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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
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
PLoS ONE, ISSN 1932-6203, 09/2014, Volume 9, Issue 9, pp. e106890 - e106890
Background and Objectives: Glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP) are important regulators of insulin... 
CELLS | BETA-ARRESTIN2 | ACTIVATION | PHYSIOLOGY | GLUCAGON-LIKE PEPTIDE-1 | MULTIDISCIPLINARY SCIENCES | PROTEIN-COUPLED RECEPTORS | CONSTITUTIVE ACTIVITY | BETA-ARRESTIN | IDENTIFICATION | POLYPEPTIDE | Cricetinae | Gastric Inhibitory Polypeptide - metabolism | Cricetulus | Glucagon-Like Peptide 1 - metabolism | Diabetes Mellitus, Type 2 - genetics | Humans | Glucagon-Like Peptide 1 - pharmacology | Diabetes Mellitus, Type 2 - metabolism | G-Protein-Coupled Receptor Kinase 2 - metabolism | Receptors, Gastrointestinal Hormone - metabolism | Arrestins - metabolism | Receptors, Gastrointestinal Hormone - agonists | Glucagon-Like Peptide-1 Receptor - genetics | Glucagon-Like Peptide-1 Receptor - metabolism | Animals | Receptors, Gastrointestinal Hormone - genetics | HEK293 Cells | Protein Binding | Gastric Inhibitory Polypeptide - pharmacology | Glucagon-Like Peptide-1 Receptor - agonists | CHO Cells | Type 2 diabetes | Pancreatic beta cells | Peptides | Luciferase | Fluorescence | Glucose | G proteins | Comparative analysis | Dextrose | Regulators | G protein-coupled receptors | Glucagon | Disease | b-Adrenergic-receptor kinase | Confocal microscopy | Secretin | Arrestin | Confocal | Kinases | Recruitment | Proteins | Adenylate cyclase | Receptors | Toxicology | Reporter gene | Rodents | Complementation | Fluorescence resonance energy transfer | Pancreas | Glucagon-like peptide 1 | Translocation | Obesity | Polypeptides | Secretion | Diabetes mellitus | Cyclic AMP | GIP protein | Pharmacology | Insulin | Medicine | Signaling | Microscopy | Pharmacy | Ligands | Diabetes | Receptor mechanisms | Energy transfer | Index Medicus
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2016, Volume 11, Issue 9, p. e0163086
The involvement of secretin (SCT) and secretin receptor (SCTR) in regulating body water homeostasis is well established. Identified as one of the vasopressin... 
COUPLED RECEPTOR DIMERIZATION | RAT-KIDNEY | BETA-ARRESTINS | MULTIDISCIPLINARY SCIENCES | SECRETIN RECEPTOR | BODY-WATER HOMEOSTASIS | FUNCTIONAL-CHARACTERIZATION | V2 VASOPRESSIN RECEPTORS | AQUAPORIN-2 | MUTATIONS | INAPPROPRIATE ANTIDIURESIS | Receptors, Gastrointestinal Hormone - chemistry | Cricetulus | Receptors, G-Protein-Coupled - metabolism | Humans | Protein Multimerization | Receptors, Vasopressin - metabolism | Receptors, Gastrointestinal Hormone - metabolism | Receptors, Vasopressin - chemistry | Diabetes Insipidus, Nephrogenic - genetics | Genetic Diseases, X-Linked - genetics | CHO Cells | Cricetinae | Gene Expression | Signal Transduction - genetics | Genetic Diseases, X-Linked - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Microscopy, Confocal | Animals | Receptors, Gastrointestinal Hormone - genetics | Receptors, Vasopressin - genetics | Protein Binding | Mice | Receptors, G-Protein-Coupled - genetics | Mutation | Receptors, G-Protein-Coupled - chemistry | Diabetes Insipidus, Nephrogenic - metabolism | Diabetes insipidus | Aquaporins | Cyclic adenylic acid | Urine | Body water | G protein-coupled receptors | Kidneys | Nondestructive testing | Trafficking | Diabetes mellitus | Homeostasis | Inspection | Reabsorption | Secretin | Pharmacology | Cell surface | Vasopressin | Proteins | Signaling | Ligands | Diabetes | Collecting duct | Aquaporin 2
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, p. e0179568
Family B G protein-coupled receptors (GPCRs) play vital roles in hormone-regulated homeostasis. They are drug targets for metabolic diseases, including type 2... 
PHOSPHOLIPID-BILAYER NANODISCS | IN-VITRO | ACTIVATION | HIGH-LEVEL EXPRESSION | LIGAND-BINDING | SECRETIN FAMILY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | RHODOPSIN | PARATHYROID-HORMONE | GLP-1 RECEPTOR | Humans | Lipoproteins, HDL - metabolism | Receptors, G-Protein-Coupled - agonists | Glucagon-Like Peptide-1 Receptor - genetics | Glucagon-Like Peptide-1 Receptor - isolation & purification | Peptides - metabolism | HEK293 Cells | Receptors, G-Protein-Coupled - isolation & purification | Lipoproteins, HDL - chemistry | Hypoglycemic Agents - therapeutic use | Microscopy, Electron, Transmission | Nanostructures - ultrastructure | Reproducibility of Results | Glucagon-Like Peptide 1 - metabolism | Nanotechnology - methods | Venoms - therapeutic use | Nanostructures - chemistry | Protein Binding | Receptors, G-Protein-Coupled - genetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Diabetes Mellitus, Type 2 - drug therapy | Venoms - metabolism | Glucagon-Like Peptide-1 Receptor - agonists | Peptides - therapeutic use | Proteins | Research | G proteins | Glucagon | Denaturation | Analysis | G protein-coupled receptors | Peptides | Stabilization | Protein purification | Homeostasis | Spectroscopic analysis | Amino acids | Lipids | Biochemistry | Solubilization | Kinases | Guanine nucleotide-binding protein | Density | Lipid bilayers | Coupling (molecular) | Osteoporosis | Signal transduction | Receptors | Biomedical materials | Functional anatomy | Rodents | Biocompatibility | Labeling | Glucagon-like peptide 1 | Activation analysis | Purification | Diabetes mellitus | Particulates | Nanostructure | Biophysics | Metabolism | Apolipoproteins | Chromatography | Diseases | Studies | Chemistry | Mutagenesis | Ligands | Environment | Diabetes | Methods | Metabolic disorders | Metabolic diseases
Journal Article
Journal Article
Journal Article
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7657, pp. 312 - 315
The glucagon-like peptide-1 receptor (GLP-1R) and the glucagon receptor (GCGR) are members of the secretin-like class B family of G-protein-coupled receptors... 
Medicine(all) | General | PROTEIN | ANTAGONIST | GLUCAGON-LIKE PEPTIDE-1 | DETERMINANTS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | VALIDATION | FORCE-FIELD | LIGAND | BINDING | AGONIST | Allosteric Regulation - drug effects | Amino Acid Sequence | Allosteric Site - drug effects | Humans | Benzamides - metabolism | Glucagon-Like Peptide-1 Receptor - chemistry | Models, Molecular | Crystallography, X-Ray | Aminopyridines - metabolism | Aminopyridines - chemistry | Glucagon-Like Peptide-1 Receptor - metabolism | Phenylurea Compounds - chemistry | Aminopyridines - pharmacology | Protein Domains | Benzamides - pharmacology | Phenylurea Compounds - metabolism | Phenylurea Compounds - pharmacology | Glucagon-Like Peptide-1 Receptor - agonists | Benzamides - chemistry | Type 2 diabetes | Physiological aspects | Glucagon | Health aspects | Protein-protein interactions | Membrane proteins | G protein-coupled receptors | Molecular structure | Peptides | Secretin | Activation | Helices | Glucose | Guanine nucleotide-binding protein | Modulators | Coupling (molecular) | Receptors | Allosteric properties | Modulation | Modelling | Physiology | Glucagon-like peptide 1 | Activation analysis | Crystal structure | Movement | Secretion | Diabetes mellitus | Insulin | Molecular modelling | Mutagenesis | Diabetes | Intracellular | Binding sites | Index Medicus
Journal Article