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Journal of Biological Chemistry, ISSN 0021-9258, 06/2017, Volume 292, Issue 24, pp. 9865 - 9881
The glucagon receptor (GCGR) belongs to the secretin-like (class B) family of G protein-coupled receptors (GPCRs) and is activated by the peptide hormone... 
BETA ADRENERGIC-RECEPTOR | LIGAND-BINDING | GLUCAGON RECEPTOR | IONIC LOCK | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING STRATEGY | METAPHYSEAL CHONDRODYSPLASIA | BETA-ADRENERGIC RECEPTOR | PEPTIDE | MUSCARINIC ACETYLCHOLINE-RECEPTOR | Receptor, Parathyroid Hormone, Type 1 - chemistry | Receptors, Corticotropin-Releasing Hormone - metabolism | Receptor, Parathyroid Hormone, Type 1 - metabolism | Humans | Receptors, Corticotropin-Releasing Hormone - agonists | Receptors, Corticotropin-Releasing Hormone - genetics | Receptor, Parathyroid Hormone, Type 1 - agonists | Recombinant Fusion Proteins - metabolism | Receptors, Vasoactive Intestinal Polypeptide, Type I - agonists | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - chemistry | Conserved Sequence | Protein Interaction Domains and Motifs | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - agonists | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - metabolism | Receptors, Vasoactive Intestinal Polypeptide, Type I - metabolism | Protein Stability | Binding Sites | Peptide Fragments - genetics | Second Messenger Systems | Receptors, Glucagon - agonists | Receptors, Glucagon - genetics | Receptors, Vasoactive Intestinal Polypeptide, Type I - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Cell Line | Peptide Fragments - metabolism | Mutagenesis, Site-Directed | Models, Molecular | Receptors, Glucagon - metabolism | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Receptors, Vasoactive Intestinal Polypeptide, Type I - genetics | Peptide Fragments - chemistry | Peptide Fragments - agonists | Receptors, Glucagon - chemistry | Hydrophobic and Hydrophilic Interactions | Receptor, Parathyroid Hormone, Type 1 - genetics | Ligands | Protein Conformation | Structural Homology, Protein | Mutation | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - genetics | Receptors, Corticotropin-Releasing Hormone - chemistry | Amino Acid Substitution | Index Medicus | Editors' Picks | 7-helix receptor | G protein-coupled receptor (GPCR) | parathyroid hormone | glucagon | arrestin
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
Nature Cell Biology, ISSN 1465-7392, 03/2010, Volume 12, Issue 3, pp. 224 - 234
Parathyroid hormone (PTH) regulates calcium homeostasis and bone metabolism by activating PTH type I receptor (PTH1R). Here we show that transforming growth... 
(PTH)/PTH-RELATED PEPTIDE | LINKED RECEPTOR | TRABECULAR BONE | GROWTH-FACTOR-BETA | PARATHYROID-HORMONE RECEPTOR | PROTEIN-COUPLED RECEPTOR | CRYSTAL-STRUCTURE | TRANSFORMING GROWTH-FACTOR-BETA-1 | RENAL-FAILURE | EXPRESSION CLONING | CELL BIOLOGY | RNA, Small Interfering - genetics | Receptors, Transforming Growth Factor beta - genetics | RANK Ligand - metabolism | Leg Bones - pathology | Receptor, Parathyroid Hormone, Type 1 - metabolism | Gene Expression - genetics | Cell Count | Humans | Leg Bones - drug effects | Male | Bone Density - genetics | Bone Remodeling - physiology | Mutation - physiology | Osteocalcin - blood | Parathyroid Hormone - metabolism | Protein Binding - drug effects | Protein Multimerization - physiology | Phosphorylation - drug effects | Cyclic AMP - metabolism | Protein-Serine-Threonine Kinases - metabolism | Osteoclasts - pathology | Endocytosis - drug effects | Mice, Knockout | Signal Transduction - drug effects | beta-Arrestins | Receptor, Parathyroid Hormone, Type 1 - genetics | Mice | Protein Multimerization - drug effects | Protein Binding - physiology | Collagen Type I - blood | Phosphorylation - physiology | Peptides - blood | Protein Interaction Domains and Motifs - physiology | Arrestins - genetics | Parathyroid Hormone - pharmacology | Peptide Fragments - pharmacology | Arrestins - metabolism | Bone Remodeling - drug effects | Endocytosis - genetics | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Parathyroid Hormone - antagonists & inhibitors | Osteoblasts - pathology | Animals | Receptors, Transforming Growth Factor beta - metabolism | Cyclic AMP Response Element-Binding Protein - metabolism | Signal Transduction - physiology | Osteoblasts - metabolism | Smad Proteins - metabolism | Index Medicus
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 | Index Medicus | BASIC BIOLOGICAL SCIENCES
Journal Article
Journal Article
Nephrology Dialysis Transplantation, ISSN 0931-0509, 02/2014, Volume 29, Issue 2, pp. 282 - 289
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2016, Volume 291, Issue 29, pp. 15119 - 15130
Journal Article