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British Journal of Pharmacology, ISSN 0007-1188, 02/2014, Volume 171, Issue 3, pp. 772 - 788
Background and Purpose Receptor activity‐modifying proteins (RAMPs) define the pharmacology of the calcitonin receptor‐like receptor (CLR). The interactions of... 
GPCR | adrenomedullin | RAMP | CGRP | receptor activity‐modifying protein | receptor activity-modifying protein | CRYSTAL-STRUCTURE | EXTRACELLULAR DOMAIN | N-TERMINUS | FAMILY | CORTICOTROPIN-RELEASING-FACTOR | STRUCTURAL BASIS | MOLECULAR RECOGNITION | PHARMACOLOGY & PHARMACY | CLASS-B GPCR | COUPLED-RECEPTOR | BINDING | Receptors, Adrenomedullin - chemistry | Humans | Adrenomedullin - chemistry | Cercopithecus aethiops | Receptor Activity-Modifying Protein 1 - chemistry | Receptor Activity-Modifying Protein 2 - chemistry | Receptor Activity-Modifying Protein 3 - genetics | Calcitonin Gene-Related Peptide - chemistry | Receptors, Calcitonin Gene-Related Peptide - metabolism | Recombinant Fusion Proteins - metabolism | Peptide Hormones - metabolism | Receptors, Calcitonin Gene-Related Peptide - chemistry | Peptide Hormones - chemistry | Protein Interaction Domains and Motifs | Calcitonin Gene-Related Peptide - metabolism | Cyclic AMP - metabolism | Peptide Fragments - genetics | Second Messenger Systems | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Receptors, Adrenomedullin - metabolism | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Rats | Receptor Activity-Modifying Protein 1 - metabolism | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Receptor Activity-Modifying Protein 2 - metabolism | Adrenomedullin - metabolism | Receptor Activity-Modifying Protein 1 - genetics | Recombinant Fusion Proteins - chemistry | Calcitonin Receptor-Like Protein - metabolism | Peptide Fragments - chemistry | Animals | Receptor Activity-Modifying Protein 3 - chemistry | Calcitonin Receptor-Like Protein - genetics | Mutant Proteins - chemistry | Receptor Activity-Modifying Protein 3 - metabolism | Receptor Activity-Modifying Protein 2 - genetics | COS Cells | Proteins | Genetic research | Pharmacology | Genetic aspects | Algorithms | Analysis | Peptides | Mutation | Research Papers
Journal Article
Molecular Cell, ISSN 1097-2765, 06/2015, Volume 58, Issue 6, pp. 1040 - 1052
Association of receptor activity-modifying proteins (RAMP1-3) with the G protein-coupled receptor (GPCR) calcitonin receptor-like receptor (CLR) enables... 
CALCITONIN-RECEPTOR | AMYLIN RECEPTORS | GENE-RELATED PEPTIDE | CRYSTAL-STRUCTURE | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXTRACELLULAR DOMAIN | PARATHYROID-HORMONE | N-TERMINUS | CGRP RECEPTOR | ADRENOMEDULLIN | CELL BIOLOGY | Humans | Protein Multimerization | Adrenomedullin - chemistry | Peptides - genetics | Cercopithecus aethiops | Molecular Sequence Data | Crystallography, X-Ray | Receptor Activity-Modifying Protein 1 - chemistry | Receptor Activity-Modifying Protein 2 - chemistry | Calcitonin Gene-Related Peptide - chemistry | Peptides - metabolism | Calcitonin Gene-Related Peptide - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Peptides - chemistry | Protein Structure, Secondary | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Receptor Activity-Modifying Protein 1 - metabolism | Calcitonin Gene-Related Peptide - genetics | Receptor Activity-Modifying Protein 2 - metabolism | Adrenomedullin - metabolism | Binding Sites - genetics | Receptor Activity-Modifying Protein 1 - genetics | Calcitonin Receptor-Like Protein - metabolism | Adrenomedullin - genetics | Sequence Homology, Amino Acid | Animals | Calcitonin Receptor-Like Protein - genetics | Protein Binding | Receptor Activity-Modifying Protein 2 - genetics | Mutation | COS Cells | G proteins | Peptides | Structure | Crystals | Membrane proteins | Protein binding | BASIC BIOLOGICAL SCIENCES
Journal Article
Biochemistry, ISSN 0006-2960, 12/2009, Volume 48, Issue 49, pp. 11773 - 11785
The three receptor activity-modifying proteins (RAMPs) have been recognized as being important for the trafficking and function of a subset of family B G... 
HELIX-HELIX INTERACTIONS | CALCITONIN-RECEPTOR | AMYLIN RECEPTORS | GENE-RELATED PEPTIDE | RAMPS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRAFFICKING | OLIGOMERIZATION | AGONIST-BINDING | DIFFERENTIALLY MODULATE | ADRENOMEDULLIN | Receptors, Gastrointestinal Hormone - chemistry | Multigene Family - physiology | Cricetulus | Receptors, G-Protein-Coupled - metabolism | Receptors, Calcitonin - metabolism | Humans | Cercopithecus aethiops | Intracellular Signaling Peptides and Proteins - metabolism | Calcitonin Receptor-Like Protein | Receptors, Gastrointestinal Hormone - metabolism | Genetic Complementation Test | Secretin - genetics | Fluorescence Resonance Energy Transfer | Luminescent Proteins - chemistry | Receptor Activity-Modifying Protein 3 | Membrane Proteins - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Receptor Activity-Modifying Protein 1 | CHO Cells | Receptor Activity-Modifying Protein 2 | Receptors, Gastrointestinal Hormone - biosynthesis | Cricetinae | Membrane Proteins - genetics | Receptors, Adrenomedullin | Receptors, G-Protein-Coupled - biosynthesis | Receptors, Peptide - antagonists & inhibitors | Protein Transport - genetics | Membrane Proteins - biosynthesis | Animals | Membrane Proteins - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Receptors, Gastrointestinal Hormone - genetics | Luminescent Proteins - genetics | Receptor Activity-Modifying Proteins | Receptors, G-Protein-Coupled - genetics | COS Cells | Receptors, G-Protein-Coupled - chemistry | Luminescent Proteins - metabolism | Receptors, Peptide - metabolism | Secretin - metabolism | Fluorescence | Biomolecules | Chemical properties | Structure | Optical properties | Analysis
Journal Article
BBA - Molecular Cell Research, ISSN 0167-4889, 10/2011, Volume 1813, Issue 10, pp. 1906 - 1916
The first and third extracellular loops (ECL) of G protein-coupled receptors (GPCRs) have been implicated in ligand binding and receptor function. This study... 
G protein-coupled receptor | Extracellular loop | Receptor activation | Juxtamembrane domain | Receptor activity-modifying protein | CGRP | AMINO-TERMINUS | ACTIVATION | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN-COUPLED RECEPTORS | AGONIST BINDING | PEPTIDE | FAMILY | CELL BIOLOGY | SECRETIN RECEPTOR | B GPCRS | HORMONE-RECEPTOR | Calcitonin Receptor-Like Protein - physiology | Protein Interaction Domains and Motifs - physiology | Humans | Cercopithecus aethiops | Molecular Sequence Data | Receptor Activity-Modifying Protein 1 - chemistry | Calcitonin Gene-Related Peptide - chemistry | Calcitonin Gene-Related Peptide - physiology | Cattle | Protein Interaction Domains and Motifs - genetics | Protein Structure, Secondary - physiology | Cell Membrane - metabolism | Calcitonin Gene-Related Peptide - metabolism | Cyclic AMP - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Receptor Activity-Modifying Protein 1 - metabolism | Calcitonin Gene-Related Peptide - genetics | Mutant Proteins - metabolism | Mutant Proteins - physiology | Calcitonin Receptor-Like Protein - metabolism | Protein Structure, Secondary - genetics | Animals | Models, Biological | Calcitonin Receptor-Like Protein - genetics | Mutant Proteins - chemistry | Protein Binding | COS Cells | Amino Acid Substitution | Lectins | Vasoactive intestinal peptides | Parathyroid hormone | Membrane proteins
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 01/2008, Volume 118, Issue 1, pp. 29 - 39
Adrenomedullin (AM) is a peptide involved both in the pathogenesis of cardiovascular diseases and in circulatory homeostasis. The high-affinity AM receptor is... 
MEDICINE, RESEARCH & EXPERIMENTAL | ACTIVITY-MODIFYING PROTEINS | ENDOGENOUS ADRENOMEDULLIN | CARDIAC-HYPERTROPHY | ENDOTHELIAL-CELLS | GENE-EXPRESSION | SMOOTH-MUSCLE-CELLS | ANGIOTENSIN-II | KNOCKOUT MICE | INDUCED AIRWAY HYPERRESPONSIVENESS | TRANSGENIC MICE | Capillary Permeability - physiology | Embryonic Stem Cells - metabolism | Edema - genetics | Receptors, Calcitonin - metabolism | Tight Junctions - genetics | Humans | Male | Receptors, Calcitonin - genetics | Calcitonin Receptor-Like Protein | Cardiovascular Diseases - pathology | Cardiovascular Diseases - genetics | Receptors, Peptide - genetics | Arteries - metabolism | Embryo Loss - metabolism | Embryo Loss - pathology | Female | Embryo Loss - genetics | Intracellular Signaling Peptides and Proteins - genetics | Receptor Activity-Modifying Protein 2 | Tight Junctions - metabolism | Cardiovascular Diseases - metabolism | Membrane Proteins - genetics | Cells, Cultured | Receptors, Adrenomedullin | Adrenomedullin - metabolism | Arteries - pathology | Adrenomedullin - genetics | Mice, Knockout | Pregnancy | Edema - metabolism | Neovascularization, Physiologic - physiology | Membrane Proteins - biosynthesis | Animals | Endothelium, Vascular - metabolism | Homeostasis - physiology | Embryonic Stem Cells - pathology | Endothelium, Vascular - pathology | Receptor Activity-Modifying Proteins | Mice | Edema - pathology | Tight Junctions - pathology | Receptors, Peptide - metabolism | Proteins | Physiological aspects | Research | Peptides | Cardiovascular diseases
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 03/2007, Volume 27, Issue 10, pp. 2693 - 2703
The neuropeptide calcitonin gene- related peptide ( CGRP) from the trigeminal ganglion has been established as a key player in the pathogenesis of migraine. In... 
Gene transfer | Transcription | Calcitonin | Migraine | Transgenic | GPCR | Neurogenic inflammation | cAMP | CGRP | Trigeminal | Cre-transgenic | NERVOUS-SYSTEM | AMYLIN RECEPTORS | migraine | calcitonin | gene transfer | transcription | ADRENOMEDULLIN RECEPTORS | ANTIMIGRAINE DRUG | NEUROSCIENCES | neurogenic inflammation | ANTAGONIST BIBN4096BS | MESSENGER-RNA | transgenic | SMOOTH-MUSCLE-CELLS | CEREBRAL-ARTERIES | trigeminal | BINDING-SITES | Inflammation - chemically induced | Intracellular Signaling Peptides and Proteins - pharmacology | Inflammation - pathology | Gene Expression - drug effects | Receptors, Calcitonin - metabolism | Humans | Intracellular Signaling Peptides and Proteins - drug effects | Nervous System - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Membrane Proteins - pharmacology | Calcitonin Receptor-Like Protein | Trigeminal Ganglion - drug effects | Receptors, Calcitonin Gene-Related Peptide - metabolism | Membrane Proteins - physiology | Membrane Proteins - metabolism | Neurons - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Receptor Activity-Modifying Protein 1 | Subcutaneous Tissue - pathology | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Transfer Techniques | Trigeminal Ganglion - cytology | Receptors, Calcitonin - drug effects | Calcitonin Gene-Related Peptide - pharmacology | Membrane Proteins - genetics | Rats | Trigeminal Ganglion - metabolism | Mice, Transgenic | Rats, Sprague-Dawley | Animals | Promoter Regions, Genetic - physiology | Membrane Proteins - drug effects | Receptor Activity-Modifying Proteins | Receptors, Calcitonin Gene-Related Peptide - genetics | Mice | In Vitro Techniques | Intracellular Signaling Peptides and Proteins - physiology | Subcutaneous Tissue - drug effects
Journal Article
BIOCHEMICAL JOURNAL, ISSN 0264-6021, 06/2017, Volume 474, Issue 12, pp. 1981 - 1992
Journal Article
Biochemistry, ISSN 0006-2960, 08/2017, Volume 56, Issue 30, pp. 3877 - 3880
The second extracellular loop (ECL2) of the G protein-coupled receptor (GPCR) family is important for ligand interaction and drug discovery. ECL2 of the family... 
COMPLEX | ACTIVATION | GENE-RELATED PEPTIDE | PROTEIN-COUPLED RECEPTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | Protein Multimerization | Cercopithecus aethiops | Peptide Fragments - pharmacology | Receptor Activity-Modifying Protein 1 - chemistry | Calcitonin Gene-Related Peptide - chemistry | Receptors, Calcitonin Gene-Related Peptide - metabolism | Calcitonin Receptor-Like Protein - agonists | Miotics - pharmacology | Receptors, Calcitonin Gene-Related Peptide - chemistry | Miotics - metabolism | Receptors, Calcitonin Gene-Related Peptide - agonists | Protein Interaction Domains and Motifs | Calcitonin Gene-Related Peptide - metabolism | Binding Sites | Peptide Fragments - genetics | Binding, Competitive | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Calcitonin Gene-Related Peptide - pharmacology | Miotics - chemistry | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Receptor Activity-Modifying Protein 1 - metabolism | Recombinant Proteins - chemistry | Calcitonin Gene-Related Peptide - genetics | Receptor Activity-Modifying Protein 1 - genetics | Recombinant Proteins - pharmacology | Calcitonin Receptor-Like Protein - metabolism | Protein Interaction Mapping | Point Mutation | Peptide Fragments - chemistry | Animals | Signal Transduction - drug effects | Calcitonin Receptor-Like Protein - genetics | Ligands | Protein Conformation | Receptors, Calcitonin Gene-Related Peptide - genetics | Structural Homology, Protein | Kinetics | COS Cells | Amino Acid Substitution | Usage | Research | Antibiosis | Antimetabolites | Calcitonin
Journal Article
Journal Article
Journal of Peptide Science, ISSN 1075-2617, 12/2015, Volume 21, Issue 12, pp. 905 - 912
The human adrenomedullin (ADM) is a 52 amino acid peptide hormone belonging to the calcitonin family of peptides, which plays a major role in the development... 
G protein‐coupled receptor (GPCR) trafficking | solid‐phase peptide synthesis (SPPS) | copper(I)‐catalyzed azide alkyne cycloaddition (CuAAC) | live cell fluorescence microscopy | adrenomedullin (ADM) | fluorescently labeled peptide | ADM receptor | receptor activity‐modifying protein 2 (RAMP2) | G protein-coupled receptor (GPCR) trafficking | copper(I)-catalyzed azide alkyne cycloaddition (CuAAC) | receptor activity-modifying protein 2 (RAMP2) | solid-phase peptide synthesis (SPPS) | CHEMISTRY, ANALYTICAL | DESENSITIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CALCITONIN | PEPTIDE | INTERNALIZATION | TRANSPORT | PROTEIN-COUPLED RECEPTOR | Fluorescent Dyes - chemistry | Peptides - chemistry | Receptors, Adrenomedullin - genetics | Receptors, Adrenomedullin - metabolism | Humans | Adrenomedullin - chemistry | Calcitonin Receptor-Like Protein - chemistry | Receptor Activity-Modifying Protein 2 - chemistry | Receptor Activity-Modifying Protein 2 - metabolism | Adrenomedullin - metabolism | Recombinant Fusion Proteins - chemistry | Calcitonin Receptor-Like Protein - metabolism | Recombinant Fusion Proteins - metabolism | Protein Transport | Lysosomes - ultrastructure | Peptides - chemical synthesis | Peptides - metabolism | Calcitonin Receptor-Like Protein - genetics | HEK293 Cells | Receptor Activity-Modifying Protein 2 - genetics | Recombinant Fusion Proteins - genetics | Rhodamines - chemistry | Fluorescence | Chorionic gonadotropin | G proteins | Peptides | Fluorescence microscopy | Membrane proteins
Journal Article
Journal Article