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Publication DateJournal of Biological Chemistry, ISSN 0021-9258, 04/2008, Volume 283, Issue 17, pp. 11340 - 11347
The glucagon-like peptide-1 receptor (GLP-1R) belongs to Family B1 of the seven-transmembrane G protein-coupled receptors, and its natural agonist ligand is...
AMINO-TERMINUS | PROTEIN-COUPLED RECEPTOR | EXENDIN-4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | MID-REGION | N-TERMINAL DOMAIN | GLP-1 RECEPTOR | BINDING | SECRETIN | SPATIAL APPROXIMATION | AGONIST | Amino Acid Sequence | Magnetic Resonance Spectroscopy | Peptides - chemistry | Protein Structure, Secondary | Humans | Molecular Sequence Data | Tryptophan - chemistry | Crystallography, X-Ray - methods | Sequence Homology, Amino Acid | Insulin-Secreting Cells - metabolism | Glucagon-Like Peptide-1 Receptor | Receptors, Glucagon - chemistry | Protein Binding | Ligands | Protein Conformation | Cell Membrane - metabolism | Venoms - chemistry | Receptors, Glucagon - physiology | Index Medicus
AMINO-TERMINUS | PROTEIN-COUPLED RECEPTOR | EXENDIN-4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | MID-REGION | N-TERMINAL DOMAIN | GLP-1 RECEPTOR | BINDING | SECRETIN | SPATIAL APPROXIMATION | AGONIST | Amino Acid Sequence | Magnetic Resonance Spectroscopy | Peptides - chemistry | Protein Structure, Secondary | Humans | Molecular Sequence Data | Tryptophan - chemistry | Crystallography, X-Ray - methods | Sequence Homology, Amino Acid | Insulin-Secreting Cells - metabolism | Glucagon-Like Peptide-1 Receptor | Receptors, Glucagon - chemistry | Protein Binding | Ligands | Protein Conformation | Cell Membrane - metabolism | Venoms - chemistry | Receptors, Glucagon - physiology | Index Medicus
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Loading RightsJournal of Biological Chemistry, ISSN 0021-9258, 01/2010, Volume 285, Issue 1, pp. 723 - 730
GLP-1 ( g lucagon- l ike p eptide-1) is an incretin released from intestinal L-cells in response to food intake. Activation of the GLP-1 receptor potentiates...
LIGAND-BINDING | HORMONE | TERMINAL DOMAIN | EXENDIN-4 | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PIG PANCREAS | IN-VIVO | N-TERMINUS | GLP-1 RECEPTOR | PROTEIN-COUPLED-RECEPTOR | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Mutagenesis, Site-Directed | Glucagon-Like Peptide 1 - metabolism | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Receptors, Glucagon - metabolism | Crystallography, X-Ray | Glucagon-Like Peptide 1 - chemistry | Mutant Proteins - metabolism | Extracellular Space - metabolism | Glucagon-Like Peptide-1 Receptor | Solutions | Mutant Proteins - chemistry | Receptors, Glucagon - chemistry | Protein Binding | Index Medicus | Protein Structure and Folding
LIGAND-BINDING | HORMONE | TERMINAL DOMAIN | EXENDIN-4 | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PIG PANCREAS | IN-VIVO | N-TERMINUS | GLP-1 RECEPTOR | PROTEIN-COUPLED-RECEPTOR | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Mutagenesis, Site-Directed | Glucagon-Like Peptide 1 - metabolism | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Receptors, Glucagon - metabolism | Crystallography, X-Ray | Glucagon-Like Peptide 1 - chemistry | Mutant Proteins - metabolism | Extracellular Space - metabolism | Glucagon-Like Peptide-1 Receptor | Solutions | Mutant Proteins - chemistry | Receptors, Glucagon - chemistry | Protein Binding | Index Medicus | Protein Structure and Folding
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Loading RightsProceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2007, Volume 104, Issue 35, pp. 13942 - 13947
Incretins, endogenous polypeptide hormones released in response to food intake, potentiate insulin secretion from pancreatic β cells after oral glucose...
Molecules | Receptors | Hydrogen bonds | Disulfides | Ligands | Amino acids | Hormones | Peptide hormones | Glucagon receptors | Crystal structure | Glucose-dependent insulinotropic polypeptide | X-ray | Diabetes mellitus | Hormone binding | CHIMERIC RECEPTORS | AMINO-TERMINUS | LIGAND-BINDING | x-ray | TERMINAL DOMAIN | MULTIDISCIPLINARY SCIENCES | diabetes mellitus | glucose-dependent insulinotropic polypeptide | BIOACTIVE DOMAIN | GLUCAGON-LIKE PEPTIDE-1 | DISULFIDE PATTERN | PARATHYROID-HORMONE | DEPENDENT INSULINOTROPIC POLYPEPTIDE | GASTRIC-INHIBITORY POLYPEPTIDE | hormone binding | Amino Acid Sequence | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Sequence Homology, Amino Acid | Insulin - metabolism | Insulin-Secreting Cells - metabolism | Sequence Alignment | Conserved Sequence | Disulfides - analysis | Protein Binding | Peptide Hormones - chemistry | Protein Conformation | Binding Sites | Insulin Secretion | Receptors, G-Protein-Coupled - chemistry | Hormone receptors | Polypeptides | Glucagon | Physiological aspects | G proteins | Diabetes | Chemical properties | Biological Sciences
Molecules | Receptors | Hydrogen bonds | Disulfides | Ligands | Amino acids | Hormones | Peptide hormones | Glucagon receptors | Crystal structure | Glucose-dependent insulinotropic polypeptide | X-ray | Diabetes mellitus | Hormone binding | CHIMERIC RECEPTORS | AMINO-TERMINUS | LIGAND-BINDING | x-ray | TERMINAL DOMAIN | MULTIDISCIPLINARY SCIENCES | diabetes mellitus | glucose-dependent insulinotropic polypeptide | BIOACTIVE DOMAIN | GLUCAGON-LIKE PEPTIDE-1 | DISULFIDE PATTERN | PARATHYROID-HORMONE | DEPENDENT INSULINOTROPIC POLYPEPTIDE | GASTRIC-INHIBITORY POLYPEPTIDE | hormone binding | Amino Acid Sequence | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Sequence Homology, Amino Acid | Insulin - metabolism | Insulin-Secreting Cells - metabolism | Sequence Alignment | Conserved Sequence | Disulfides - analysis | Protein Binding | Peptide Hormones - chemistry | Protein Conformation | Binding Sites | Insulin Secretion | Receptors, G-Protein-Coupled - chemistry | Hormone receptors | Polypeptides | Glucagon | Physiological aspects | G proteins | Diabetes | Chemical properties | Biological Sciences
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Loading RightseLife, ISSN 2050-084X, 2013, Volume 2, p. e01340
The Hedgehog (Hh) signal is transduced across the membrane by the heptahelical protein Smoothened (Smo), a developmental regulator, oncoprotein and drug target...
oxysterol | Hedgehog signaling | Zebrafish | cysteine rich domain | smoothened | MAXIMUM-LIKELIHOOD | STEM-CELLS | PROTEIN | SONIC HEDGEHOG | CYSTEINE-RICH DOMAINS | CRYSTAL-STRUCTURE | PATHWAY ACTIVITY | BIOLOGY | N-TERMINAL DOMAIN | MAMMALIAN-CELLS | PRIMARY CILIUM | Hedgehog Proteins - chemistry | Receptors, G-Protein-Coupled - metabolism | Hedgehog Proteins - metabolism | Crystallography, X-Ray | Structure-Activity Relationship | Hedgehog Proteins - genetics | Gene Expression Regulation, Developmental | Smoothened Receptor | Escherichia coli - metabolism | Binding Sites | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Protein Structure, Secondary | Signal Transduction | Zebrafish Proteins - chemistry | Sterols - chemistry | Zebrafish Proteins - metabolism | Zebrafish Proteins - antagonists & inhibitors | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Zebrafish - growth & development | Zebrafish - genetics | Animals | Escherichia coli - genetics | Zebrafish - metabolism | Embryo, Nonmammalian | Receptors, G-Protein-Coupled - antagonists & inhibitors | Protein Binding | Ligands | Mice | Receptors, G-Protein-Coupled - genetics | Zebrafish Proteins - genetics | Receptors, G-Protein-Coupled - chemistry | Wnt protein | Frizzled protein | Genes | Lipids | Biology | Hydrophobicity | Chromatography | Membrane proteins | Medicine | Proteins | Hedgehog protein | Binding sites | Crystal structure | Structure-function relationships
oxysterol | Hedgehog signaling | Zebrafish | cysteine rich domain | smoothened | MAXIMUM-LIKELIHOOD | STEM-CELLS | PROTEIN | SONIC HEDGEHOG | CYSTEINE-RICH DOMAINS | CRYSTAL-STRUCTURE | PATHWAY ACTIVITY | BIOLOGY | N-TERMINAL DOMAIN | MAMMALIAN-CELLS | PRIMARY CILIUM | Hedgehog Proteins - chemistry | Receptors, G-Protein-Coupled - metabolism | Hedgehog Proteins - metabolism | Crystallography, X-Ray | Structure-Activity Relationship | Hedgehog Proteins - genetics | Gene Expression Regulation, Developmental | Smoothened Receptor | Escherichia coli - metabolism | Binding Sites | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Protein Structure, Secondary | Signal Transduction | Zebrafish Proteins - chemistry | Sterols - chemistry | Zebrafish Proteins - metabolism | Zebrafish Proteins - antagonists & inhibitors | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Zebrafish - growth & development | Zebrafish - genetics | Animals | Escherichia coli - genetics | Zebrafish - metabolism | Embryo, Nonmammalian | Receptors, G-Protein-Coupled - antagonists & inhibitors | Protein Binding | Ligands | Mice | Receptors, G-Protein-Coupled - genetics | Zebrafish Proteins - genetics | Receptors, G-Protein-Coupled - chemistry | Wnt protein | Frizzled protein | Genes | Lipids | Biology | Hydrophobicity | Chromatography | Membrane proteins | Medicine | Proteins | Hedgehog protein | Binding sites | Crystal structure | Structure-function relationships
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Loading RightsFEBS Letters, ISSN 0014-5793, 01/2011, Volume 585, Issue 2, pp. 357 - 363
The eukaryotic-type serine/threonine kinase StkP from is an important signal-transduction element that regulates the expression of numerous pneumococcal genes....
Signal transduction | Penicillin-binding protein and Ser/Thr protein kinase-associated domain | Peptidoglycan | β-Lactam antibiotics | Protein structure | Streptococcus pneumoniae | N-acetylglucosamine | eukaryotic-type Ser/Thr protein kinase | C-StkP | C-terminal domain of StkP kinase | circular dichroism | peptidoglycan | 6-aminopenicillanic acid | PASTA domain | 6-APA | NAG | PGN | STPK | penicillin-binding protein and Ser/Thr protein kinase-associated domain | BACTERIA | PASTA DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta-Lactam antibiotics | PKNB | IDENTIFICATION | CELL BIOLOGY | CIRCULAR-DICHROISM | ENZYME | BIOPHYSICS | EXPRESSION | Peptidoglycan - metabolism | beta-Lactams - metabolism | Peptidoglycan - chemistry | Models, Molecular | Cell Wall - chemistry | beta-Lactams - chemistry | Bacterial Proteins | Anti-Bacterial Agents | Protein Binding | Protein Interaction Domains and Motifs | Protein-Serine-Threonine Kinases - chemistry | Spectrum Analysis | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Streptococcus pneumoniae - enzymology | β-lactam antibiotics | PASTA domains
Signal transduction | Penicillin-binding protein and Ser/Thr protein kinase-associated domain | Peptidoglycan | β-Lactam antibiotics | Protein structure | Streptococcus pneumoniae | N-acetylglucosamine | eukaryotic-type Ser/Thr protein kinase | C-StkP | C-terminal domain of StkP kinase | circular dichroism | peptidoglycan | 6-aminopenicillanic acid | PASTA domain | 6-APA | NAG | PGN | STPK | penicillin-binding protein and Ser/Thr protein kinase-associated domain | BACTERIA | PASTA DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta-Lactam antibiotics | PKNB | IDENTIFICATION | CELL BIOLOGY | CIRCULAR-DICHROISM | ENZYME | BIOPHYSICS | EXPRESSION | Peptidoglycan - metabolism | beta-Lactams - metabolism | Peptidoglycan - chemistry | Models, Molecular | Cell Wall - chemistry | beta-Lactams - chemistry | Bacterial Proteins | Anti-Bacterial Agents | Protein Binding | Protein Interaction Domains and Motifs | Protein-Serine-Threonine Kinases - chemistry | Spectrum Analysis | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Streptococcus pneumoniae - enzymology | β-lactam antibiotics | PASTA domains
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Loading RightsCancer Treatment Reviews, ISSN 0305-7372, 2011, Volume 38, Issue 2, pp. 133 - 142
Abstract The transmembrane protein HER2 is over-expressed in approximately 15% of invasive breast cancers as a result of HER2 gene amplification. HER2...
Hematology, Oncology and Palliative Medicine | HER2-ECD | Shedding | Tumor markers | Serum HER2 | Breast cancer | Predictive value of tests | Oncogene Protein HER2 | ELISA | PROGRESSION-FREE SURVIVAL | MONOCLONAL-ANTIBODY | METASTATIC SITES | TRASTUZUMAB-BASED THERAPY | GROWTH-FACTOR RECEPTOR | ONCOLOGY | TERMINAL FRAGMENTS | GENE AMPLIFICATION | FATTY-ACID SYNTHASE | 1ST-LINE THERAPY | HORMONE-RECEPTOR | Biomarkers, Tumor - blood | Protein Structure, Tertiary | Breast Neoplasms - enzymology | Animals | Humans | Receptor, ErbB-2 - metabolism | Biomarkers, Tumor - metabolism | Female | Mammary Neoplasms, Experimental - metabolism | Mammary Neoplasms, Experimental - blood | Receptor, ErbB-2 - blood | Care and treatment | Metastasis | Genes | Enzyme-linked immunosorbent assay | Cancer
Hematology, Oncology and Palliative Medicine | HER2-ECD | Shedding | Tumor markers | Serum HER2 | Breast cancer | Predictive value of tests | Oncogene Protein HER2 | ELISA | PROGRESSION-FREE SURVIVAL | MONOCLONAL-ANTIBODY | METASTATIC SITES | TRASTUZUMAB-BASED THERAPY | GROWTH-FACTOR RECEPTOR | ONCOLOGY | TERMINAL FRAGMENTS | GENE AMPLIFICATION | FATTY-ACID SYNTHASE | 1ST-LINE THERAPY | HORMONE-RECEPTOR | Biomarkers, Tumor - blood | Protein Structure, Tertiary | Breast Neoplasms - enzymology | Animals | Humans | Receptor, ErbB-2 - metabolism | Biomarkers, Tumor - metabolism | Female | Mammary Neoplasms, Experimental - metabolism | Mammary Neoplasms, Experimental - blood | Receptor, ErbB-2 - blood | Care and treatment | Metastasis | Genes | Enzyme-linked immunosorbent assay | Cancer
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Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2
Nature, ISSN 0028-0836, 08/2003, Volume 424, Issue 6949, pp. 677 - 681
Synaptic transmission from excitatory nerve cells in the mammalian brain is largely mediated by AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic...
N-TERMINAL DOMAINS | GLUTAMATE RECEPTORS | NMDA RECEPTORS | SYNAPSES | DESENSITIZATION | MULTIDISCIPLINARY SCIENCES | NEURONS | CHANNELS | EXPRESSION | BINDING-PROTEINS | DEPENDENCE | Protein Structure, Tertiary | RNA, Small Interfering - genetics | gamma-Aminobutyric Acid - metabolism | Humans | Cells, Cultured | Receptors, AMPA - chemistry | Rats | Cell Size | Recombinant Fusion Proteins - chemistry | Hippocampus - cytology | Recombinant Fusion Proteins - metabolism | Hippocampus - metabolism | Animals | Interneurons - metabolism | Dendrites - physiology | Recombinant Fusion Proteins - genetics | Interneurons - cytology | COS Cells | Receptors, AMPA - genetics | Receptors, AMPA - metabolism | RNA, Small Interfering - metabolism | Spine | Nervous system | Cells
N-TERMINAL DOMAINS | GLUTAMATE RECEPTORS | NMDA RECEPTORS | SYNAPSES | DESENSITIZATION | MULTIDISCIPLINARY SCIENCES | NEURONS | CHANNELS | EXPRESSION | BINDING-PROTEINS | DEPENDENCE | Protein Structure, Tertiary | RNA, Small Interfering - genetics | gamma-Aminobutyric Acid - metabolism | Humans | Cells, Cultured | Receptors, AMPA - chemistry | Rats | Cell Size | Recombinant Fusion Proteins - chemistry | Hippocampus - cytology | Recombinant Fusion Proteins - metabolism | Hippocampus - metabolism | Animals | Interneurons - metabolism | Dendrites - physiology | Recombinant Fusion Proteins - genetics | Interneurons - cytology | COS Cells | Receptors, AMPA - genetics | Receptors, AMPA - metabolism | RNA, Small Interfering - metabolism | Spine | Nervous system | Cells
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Loading RightsScientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 17159 - 11
Familial mutations in C99 can increase the total level of the soluble A beta peptides produced by proteolysis, as well as the A beta 42/A beta 40 ratio, both...
FLEMISH MUTATION | CEREBRAL-HEMORRHAGE | CHOLESTEROL | GENE | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | TRANSMEMBRANE DOMAIN | C-TERMINAL DOMAIN | GAMMA-SECRETASE | PRECURSOR-PROTEIN APP | PEPTIDE | Amyloidogenesis | Fourier transforms | Nuclear magnetic resonance--NMR | Mutation | Proteolysis
FLEMISH MUTATION | CEREBRAL-HEMORRHAGE | CHOLESTEROL | GENE | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | TRANSMEMBRANE DOMAIN | C-TERMINAL DOMAIN | GAMMA-SECRETASE | PRECURSOR-PROTEIN APP | PEPTIDE | Amyloidogenesis | Fourier transforms | Nuclear magnetic resonance--NMR | Mutation | Proteolysis
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Loading RightsCurrent Molecular Pharmacology, ISSN 1874-4672, 2017, Volume 10, Issue 4, pp. 318 - 324
Corticotropin releasing factor (CRF) receptors belong to the secretin family of G protein coupled receptors (GPCRs) and are responsible for initiating...
Ligand binding | GPCR | Structure | CRF receptors | First extracellular domain | ECD | LIGAND-BINDING | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | 1ST-EXTRACELLULAR DOMAIN | first extracellular domain | structure | SIGNAL-PEPTIDE | CORTICOTROPIN-RELEASING-FACTOR | SOLUBLE FORM | MOLECULAR RECOGNITION | N-TERMINAL DOMAIN | NMR STRUCTURE | PHARMACOLOGY & PHARMACY | ligand binding | PROTEIN-COUPLED-RECEPTOR
Ligand binding | GPCR | Structure | CRF receptors | First extracellular domain | ECD | LIGAND-BINDING | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | 1ST-EXTRACELLULAR DOMAIN | first extracellular domain | structure | SIGNAL-PEPTIDE | CORTICOTROPIN-RELEASING-FACTOR | SOLUBLE FORM | MOLECULAR RECOGNITION | N-TERMINAL DOMAIN | NMR STRUCTURE | PHARMACOLOGY & PHARMACY | ligand binding | PROTEIN-COUPLED-RECEPTOR
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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2004, Volume 101, Issue 35, pp. 12836 - 12841
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands' effects...
Proteins | Biological Sciences | Receptors | Databases | Mutagenesis | Amino acids | Ligands | Hormones | Peptide hormones | Binding sites | Family structure | UROCORTIN-III | METABOTROPIC GLUTAMATE-RECEPTOR | CORTICOTROPIN-RELEASING-FACTOR | LIGAND-BINDING | DISULFIDE PATTERN | CRYSTAL-STRUCTURE | AMINO-ACIDS | MULTIDISCIPLINARY SCIENCES | N-TERMINAL DOMAIN | HIGH-AFFINITY | 1ST EXTRACELLULAR DOMAIN | Peptide Hormones - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Animals | Magnetic Resonance Spectroscopy | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Mice | Binding Sites | Receptors, G-Protein-Coupled - chemistry | Corticotropin releasing hormone | Physiological aspects | Research | Ligands (Biochemistry)
Proteins | Biological Sciences | Receptors | Databases | Mutagenesis | Amino acids | Ligands | Hormones | Peptide hormones | Binding sites | Family structure | UROCORTIN-III | METABOTROPIC GLUTAMATE-RECEPTOR | CORTICOTROPIN-RELEASING-FACTOR | LIGAND-BINDING | DISULFIDE PATTERN | CRYSTAL-STRUCTURE | AMINO-ACIDS | MULTIDISCIPLINARY SCIENCES | N-TERMINAL DOMAIN | HIGH-AFFINITY | 1ST EXTRACELLULAR DOMAIN | Peptide Hormones - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Animals | Magnetic Resonance Spectroscopy | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Mice | Binding Sites | Receptors, G-Protein-Coupled - chemistry | Corticotropin releasing hormone | Physiological aspects | Research | Ligands (Biochemistry)
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Loading RightsEMBO JOURNAL, ISSN 0261-4189, 05/2008, Volume 27, Issue 9, pp. 1321 - 1332
The G-protein-coupled receptor (GPCR) activated by the neurotransmitter GABA is made up of two subunits, GABA(B1) and GABA(B2). GABA(B1) binds agonists,...
ACID RECEPTOR | METABOTROPIC GLUTAMATE-RECEPTOR | ACTIVATION | LIGAND-BINDING | class C GPCRs | BIOCHEMISTRY & MOLECULAR BIOLOGY | drug addiction | TRAFFICKING | MOLECULAR DETERMINANTS | SUBUNITS | baclofen | CELL BIOLOGY | anxiety | TERMINAL DOMAINS | allosteric modulators | REGIONS | HEPTAHELICAL DOMAIN | Protein Structure, Tertiary | Cell Line | Receptors, GABA-B - genetics | Immunoprecipitation | Enzyme-Linked Immunosorbent Assay | Protein Structure, Secondary | gamma-Aminobutyric Acid - metabolism | Allosteric Regulation | Humans | Computational Biology | Cercopithecus aethiops | Models, Molecular | Structure-Activity Relationship | Binding Sites - genetics | Blotting, Western | Polysaccharides - metabolism | Receptors, GABA-B - chemistry | Animals | Transfection | Fluorescence Resonance Energy Transfer | Protein Binding | COS Cells | Dimerization | Receptors, GABA-B - metabolism | Life Sciences | Neurons and Cognition | Neurobiology
ACID RECEPTOR | METABOTROPIC GLUTAMATE-RECEPTOR | ACTIVATION | LIGAND-BINDING | class C GPCRs | BIOCHEMISTRY & MOLECULAR BIOLOGY | drug addiction | TRAFFICKING | MOLECULAR DETERMINANTS | SUBUNITS | baclofen | CELL BIOLOGY | anxiety | TERMINAL DOMAINS | allosteric modulators | REGIONS | HEPTAHELICAL DOMAIN | Protein Structure, Tertiary | Cell Line | Receptors, GABA-B - genetics | Immunoprecipitation | Enzyme-Linked Immunosorbent Assay | Protein Structure, Secondary | gamma-Aminobutyric Acid - metabolism | Allosteric Regulation | Humans | Computational Biology | Cercopithecus aethiops | Models, Molecular | Structure-Activity Relationship | Binding Sites - genetics | Blotting, Western | Polysaccharides - metabolism | Receptors, GABA-B - chemistry | Animals | Transfection | Fluorescence Resonance Energy Transfer | Protein Binding | COS Cells | Dimerization | Receptors, GABA-B - metabolism | Life Sciences | Neurons and Cognition | Neurobiology
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Loading RightsJournal of Biological Chemistry, ISSN 0021-9258, 12/2010, Volume 285, Issue 49, pp. 38580 - 38589
The corticotropin-releasing factor (CRF) peptide hormone family members coordinate endocrine, behavioral, autonomic, and metabolic responses to stress and play...
CHIMERIC RECEPTORS | ASTRESSIN ANALOGS | LIGAND-BINDING | GLUCAGON-LIKE PEPTIDE-1 | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-TERMINAL DOMAIN | PARATHYROID-HORMONE | COMPETITIVE ANTAGONISTS | 1ST-EXTRACELLULAR DOMAIN | PROTEIN-COUPLED-RECEPTOR | Protein Structure, Tertiary | Receptors, Corticotropin-Releasing Hormone - metabolism | Protein Structure, Secondary | Humans | Receptors, Corticotropin-Releasing Hormone - agonists | Receptors, Corticotropin-Releasing Hormone - genetics | Corticotropin-Releasing Hormone - chemistry | Corticotropin-Releasing Hormone - metabolism | Protein Structure, Quaternary | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Corticotropin-Releasing Hormone - genetics | Receptors, Corticotropin-Releasing Hormone - chemistry | Protein Structure and Folding | Corticotropin-releasing Factor | G Protein-coupled Receptors (GPCR) | NMR | ECD1-CRF-R1 | alphahcCRF | Peptide Biosynthesis | Peptides | CRF | Peptide Chemical Synthesis | Peptide Conformation
CHIMERIC RECEPTORS | ASTRESSIN ANALOGS | LIGAND-BINDING | GLUCAGON-LIKE PEPTIDE-1 | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-TERMINAL DOMAIN | PARATHYROID-HORMONE | COMPETITIVE ANTAGONISTS | 1ST-EXTRACELLULAR DOMAIN | PROTEIN-COUPLED-RECEPTOR | Protein Structure, Tertiary | Receptors, Corticotropin-Releasing Hormone - metabolism | Protein Structure, Secondary | Humans | Receptors, Corticotropin-Releasing Hormone - agonists | Receptors, Corticotropin-Releasing Hormone - genetics | Corticotropin-Releasing Hormone - chemistry | Corticotropin-Releasing Hormone - metabolism | Protein Structure, Quaternary | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Corticotropin-Releasing Hormone - genetics | Receptors, Corticotropin-Releasing Hormone - chemistry | Protein Structure and Folding | Corticotropin-releasing Factor | G Protein-coupled Receptors (GPCR) | NMR | ECD1-CRF-R1 | alphahcCRF | Peptide Biosynthesis | Peptides | CRF | Peptide Chemical Synthesis | Peptide Conformation
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13.
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NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains
The FEBS Journal, ISSN 1742-464X, 05/2013, Volume 280, Issue 9, pp. 2068 - 2084
Chemokines constitute a large family of small proteins that regulate leukocyte trafficking to the site of inflammation by binding to specific cell‐surface...
gp120 | sulfotyrosine | HIV‐1 | chemokines | HIV-1 | VIRUS TYPE-1 ENTRY | CORECEPTOR | CHEMOKINE-RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | TYROSINE SULFATION | ENVELOPE GLYCOPROTEIN | N-TERMINUS | HIV-1 GP120 | AMINO-TERMINAL DOMAIN | BINDING | WATER SUPPRESSION | Protein Structure, Tertiary | Amino Acid Sequence | Humans | Models, Molecular | Molecular Sequence Data | Recombinant Fusion Proteins - chemistry | Amino Acid Motifs | Chemokine CCL5 - chemistry | Cystine - chemistry | Surface Properties | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Receptors, CCR5 - chemistry | Binding Sites | Peptides | Nuclear magnetic resonance spectroscopy | Biosynthesis | Nuclear magnetic resonance--NMR | Cellular biology | Spectrum analysis | Chemokines
gp120 | sulfotyrosine | HIV‐1 | chemokines | HIV-1 | VIRUS TYPE-1 ENTRY | CORECEPTOR | CHEMOKINE-RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | TYROSINE SULFATION | ENVELOPE GLYCOPROTEIN | N-TERMINUS | HIV-1 GP120 | AMINO-TERMINAL DOMAIN | BINDING | WATER SUPPRESSION | Protein Structure, Tertiary | Amino Acid Sequence | Humans | Models, Molecular | Molecular Sequence Data | Recombinant Fusion Proteins - chemistry | Amino Acid Motifs | Chemokine CCL5 - chemistry | Cystine - chemistry | Surface Properties | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Receptors, CCR5 - chemistry | Binding Sites | Peptides | Nuclear magnetic resonance spectroscopy | Biosynthesis | Nuclear magnetic resonance--NMR | Cellular biology | Spectrum analysis | Chemokines
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