Search results for "TYR"

showing 10 items of 2017 documents

Receptor-guided 3D-QSAR approach for the discovery of c-kit tyrosine kinase inhibitors

2012

Studies of the the three-dimensional quantitative structure–activity relationships for ninety-five c-kit tyrosine kinase inhibitors were performed. Based on a co-crystallized compound (1 T46), known inhibitors were aligned with c-kit by induced-fit docking, and multiple training/test set splitting was performed to validate the selected pharmacophore model. The best pharmacophore model consisted of five features: one hydrogen-bond donor and four aromatic rings. Reliable statistics were obtained (R 2 = 0.95, R pred 2  = 0.75), and the model was validated by using it to select c-kit inhibitors from a database; 82.1% of the hits it retrieved were active. Accordingly, our model can be reliably u…

Models MolecularQuantitative structure–activity relationshipChemistryStereochemistryOrganic ChemistryQuantitative Structure-Activity RelationshipC-kit . 3D-QSAR . Kohonen maps . Induced-fit dockingSettore CHIM/08 - Chimica FarmaceuticaCatalysisComputer Science ApplicationsInorganic ChemistryProto-Oncogene Proteins c-kitComputational Theory and MathematicsDocking (molecular)Drug DiscoveryPhysical and Theoretical ChemistryPharmacophoreReceptorTyrosine kinaseProtein Kinase Inhibitors
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TOMOCOMD-CARDD descriptors-based virtual screening of tyrosinase inhibitors: evaluation of different classification model combinations using bond-bas…

2006

Abstract A new set of bond-level molecular descriptors (bond-based linear indices) are used here in QSAR (quantitative structure–activity relationship) studies of tyrosinase inhibitors, for finding functions that discriminate between the tyrosinase inhibitor compounds and inactive ones. A database of 246 compounds was collected for this study; all organic chemicals were reported as tyrosinase inhibitors; they had great structural diversity. This dataset can be considered as a helpful tool, not only for theoretical chemists but also for other researchers in this area. The set used as inactive has 412 drugs with other clinical uses. Twelve LDA-based QSAR models were obtained, the first six us…

Models MolecularQuantitative structure–activity relationshipMolecular modelStereochemistryTyrosinaseClinical BiochemistryPharmaceutical ScienceQuantitative Structure-Activity RelationshipBiochemistryModels BiologicalChemometricsMolecular descriptorDrug DiscoveryComputer SimulationMolecular BiologyVirtual screeningMolecular StructureChemistryMonophenol MonooxygenaseOrganic ChemistryDiscriminant AnalysisLinear discriminant analysisModels ChemicalTopological indexMolecular MedicineBiological systemAgaricalesPeptidesAlgorithmsBioorganicmedicinal chemistry
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3-acetylaltholactone and related styryl-lactones, mitochondrial respiratory chain inhibitors.

2000

A novel furano-pyrone, 3-acetylaltholactone, and two other known styryl-lactones, altholactone and 5-acetoxyisogoniothalamin oxide, have been isolated from Goniothalamus arvensis (Annonaceae) stem bark. We report here the isolation and structural elucidation of these compounds with furane-pyrone and styryl-pyrone skeletons, postulating also for the first time their mechanism of cytotoxicity based on inhibition on mammalian mitochondrial respiratory chain.

Models MolecularStereochemistryChemical structureSubmitochondrial ParticlesMolecular ConformationPlant ScienceHorticultureBiochemistryMitochondria HeartStyrenesLactonesOxygen ConsumptionAnimals3-acetylaltholactoneCytotoxicityFuransMolecular BiologyGoniothalamusStem barkPlants MedicinalbiologyMolecular StructurePlant StemsUncoupling AgentsGeneral Medicinebiology.organism_classificationNADKineticsMitochondrial respiratory chainAnnonaceaePyronesvisual_artvisual_art.visual_art_mediumBarkCattlePhytochemistry
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Tyrosinase versus Catechol Oxidase: One Asparagine Makes the Difference

2015

Tyrosinases mediate the ortho-hydroxylation and two-electron oxidation of monophenols to ortho-quinones. Catechol oxidases only catalyze the oxidation of diphenols. Although it is of significant interest, the origin of the functional discrimination between tyrosinases and catechol oxidases has been unclear. Recently, it has been postulated that a glutamate and an asparagine bind and activate a conserved water molecule towards deprotonation of monophenols. Here we demonstrate for the first time that a polyphenoloxidase, which exhibits only diphenolase activity, can be transformed to a tyrosinase by mutation to introduce an asparagine. The asparagine and a conserved glutamate are necessary to…

Models MolecularStereochemistryCopper proteinTyrosinase010402 general chemistrymedicine.disease_cause01 natural sciencesCatalysischemistry.chemical_compoundDeprotonationmedicineMoleculeAsparagineCatechol oxidaseCatecholMutationbiologyMonophenol Monooxygenase010405 organic chemistryGeneral Chemistry0104 chemical scienceschemistryBiochemistrybiology.proteinAsparagineCatechol OxidaseAngewandte Chemie International Edition
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Tyrosinase Enzyme: 1. An Overview on a Pharmacological Target

2014

The tyrosinase enzyme (EC 1.14.18.1) is an oxidoreductase inside the general enzyme classification and is involved in the oxidation and reduction process in the epidermis. These chemical reactions that the enzyme catalyzes are of principal importance in the melanogenesis process. This process of melanogenesis is related to the melanin formation, a heteropolymer of indolic nature that provides the different tonalities in the skin and helps to the protection from the ultraviolet radiation. However, a pigment overproduction, come up by the action of the tyrosinase, can cause different disorders in the skin related to the hyperpigmentation. Several studies mainly focused on the characteristics …

Models Molecularchemistry.chemical_classificationMolecular StructureEpidermis (botany)Monophenol MonooxygenaseTyrosinaseGeneral MedicineHyperpigmentationMelaninStructure-Activity RelationshipEnzymechemistryBiochemistryOxidoreductaseDrug DiscoveryMolecular mechanismmedicineAnimalsHumansEnzyme Inhibitorsmedicine.symptomOverproductionCurrent Topics in Medicinal Chemistry
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Untersuchungen zur Reaktionsfähigkeit statistisch verteilter Estergruppierungen in Copolymeren aus Styrol und Acrylsäureestern

1974

Die Aminolyse der ortho- und para-Nitrophenylester von Propionsaure, Isobuttersaure, 4-Phenylbuttersaure und 4-Phenylvaleriansaure sowie von Copolymeren aus Styrol und geringen Mengen Acrylsaure wurde mit Butylamin in Dioxan untersucht. Bei grosem Aminuberschus reagieren die niedermolekularen Ester streng nach erster Ordnung, wobei die Reaktionsgeschwindigkeit durch Zugabe von Polystyrol nicht beeinflust wird. Fur Copolymere, deren Reaktionsgeschwindigkeit deutlich geringer ist, erhalt man dagegen keine Beziehung erster Ordnung, obwohl die Anfangsgeschwindigkeit der Gesamtkonzentration der Estergruppen direkt proportional ist. Bei den Copolymeren erhalt man annahernd die gleichen Aktivierun…

Molar massPolymers and PlasticsButylamineMedicinal chemistryStyreneIsobutyric acidchemistry.chemical_compoundColloid and Surface ChemistryPropanoic acidAminolysischemistryPolymer chemistryMaterials ChemistryAmine gas treatingPhysical and Theoretical ChemistryAcrylic acidDie Makromolekulare Chemie
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In murine 3T3 fibroblasts, different second messenger pathways resulting in the induction of NO synthase II (iNOS) converge in the activation of tran…

1996

Transcription factor NF-kappaB is essential for the induction of nitric oxide synthase (NOS) II (iNOS) by bacterial lipopolysaccharide in murine macrophages (Xie, Q. W., Kashiwabara, Y., and Nathan, C. (1994) J. Biol. Chem. 269, 4705-4708). In 3T3 fibroblasts, agents other than cytokines are efficacious inducers of NOS II expression. In addition to cytokines such as interferon-gamma or tumor necrosis factor-alpha, protein kinase C-stimulating agents such as tetradecanoylphorbol-13-acetate, or cyclic AMP-elevating agents such as forskolin and 8-bromo-cAMP markedly increased NOS II mRNA (measured by Sl nuclease and RNase protection analyses), NOS II protein (determined by Western blotting), a…

Molecular Sequence DataBiochemistrySecond Messenger SystemsDexamethasoneGene Expression Regulation Enzymologicchemistry.chemical_compoundMicePyrrolidine dithiocarbamateTransforming Growth Factor betaAnimalsHumansAmino Acid SequenceRNA MessengerNuclear proteinProtein kinase AMolecular BiologyTranscription factorProtein Kinase CDNA PrimersForskolinbiologyBase SequenceNF-kappa BReceptor Protein-Tyrosine KinasesCell Biology3T3 CellsMolecular biologyCyclic AMP-Dependent Protein KinasesActinsNitric oxide synthasechemistryEnzyme InductionSecond messenger systembiology.proteinTumor necrosis factor alphaNitric Oxide SynthaseThe Journal of biological chemistry
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Receptor protein-tyrosine phosphatases: origin of domains (catalytic domain, Ig-related domain, fibronectin type III module) based on the sequence of…

2001

Abstract Reversible tyrosine phosphorylation of proteins is one of the major regulatory physiological events in response to cell-cell- and cell-matrix contact in Metazoa. Previously it was documented that the tyrosine phosphorylating enzymes, the tyrosine kinases (TKs), are autapomorphic characters of Metazoa, including sponges. In this paper the tyrosine dephosphorylating enzymes, the protein-tyrosine phosphatases (PTPs), are studied which can be grouped into two subfamilies, the soluble PTPs and the receptor PTPs (RPTPs). PTPs are characterized by one PTPase domain which interestingly comprises sequence similarity to yeast PTPs. In contrast to the PTPs, the RPTPs – which have been found o…

Molecular Sequence DataImmunoglobulinsBiologyPolymerase Chain ReactionEvolution Molecularchemistry.chemical_compoundCatalytic DomainGene duplicationGeneticsAnimalsAmino Acid SequenceTyrosineCloning MolecularPhylogenychemistry.chemical_classificationPhylogenetic treeSequence Homology Amino AcidTyrosine phosphorylationGeneral MedicineProtein-Tyrosine KinasesAmino acidFibronectinsPoriferaProtein Structure TertiaryOpen reading framechemistryBiochemistryPhosphorylationProtein Tyrosine PhosphatasesTyrosine kinaseSequence AnalysisGene
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Multiple Ig-like featuring genes divergent within and among individuals of the marine sponge Geodia cydonium.

1998

Abstract The receptor tyrosine kinase of the marine sponge Geodia cydonium features two extracellular Ig-like domains in which we recently documented RT-PCR polymorphism among individuals. Genomic-PCR analysis presented here revealed 14 unique sequences from four sponges, differing predominantly in the sequence of an intron which splits the Ig-like domains. Nevertheless, analysis of putative coding regions in 19 distinct clones (156–159 aa) from seven sponges revealed 69 positions of nucleotide substitutions, 67.6% of them non-synonymous, translating into 43 positions of divergent residues. Excluding aa deletions, these 19 sequences share pairwise aa identities of 89–99%. In three sponges, …

Molecular Sequence DataImmunoglobulinsGenomePolymerase Chain ReactionReceptor tyrosine kinaselaw.inventionlawMHC class IGeneticsCoding regionAnimalsHumansAmino Acid SequenceGenePolymerase chain reactionGeneticsPolymorphism GeneticbiologyBase SequenceSequence Homology Amino AcidIntronReceptor Protein-Tyrosine KinasesGeneral MedicineDNAbiology.organism_classificationIntronsPoriferaSpongeMultigene Familybiology.proteinSequence AlignmentGene
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Lactaturia and loss of sodium-dependent lactate uptake in the colon of SLC5A8-deficient mice.

2008

SLC5A8 is a member of the sodium/glucose cotransporter family. It has been proposed that SLC5A8 might act as an apical iodide transporter in the thyroid follicular cells or as a transporter of short chain monocarboxylates. We have directly addressed the functional role of SLC5A8 in vivo by generation of SLC5A8 mutant mice. We found that SLC5A8 is responsible for the re-absorption of lactate at the apical membrane of the kidney proximal tubules and of serous salivary gland ducts. In addition, SLC5A8 mediated the uptake of lactate into colonocytes under physiological conditions. We did not find any evidence of SLC5A8 being essential for the apical iodide transport in the thyroid gland, even i…

Monocarboxylic Acid Transportersmedicine.medical_specialtyColonButyrateBiologyBiochemistryIntestinal absorptionMiceInternal medicinemedicineAnimalsIodide transportLactic AcidMolecular BiologyCation Transport ProteinsMice KnockoutThyroidSodiumTransporterCell BiologyNeoplasms ExperimentalApical membraneTransport proteinButyratesMembrane Transport Structure Function and BiogenesisEndocrinologymedicine.anatomical_structureCell Transformation NeoplasticIntestinal AbsorptionCarcinogensKidney DiseasesCotransporterThe Journal of biological chemistry
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