Search results for "TYR"

showing 10 items of 2017 documents

Conformational clamping by a membrane ligand activates the EphA2 receptor

2021

AbstractThe EphA2 receptor is a promising drug target for cancer treatment, since EphA2 activation can inhibit metastasis and tumor progression. It has been recently described that the TYPE7 peptide activates EphA2 using a novel mechanism that involves binding to the single transmembrane domain of the receptor. TYPE7 is a conditional transmembrane (TM) ligand, which only inserts into membranes at neutral pH in the presence of the TM region of EphA2. However, how membrane interactions can activate EphA2 is not known. We systematically altered the sequence of TYPE7 to identify the binding motif used to activate EphA2. With the resulting six peptides, we performed biophysical and cell migratio…

Protein ConformationSequence HomologyTm ligandsPeptideMolecular Dynamics SimulationLigandsReceptor tyrosine kinaseArticleBimolecular fluorescence complementationProtein DomainsStructural BiologyCell MovementCell surface receptorTumor Cells CulturedHumansAmino Acid SequenceReceptorMolecular BiologyMelanomachemistry.chemical_classificationBinding SitesMembranesbiologyChemistryReceptor EphA2Membrane ProteinsLigand (biochemistry)Peptide FragmentsTransmembrane proteinTransmembrane domainMembranebiology.proteinBiophysicsProtein MultimerizationProtein Binding
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Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

2011

The vanadium haloperoxidase (V-HPO) enzyme, extracted from the brown alga Laminaria saccharina, is able to catalyze the formation of a black precipitate, using as precursor the amino acid L-dopa in the presence of hydrogen peroxide and iodide, in one-pot synthesis. The L-dopa oxidation is a multistep reaction with a crucial role played by the iodide in the enzyme catalyzed peroxidative production of dopachrome, a well known intermediate in the synthesis of melanin. Dopachrome is then converted to a synthetic form of melanin through a polymerization reaction. Factors, such as buffer composition and pH, influence significantly the reaction first steps, but further steps of melanin production …

Protein ConformationTyrosinaseIodideBuffersBiochemistryPolymerizationLevodopaInorganic ChemistryMelaninchemistry.chemical_compoundHaloperoxidaseOrganic chemistryIndolequinonesHydrogen peroxideMelaninschemistry.chemical_classificationChemistryVanadiumHydrogen PeroxideHydrogen-Ion ConcentrationIodidesKineticsPeroxidasesPolymerizationBiocatalysisBiocatalysisMicroscopy Electron ScanningDopachromeJournal of Inorganic Biochemistry
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The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One

2017

Show your metal: l-Tyrosine is converted into the protective antioxidative polymer melanin in a sequence of reactions. In humans, the catalytic pathway starts with the tyrosinase HsTYR and two tyrosinase-related proteins HsTYRP1 and HsTYRP2. All three enzymes have the same active site but the latter two contain two zinc ions instead of copper ions.

Protein ConformationTyrosinasechemistry.chemical_elementNanotechnologyZincCrystallography X-Ray010402 general chemistry01 natural sciencesAntioxidantsCatalysisMelaninProtein structureCatalytic DomainHumansTYRP1MelanosomeMelaninschemistry.chemical_classificationMembrane Glycoproteinsbiology010405 organic chemistryActive siteGeneral ChemistryCombinatorial chemistry0104 chemical sciencesZincEnzymechemistrybiology.proteinTyrosineOxidoreductasesCopperAngewandte Chemie International Edition
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Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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Conversion of crustacean hemocyanin to catecholoxidase

2004

Crustacean hemocyanin as oxygen carrier and catecholoxidase as enzymes belong to the same protein family (type 3 copper proteins) sharing very similar active sites. Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess the ability of catecholoxidase activity.

Protein familyCopper proteinTyrosinasemedicine.medical_treatmentGeneral Physics and Astronomychemistry.chemical_elementchemical and pharmacologic phenomenacomplex mixturesOxygenStructural BiologyCrustaceamedicineAnimalsGeneral Materials ScienceCatechol oxidasechemistry.chemical_classificationbiologyActive sitehemic and immune systemsHemocyaninCell BiologyEnzymechemistryBiochemistryHemocyaninsbiology.proteinCatechol OxidaseMicron
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Inhibition of intrinsic protein tyrosine kinase activity of EGF-receptor kinase complex from human breast cancer cells by the marine sponge metabolit…

1990

1. (+)-Aeroplysinin-1, a naturally occurring tyrosine metabolite from the marine sponge Verongia aerophoba, was found to inhibit the phosphorylation of lipocortin-like proteins by a highly purified preparation of the epidermal growth factor (EGF) receptor-tyrosine protein kinase complex from MCF-7 breast carcinoma cells. 2. (+)-Aeroplysinin-1 blocked the EGF-dependent proliferation of both MCF-7 and ZR-75-1 human breast cancer cells and inhibited the ligand-induced endocytosis of the EGF receptor in vitro. 3. Treatment with aeroplysinin-1 in the concentration range at 0.25-0.5 microM resulted in a time- and dose-dependent total tumor cell death in vitro. 4. At a 10-fold higher concentration…

Protein kinase complexAcetonitrilesTime FactorsPhysiologyBlotting WesternBreast NeoplasmsBiologyBiochemistrySubstrate SpecificityMiceEpidermal growth factorCyclohexenesTumor Cells CulturedAnimalsHumansPhosphorylationTyrosineMolecular BiologyDose-Response Relationship DrugKinaseGeneral MedicineProtein-Tyrosine KinasesMolecular biologyPoriferaErbB ReceptorsBiochemistryCell cultureCancer cellPhosphorylationCalciumTyrosine kinaseCell DivisionComparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Direct evidence that FK506 inhibition of FcεRI-mediated exocytosis from RBL mast cells involves calcineurin

1998

eRI-mediated exocytosis of preformed mediators from mast cells and basophils (e.g. histamine, serotonin, beta-hexosaminidase) is sensitive to the immunosuppressants cyclosporin A and FK506 (IC 50 200 and 4 n M , respectively) but not rapamycin. The mechanism of inhibition does not appear to involve tyrosine phosphorylation, hydrolysis of inositol phosphates or calcium flux. Here we report experiments using a molecular approach to assess the role of calcineurin, a serine/threonine phosphatase thought to be the primary pharmacological target of these drugs. Calcineurin’s activity requires association of its catalytic (A) subunit with an intrinsic regulatory (B) subunit. We hypothesized that c…

Protein subunitDermatologyBiologyTransfectionSensitivity and SpecificityCell DegranulationExocytosisTacrolimusExocytosischemistry.chemical_compoundCyclosporin aCalcium fluxTumor Cells CulturedmedicineAnimalsMast CellsDose-Response Relationship DrugReceptors IgECalcineurinTyrosine phosphorylationGeneral MedicineMast cellRatsCell biologyCalcineurinElectroporationmedicine.anatomical_structureLeukemia Basophilic AcutechemistryBiochemistryImmunosuppressive AgentsHistamineArchives of Dermatological Research
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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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Investigation of cancer drug resistance mechanisms by phosphoproteomics

2020

Abstract Cancer cell mutations can be identified by genomic and transcriptomic techniques. However, they are not sufficient to understand the full complexity of cancer heterogeneity. Analyses of proteins expressed in cancers and their modification profiles show how these mutations could be translated at the functional level. Protein phosphorylation is a major post-translational modification critical for regulating several cellular functions. The covalent addition of phosphate groups to serine, threonine, and tyrosine is catalyzed by protein kinases. Over the past years, kinases were strongly associated with cancer, thus inhibition of protein kinases emanated as novel cancer treatment. Howev…

Proteomics0301 basic medicineProteomeAntineoplastic AgentsBiologyProteomics03 medical and health sciences0302 clinical medicineNeoplasmsBiomarkers TumormedicineAnimalsHumansProtein phosphorylationPhosphorylationProtein Kinase InhibitorsPharmacologyKinasePhosphoproteomicsCancermedicine.diseaseNeoplasm Proteins030104 developmental biologyDrug Resistance Neoplasm030220 oncology & carcinogenesisCancer cellCancer researchPhosphorylationProtein Processing Post-TranslationalTyrosine kinasePharmacological Research
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