Search results for "Protein-Arginine N-Methyltransferases"

showing 4 items of 4 documents

Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1

2017

Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds co…

Models Molecular0301 basic medicineProtein-Arginine N-MethyltransferasesAdenosineMethyltransferaseCARM1ArgininePRMTCrystallography X-RayPoly(A)-Binding Protein ICofactorMice03 medical and health sciences0302 clinical medicineCatalytic DomainCoactivatorAnimalsAmino Acid Sequencetransition state mimicschemistry.chemical_classificationBinding SitesMultidisciplinarybiologycocrystal structuresActive siteProtein arginine N-methyltransferase; PRMT; CARM1; Transition state mimics; Cocrystal structuresMethylationBiological Sciencesprotein arginine N-methyltransferase030104 developmental biologyEnzymeCARM1chemistryBiochemistry030220 oncology & carcinogenesisbiology.proteinPeptidesProtein Binding
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A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on

2019

Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some α- and β-tubulin genes have been identified in P. lividus, while no data are available in echinoderms for arginine methyl transferases (PRMT). To evaluate the exploiting of the sea urchin embryo in the field o…

Protein-Arginine N-MethyltransferasesEmbryo NonmammalianPRMTechinodermsIntracellular Signaling Peptides and Proteinsmacromolecular substancesCytostatic AgentsMethylationTubulin ModulatorsArticlearginine methylationsea urchintubulinpost-translational modificationSea Urchinsembryonic structuresToxicity TestsAnimalsProtein Processing Post-TranslationalInternational journal of molecular sciences
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A TR-FRET based functional assay for screening activators of CARM1

2013

Epigenome is an emerging field that demands selective cell-permeable chemical probes to perturb, especially in vivo, the activity of specific enzymes involved in modulating the epigenetic codes. Coactivator Associated Arginine (R) Methyltransferase 1 (CARM1) is a coactivator of estrogen receptor α (ERα), the main target in human breast cancer. We previously showed that overexpression of CARM1 by two-fold in MCF7 breast cancer cells increased the expression of ERα-target genes involved in differentiation and reduced cell proliferation, leading to the hypothesis that activating CARM1 by chemical activators may be therapeutically effective in breast cancer. Selective, potent, cell-permeable CA…

Protein-Arginine N-MethyltransferasesTime FactorsCARM1CARM1; arginine; FRET; methylation; PABP1High-throughput screeningEstrogen receptorarginineBacMamBreast NeoplasmsBiologyBiochemistryArticleEnzyme activatorCoactivatorFluorescence Resonance Energy TransferHumansEpigeneticsPABP1Molecular BiologyOrganic ChemistryFusion proteinEnzyme ActivationCARM1BiochemistryFRETMCF-7 CellsMolecular MedicineFemalemethylation
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Estradiol, acting through estrogen receptor alpha, restores dimethylarginine dimethylaminohydrolase activity and nitric oxide production in oxLDL-tre…

2011

Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide (NO) synthase. ADMA accumulation, mainly due to a decreased dimethylarginine dimethylaminohydrolase (DDAH) activity, has been related to the development of cardiovascular diseases. We investigate whether estradiol prevents the changes induced by oxidized low density lipoprotein (oxLDL) on the DDAH/ADMA/NO pathway in human umbilical artery endothelial cells (HUAEC). HUAEC were exposed to estradiol, native LDL (nLDL), oxLDL and their combinations for 24 h. In some experiments, cells were also exposed to the unspecific estrogen receptor (ER) antagonist ICI 182780, the specific ERα antagonist MPP or specific agonists …

medicine.medical_specialtyProtein-Arginine N-MethyltransferasesEndotheliumNitric Oxide Synthase Type IIImedicine.drug_classBlotting WesternArginineNitric OxideBiochemistryUmbilical ArteriesNitric oxideAmidohydrolasesReceptors G-Protein-Coupledchemistry.chemical_compoundEndocrinologyEnosInternal medicinemedicineEstrogen Receptor betaHumansEstrogens Non-SteroidalMolecular BiologyCells CulturedbiologyEstradiolArtèriesProtein StabilityEstrogen AntagonistsEstrogen Receptor alphaEndoteli vascularbiology.organism_classificationNitric oxide synthaseIsoenzymesLipoproteins LDLRepressor Proteinsmedicine.anatomical_structureEndocrinologychemistryReceptors EstrogenEstrogenbiology.proteinlipids (amino acids peptides and proteins)Endothelium VascularAsymmetric dimethylarginineEstrogen receptor alphaGPER
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