Search results for "PRMT"

showing 3 items of 3 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 survey on tubulin and arginine methyltransferase families sheds light on p. lividus embryo as model system for antiproliferative drug development

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 &alpha

Sea urchinPRMTSettore BIO/11 - Biologia MolecolareDrug actionmacromolecular substancesBiologyCatalysisCatalysilcsh:ChemistryInorganic ChemistryMicrotubuleArginine methylationTubulinbiology.animalGene familyPhysical and Theoretical ChemistrySea urchinlcsh:QH301-705.5Molecular BiologySpectroscopyEchinodermechinodermsOrganic ChemistryEmbryoComputer Science Applications1707 Computer Vision and Pattern RecognitionGeneral MedicineMethylationComputer Science ApplicationsCell biologyTubulinDrug developmentlcsh:Biology (General)lcsh:QD1-999embryonic structuresbiology.proteinPost-translational modification
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