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PLoS ONE, ISSN 1932-6203, 07/2012, Volume 7, Issue 7, pp. e41823 - e41823
The multiligand Receptor for Advanced Glycation End products (RAGE) is involved in various pathophysiological processes, including diabetic inflammatory... 
CEREBELLAR GRANULE NEURONS | ALPHA-SECRETASE | PATHWAY | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | GROWTH | POLYPEPTIDE PACAP | AMYLOID PRECURSOR PROTEIN | CLEAVAGE | GLYCATION END-PRODUCTS | SOLUBLE RECEPTOR | ADAM17 Protein | Amyloid Precursor Protein Secretases - genetics | Humans | Receptors, Vasopressin - metabolism | Male | Phosphatidylinositol 3-Kinases - metabolism | Gene Knockdown Techniques | MAP Kinase Signaling System | Protease Inhibitors - pharmacology | Matrix Metalloproteinase 9 - metabolism | RNA Interference | Matrix Metalloproteinase 9 - genetics | Proteolysis | Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology | HEK293 Cells | Lung - metabolism | Membrane Proteins - metabolism | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - metabolism | Hydroxamic Acids - pharmacology | Receptor for Advanced Glycation End Products | Calcium Signaling | Cyclic AMP-Dependent Protein Kinases - metabolism | ADAM Proteins - antagonists & inhibitors | Matrix Metalloproteinase 2 - metabolism | Membrane Proteins - genetics | Dipeptides - pharmacology | ADAM10 Protein | Adenylyl Cyclases - metabolism | Pituitary Adenylate Cyclase-Activating Polypeptide - physiology | Matrix Metalloproteinase 2 - genetics | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Receptors, Oxytocin - metabolism | Animals | Membrane Proteins - antagonists & inhibitors | Phosphatidylinositol 3-Kinases - physiology | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Receptors, Immunologic - metabolism | Alzheimer's disease | Health aspects | G proteins | Protein kinase C | G protein-coupled receptors | Disease | Lung | Biochemistry | Odorant receptors | Proteins | Adenylate cyclase | Receptors | Cell activation | Growth factors | Vasopressin V2 receptors | Immunoglobulins | Advanced glycosylation end products | Polypeptides | Oxytocin | Medical treatment | Glycosylation | Insulin | Membrane proteins | Studies | Pituitary adenylate cyclase-activating polypeptide | Pharmacy | Ligands | Shedding | Biotechnology | PAC1 protein | Calcium | Medical services | Stimulation | Kinases | Cell surface | Inflammatory diseases | Calcium signalling | Rodents | Cascades | Atherosclerosis | Vomeronasal organ | Recombinant | Diabetes mellitus | siRNA | Pharmacology | Vasopressin | Gelatinase B | Phospholipase C | Phospholipase | Cell lines | Diabetes | Ca2+/calmodulin-dependent protein kinase II | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 32, pp. 19584 - 19596
The photoreceptor-specific proteins guanylyl cyclase-activating proteins (GCAPs) bind and regulate retinal membrane guanylyl cyclase 1 (RetGC1) but not... 
LEBER CONGENITAL AMAUROSIS | KNOCK-OUT MICE | MECHANISM | CONE-ROD DYSTROPHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATIONS | CALCIUM SENSITIVITY | CATALYTIC-ACTIVITY | IDENTIFICATION | PHOTORECEPTOR CELLS | DEGENERATION | Humans | Protein Multimerization | Eye Proteins - chemistry | Molecular Sequence Data | Recombinant Fusion Proteins - metabolism | HEK293 Cells | Receptors, Cell Surface - chemistry | Protein Interaction Domains and Motifs | Eye Proteins - genetics | Binding Sites | Guanylate Cyclase - chemistry | Genes, Reporter | Amino Acid Sequence | Guanylate Cyclase-Activating Proteins - chemistry | Protein Structure, Secondary | Signal Transduction | Methionine - metabolism | Receptors, Atrial Natriuretic Factor - metabolism | Gene Expression Regulation | Models, Molecular | Receptors, Cell Surface - metabolism | Guanylate Cyclase - metabolism | Recombinant Fusion Proteins - chemistry | Arginine - chemistry | Guanylate Cyclase-Activating Proteins - metabolism | Sequence Alignment | Eye Proteins - metabolism | Methionine - chemistry | Receptors, Atrial Natriuretic Factor - chemistry | Protein Binding | Receptors, Atrial Natriuretic Factor - genetics | Recombinant Fusion Proteins - genetics | Guanylate Cyclase - genetics | Guanylate Cyclase-Activating Proteins - genetics | Luminescent Proteins - genetics | Mutation | Arginine - metabolism | Amino Acid Substitution | Luminescent Proteins - metabolism | Receptors, Cell Surface - genetics | Index Medicus | eye | guanylate cyclase (guanylyl cyclase) | calcium-binding protein | cyclic GMP (cGMP) | phototransduction | Neurobiology
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4429 - 4441
GCAP1, a member of the neuronal calcium sensor subclass of the calmodulin superfamily, confers Ca2+-sensitive activation of retinal guanylyl cyclase 1... 
MYRISTOYL SWITCH | TARGET | CA2+-BINDING PROTEINS | NMR | NEURONAL CALCIUM SENSOR | MECHANISM | MOLECULAR-STRUCTURE | CA2 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING | Calcium - metabolism | Protein Unfolding | Humans | Eye Proteins - chemistry | Molecular Sequence Data | Eye Proteins - agonists | Calcium - chemistry | Cattle | HEK293 Cells | Receptors, Cell Surface - chemistry | Eye Proteins - genetics | Binding Sites | Guanylate Cyclase - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Guanylate Cyclase-Activating Proteins - chemistry | Lipoylation | Receptors, Cell Surface - agonists | Models, Molecular | Receptors, Cell Surface - metabolism | Recombinant Proteins - chemistry | Guanylate Cyclase - metabolism | Magnesium - metabolism | Guanylate Cyclase-Activating Proteins - metabolism | Magnesium - chemistry | Myristic Acid - metabolism | Sequence Alignment | Animals | Eye Proteins - metabolism | Guanylate Cyclase - genetics | Guanylate Cyclase-Activating Proteins - genetics | Protein Conformation | Protein Processing, Post-Translational | Mutation | Amino Acid Substitution | Receptors, Cell Surface - genetics | Index Medicus | vision | calorimetry | calcium | calcium-binding protein | Signal Transduction | nuclear magnetic resonance (NMR) | guanylate cyclase (guanylyl cyclase) | phototransduction
Journal Article
BBA - Proteins and Proteomics, ISSN 1570-9639, 10/2015, Volume 1854, Issue 10, pp. 1325 - 1337
Neuronal responses to Ca -signals are provided by EF-hand-type neuronal Ca -sensor (NCS) proteins, which have similar core domains containing Ca -binding and... 
Photoreceptors | Recoverin | Neuronal calcium sensor (NCS) protein | Rhodopsin kinase (RK, GRK1) | Retinal guanylate cyclase (ROS-GC1) | Guanylate cyclase-activating protein 2 (GCAP2) | NEURONAL CALCIUM SENSOR | RHODOPSIN KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | 3-DIMENSIONAL STRUCTURE | CONFORMATIONAL-CHANGES | BIOPHYSICS | STRUCTURAL BASIS | CA2 | CA2+-MYRISTOYL SWITCH | CA2+-BINDING SITES | BINDING | Phosphorylation | Rod Cell Outer Segment - metabolism | Calcium - metabolism | Protein Multimerization | Molecular Sequence Data | Recombinant Fusion Proteins - metabolism | Recoverin - chemistry | Cattle | G-Protein-Coupled Receptor Kinase 1 - metabolism | Binding Sites | Calcium Signaling | Recoverin - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Guanylate Cyclase-Activating Proteins - chemistry | Protein Structure, Secondary | Gene Expression Regulation | Guanylate Cyclase - metabolism | Recombinant Fusion Proteins - chemistry | Guanylate Cyclase-Activating Proteins - metabolism | Sequence Alignment | Animals | G-Protein-Coupled Receptor Kinase 1 - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Recombinant Fusion Proteins - genetics | Guanylate Cyclase - genetics | Guanylate Cyclase-Activating Proteins - genetics | Recoverin - metabolism | Proteins | Phosphotransferases | Rhodopsin
Journal Article
Biochemistry, ISSN 0006-2960, 11/2011, Volume 50, Issue 44, pp. 9511 - 9519
Journal Article
Cellular Signalling, ISSN 0898-6568, 11/2013, Volume 25, Issue 11, pp. 2222 - 2230
Journal Article
Experimental Cell Research, ISSN 0014-4827, 03/2014, Volume 322, Issue 1, pp. 108 - 121
PACAP and its cognate peptide VIP participate in various biological functions, including myelin maturation and synthesis. However, defining whether these... 
PACAP | Myelin | Peripheral nerve sheath tumor | VIP | Myelin-associated glycoprotein | Myelin basic protein | Protein zero | SURVIVAL | NERVOUS-SYSTEM | REGENERATION | KINASE | PROLIFERATION | PEPTIDE | CEREBELLAR GRANULE CELLS | CELL BIOLOGY | TUMOR MPNST CELLS | ONCOLOGY | MICE | POLYPEPTIDE | Myelin Basic Protein - metabolism | Myelin-Associated Glycoprotein - genetics | Myelin-Associated Glycoprotein - metabolism | Rats | Phosphatidylinositol 3-Kinases - metabolism | Schwann Cells - metabolism | Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I - physiology | Myelin Proteins - genetics | Myelin Basic Protein - genetics | Receptors, Vasoactive Intestinal Peptide, Type II - physiology | Animals | Signal Transduction - drug effects | Vasoactive Intestinal Peptide - pharmacology | Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology | Cell Line, Tumor | Myelin P0 Protein - genetics | Signal Transduction - physiology | Gene Expression Regulation, Neoplastic - drug effects | Myelin P0 Protein - metabolism | Myelin Proteins - metabolism | Oncogene Protein v-akt - metabolism | Enzyme Activation - physiology | Schwann Cells - drug effects | Genetic research | Starvation | Gene expression | Myelin proteins | Signal transduction | Protein expression | Phosphorylation | Cellular biology | Peptides | Rodents | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2013, Volume 8, Issue 3, pp. e57037 - e57037
A wide range of growth factors encode information into specific temporal patterns of MAP kinase (MAPK) and CREB phosphorylation, which are further decoded by... 
SIGNALING PATHWAYS | ACTIVATION | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | NEURONAL DIFFERENTIATION | NETWORKS | MECHANISMS | PC12 CELLS | NEGATIVE FEEDBACK | ERK OSCILLATIONS | NERVE GROWTH-FACTOR | PC12 Cells - cytology | Proto-Oncogene Proteins c-fos - metabolism | Nerve Growth Factor - pharmacology | Rats | Transcription Factors - genetics | Gene Expression Regulation - drug effects | Transcription Factors - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | PC12 Cells - drug effects | Animals | Signal Transduction - drug effects | Time Factors | Models, Biological | PC12 Cells - metabolism | Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology | Cyclic AMP Response Element-Binding Protein - metabolism | Anisomycin - pharmacology | Mitogen-Activated Protein Kinases - genetics | Proto-Oncogene Proteins c-fos - genetics | Genes, Immediate-Early | Phosphorylation - drug effects | Mitogen-Activated Protein Kinases - metabolism | Physiological aspects | Nerve growth factor | Transcription factors | Research | Gene expression | Analysis | Phosphorylation | EGR-1 protein | Extracellular signal-regulated kinase | MAP kinase | Data processing | Decoding | Cyclic AMP response element-binding protein | Kinases | JunB protein | Pituitary adenylate cyclase-activating polypeptide | Filters | Epidermal growth factor | Fos protein | Rodents | Information processing | Signal processing | Growth factors | c-Fos protein | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2013, Volume 8, Issue 11, pp. e81822 - e81822
Journal Article