grant

Defining the Biochemical Function and Therapeutic Utility of Unique PARP14 and PARP15 ADP-Ribosylation Sites

Organization SANTA CLARA UNIVERSITYLocation SANTA CLARA, UNITED STATESPosted 1 Aug 2020Deadline 31 Aug 2028
NIHUS FederalResearch GrantFY2025ADP RiboseADP ribosylationAbscissionAdenosine 5'-(trihydrogen diphosphate), P'-5-ester with D-riboseAdenosine 5'-DiphosphoriboseAdenosine Diphosphate RiboseAdenosine DiphosphoriboseAffectAmino AcidsAnti-viral AgentsAnti-viral ResponseAssayBehaviorBinding ProteinsBioassayBiochemicalBiochemical PathwayBiogenesisBiological AssayBiologyCapsidCell BodyCell Communication and SignalingCell FunctionCell PhysiologyCell ProcessCell SignalingCellsCellular FunctionCellular PhysiologyCellular ProcessCellular biologyChemicalsDNA Damage RepairDNA RepairDataDevelopmentDevelopmental BiologyDiseaseDisorderEnzyme GeneEnzymesEventExcisionExhibitsExtirpationFamilyFutureGlycohydrolasesGlycosidasesGlycoside HydrolasesHumanImmune responseImmunityIntracellular Communication and SignalingKinasesKnowledgeLibrariesLifeLife CycleLife Cycle StagesLigand Binding ProteinLigand Binding Protein GeneLinkLocationMapsMass Photometry/Spectrum AnalysisMass SpectrometryMass SpectroscopyMass SpectrumMass Spectrum AnalysesMass Spectrum AnalysisMedicineMetabolic NetworksMethodsModelingModern ManModificationN-substituted GlycinesNon-Polyadenylated RNAOrigin of LifePARP PolymerasePARP proteinPARSPathway interactionsPeptide SynthesisPeptidesPeptoidsPhosphotransferase GenePhosphotransferasesPhysiologicPhysiologicalPlayPoly(ADP-ribose) PolymerasesPoly(ADPribose) PolymerasePost-Translational Modification Protein/Amino Acid BiochemistryPost-Translational ModificationsPost-Translational Protein ModificationPost-Translational Protein ProcessingPosttranslational ModificationsPosttranslational Protein ProcessingProtein BindingProtein ModificationProteinsProteomeProteomicsRNARNA Gene ProductsRegulationRemovalResearchRibonucleic AcidRoleSeriesSignal TransductionSignal Transduction SystemsSignalingSiteSpecificityStructure-Activity RelationshipSubcellular ProcessSurgical RemovalTechniquesTherapeuticTherapeutic InterventionTransphosphorylasesUnscheduled DNA SynthesisVariantVariationViralViral ActivityViral DiseasesViral FunctionViral PhysiologyVirus DiseasesVirus ReplicationWorkaminoacidanti-viral compoundanti-viral drugsanti-viral medicationanti-viral therapeuticanti-viralsbiological signal transductionbound proteincancer progressioncell biologychemical structure functiondesigndesigningdevelopmentalexperiencehost responseimmune system responseimmunoresponseinhibitorinsightinterdisciplinary approachintervention therapylife coursemimeticsmultidisciplinary approachneoplasm progressionneoplastic progressionnew drug treatmentsnew drugsnew pharmacological therapeuticnew therapeutic approachnew therapeutic interventionnew therapeutic strategiesnew therapeuticsnew therapynew therapy approachesnew treatment approachnew treatment strategynext generation therapeuticsnovelnovel drug treatmentsnovel drugsnovel pharmaco-therapeuticnovel pharmacological therapeuticnovel therapeutic approachnovel therapeutic interventionnovel therapeutic strategiesnovel therapeuticsnovel therapynovel therapy approachpathwaypeptide aminoacid sequencepeptide mimeticpeptide mimicpeptide sequencepeptidomimeticspoly ADP polymerasepoly ADP ribose synthetasepreferenceprotein aminoacid sequenceresectionside effectsocial rolestructure function relationshiptherapeutic targettumor progressionviral infectionviral multiplicationviral replicationvirus infectionvirus multiplicationvirus-induced disease
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SUMMARY
ADP-ribosylation was one of the first post-translational modifications (PTMs) discovered. It is a widespread and

ubiquitous post-translational modification across all kingdoms of life – whose biochemical selectivity, cellular

consequences, and final fates remain poorly understood. Our objective is to investigate the entire life-cycle of…

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Defining the Biochemical Function and Therapeutic Utility of Unique PARP14 and PARP15 ADP-Ribosylation Sites — SANTA CLA | Dev Procure