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Single nucleotide polymorphism of RAMP2 is associated with Stroke.
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This work suggests that RAMP2 may modify the agonist activity and trafficking of the GCGR, with potential relevance to production of new peptide analogs with selective agonist activities.
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Data suggest that a single GlcNAc residue at CTR N130 (asparagine 130) is responsible for enhanced affinity of calcitonin for CTR ECD; the same appears to apply for enhanced affinity of amylin for RAMP2-CTR ECD. [GlcNAc = N-acetylglucosamine; CTR = calcitonin receptor; ECD = extracellular domain; RAMP2 = receptor (calcitonin) activity modifying protein 2].
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interaction of RAMP2 or RAMP3 with CLR induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
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This study reveals the glucagon receptor as a previously unidentified target for GLP-1 receptor agonists and highlights a role for RAMP2 in regulating its pharmacology.
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Data suggest that ligand binding of a G protein-coupled receptor (GPCR) may inform drug development targeting calcitonin receptor-like receptor (CLR):receptor activity-modifying proteins RAMP1/2 complexes.
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the AM system is widely expressed in human thymus from newborns; both AM1 receptor components CLR and RAMP2, but not RAMP3, are not associated with the plasma membrane of TECs and thymocytes but are located intracellularly, notably in the nucleus
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Adrenomedullin-RAMP2 system suppresses ER stress-induced tubule cell death and is involved in kidney protection.
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Data suggest isoforms of RAMP modulate accessibility of peptides to residues situated on CALCRL (calcitonin receptor-like receptor) N-terminal domain; RAMP3/RAMP2/RAMP1 appear to alter accessibility of specific residues at CALCRL-RAMP interface.
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RAMP2 gene expression increases with gestational age development in the fetal lung.
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The CRLR-RAMP2 interactions were confirmed for the full-length proteins on the cell surface by site-specific photo-crosslinking.
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the hCRLR C-tail is crucial for adrenomedullin-evoked cAMP production and internalization of the CRLR/RAMP2, while the receptor internalization is dependent on the aforementioned GPCR kinases, but not Gs coupling.
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results show the presence of calcitonin receptor-like receptor and receptor activity-modifying proteins in middle meningeal, middle cerebral, pial, and superficial temporal vessels
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Co-expression of calcitonin receptors (CT) lacking a portion of domain 1 with receptor activity-modifying protein (RAMP) 1, 2, or 3 appears to produce functional CT-(8-32)-sensitive adrenomedullin receptors.
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TNF-alpha induced time- and dose-dependent decreases in the expression of RAMP2 mRNA in cultured human coronary artery smooth muscle cells , thereby diminishing AM-evoked cAMP production
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Data found that expressions of RAMP1, RAMP2 and RAMP3 mRNAs increased with the worsening of heart function, but the expressions of RAMP1 and RAMP2 mRNA decreased at level IV of heart failure.
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adrenomedullin receptors are comprised of RAMP2 and calcitonin receptor-like receptor.
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the respective C-tails of hRAMP2 and -3 differentially affect hCRLR surface delivery and internalization
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This study reveals important functionality of the RAMP C-terminal domain and identifies key differences in the role of the RAMP C terminus for calcitonin receptor versus calcitonin receptor-like receptor-based receptors.
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RAMP2 is silenced by promoter hypermethylation in lung cancer
