a
10 calcitonin receptor-like receptor (CLR) and receptor activity-modifying protein 1 (RAMP1), and the d
11 ith calcitonin receptor-like receptor (CLR), receptor activity-modifying protein 1 (RAMP1), beta-arre
12 Our findings demonstrate that a single gene, receptor activity-modifying protein 1 (RAMP1), can be a
13 calcitonin receptor-like receptor (CLR) and receptor activity-modifying protein 1 (RAMP1), respectiv
15 in vitro and in vivo by expression of human receptor activity-modifying protein-1 (hRAMP1), an oblig
16 evealed marked anatomical gradients for both receptor activity-modifying protein-1 (RAMP-1) and calci
17 lcitonin receptor-like receptor (Calcrl) and receptor activity modifying protein 2/3, are highly expr
18 citonin receptor-like receptor (CLR) and the receptor activity-modifying protein 2 (RAMP2) comprise a
19 calcitonin receptor-like receptor (CLR), and receptor activity-modifying proteins 2 and 3 (RAMP2 and
20 iation with the receptor-interacting protein receptor activity-modifying protein-2 (RAMP2), and the r
21 through the calcitonin receptor (CalcR) and receptor activity modifying protein 3 (RAMP3) to inhibit
23 ptor, calcitonin receptor-like receptor, and receptor activity-modifying proteins in human microvesse
24 mbrane-domain proteins, which we have called receptor-activity-modifying proteins or RAMPs, are expre
26 eceptor (CRLR) with different members of the receptor activity modifying protein (RAMP) family, which
28 CR) which requires coexpression of different receptor activity modifying proteins (RAMP) to become a
30 A library, we isolated a cDNA clone encoding receptor activity-modifying protein (RAMP)-like triterpe
34 alcitonin receptor-like receptor (CRLR), and receptor activity modifying proteins (RAMPs) have become
39 or-like receptor (CRLR) and one of the three receptor activity-modifying proteins (RAMPs) showed that
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