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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
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
Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, 05/2019, Volume 37, Issue 8, pp. 1968 - 1991
Toll-like receptor 4 (TLR4) is a member of Toll-Like Receptors (TLRs) family that serves as a receptor for bacterial lipopolysaccharide (LPS). TLR4 alone... 
ADR: Adverse drug reaction | fs: femto seconds | ps: pico seconds | TLR4: Toll-like receptor 4 | protein-protein interactions (PPIs) | DTs: Drug transporters | TIR: Toll/IL-1 receptor like | RMSF: Root mean square fluctuation | API: Active pharmaceutical ingredient | NF-κB: Nuclear factor Kappa B | ECD: Extra cellular domain | CHARMM: Chemistry at HARvard macromolecular mechanics | RMSD: Root mean square deviation | PAMPs: Pathogen associated molecular patterns | Ro4: Rule of four | Toll-Like Receptor 4 (TLR4) | ns: nano seconds | PPIs: Protein-protein interactions | VMD: Visual molecular dynamics | MD: Molecular dynamics | ADMET: Absorption, distribution, metabolism, excretion and toxicity | NAMD: NAnoscale molecular dynamics | lipopolysaccharide (LPS) | hTLR4−MD-2 complex inhibitors | TLRs: Toll-like receptors | LRRs: Leucine rich repeats | LMWIs: Low molecular weight inhibitors | VS: Virtual screening | PRRs: Pattern recognition receptors | SMPPIIs: Small molecule protein-protein interaction inhibitors | TMD: Transmembrane domain | small molecule protein-protein interaction inhibitors (SMPPIIs) | LPS: LipoPolySaccharide | DMEs: Drug-metabolizing enzymes | DAMPs: Danger/damage associated molecular patterns | MDS: Molecular dynamics simulation | MD-2: Myeloid differentiation factor-2 | LE: Ligand efficiency | protein–protein interactions (PPIs) | small molecule protein–protein interaction inhibitors (SMPPIIs) | hTLR4-MD-2 complex inhibitors | TLR4 ANTAGONIST | BIOCHEMISTRY & MOLECULAR BIOLOGY | IL-1 receptor like | PREDICTION | HOT-SPOTS | metabolism | GENERAL FORCE-FIELD | DAMPs: Danger | FREE TOOL | DESIGN | damage associated molecular patterns | NF-B: Nuclear factor Kappa B | distribution | DRUG-METABOLIZING-ENZYMES | DISCOVERY | SMALL-MOLECULE INHIBITORS | excretion and toxicity | TIR: Toll | BIOPHYSICS | ADMET: Absorption | WEB SERVER
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
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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2013, Volume 110, Issue 37, pp. 14918 - 14923
Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and... 
Receptors | Experimental data | Cytokines | Lymphocytes | Architectural models | Ligands | Mast cells | Binding sites | Endothelial cells | Crystal structure | X-ray crystallography | Protein-protein interaction | Cytokine signaling | SAXS | BINDING MODE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | X-RAY-SCATTERING | INTERLEUKIN-33 | INNATE LYMPHOID-CELLS | FAMILY | IL-1-LIKE CYTOKINE IL-33 | ACCESSORY PROTEIN | BIOLOGICAL-ACTIVITY | cytokine signaling | TYPE-2 IMMUNITY | protein-protein interaction | Interleukin-1 Receptor Accessory Protein - genetics | Interleukin-1 Receptor-Like 1 Protein | Surface Plasmon Resonance | Interleukin-1 Receptor Accessory Protein - chemistry | Humans | Molecular Sequence Data | Crystallography, X-Ray | Interleukins - metabolism | Interleukin-1 Receptor Accessory Protein - metabolism | Interleukins - genetics | X-Ray Diffraction | Receptors, Cell Surface - chemistry | Protein Interaction Domains and Motifs | Interleukins - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Interleukin-33 | Models, Molecular | Receptors, Cell Surface - metabolism | Recombinant Proteins - chemistry | Scattering, Small Angle | Recombinant Proteins - genetics | Static Electricity | Protein Conformation | Receptors, Cell Surface - genetics | Index Medicus | protein–protein interaction | Biological Sciences
Journal Article
Journal Article