grant

Proteomics Core

Organization MEDICAL UNIVERSITY OF SOUTH CAROLINALocation CHARLESTON, UNITED STATESPosted 1 Aug 2021Deadline 31 Jul 2026
NIHUS FederalResearch GrantFY20252-oxo-propanalAPF-1ATP-Dependent Proteolysis Factor 1AcetylationAcetylformaldehydeAddressAdvanced DevelopmentAgreementApplications GrantsArginineAwardBioinformaticsBiological MarkersBiologyBody TissuesCCSGCOBRECancer Center Support GrantCell BodyCell Communication and SignalingCell SignalingCellsCenter of Biomedical Research ExcellenceCenters of Research ExcellenceComplementComplement ProteinsComputer softwareConsultConsultationsCysteineData AnalysesData AnalysisDedicationsDetectionDevelopmentDiseaseDisease ProgressionDisorderDissociationDrug resistanceEducationEducational aspectsElectron TransportEnsureEnzyme GeneEnzymesEquilibriumEvaluationExperimental DesignsFacultyFreezingGoalsGrantGrant ProposalsHMG-20Half-CystineHigh Mobility Protein 20Human ResourcesInfrastructureInstitutionIntracellular Communication and SignalingInvestigatorsInvestmentsL-ArginineL-CysteineL-LysineL-ProlineL-SerineL-ThreonineLysineMALD-MSMALDIMALDI-MSManpowerMass Photometry/Spectrum AnalysisMass SpectrometryMass SpectroscopyMass SpectrumMass Spectrum AnalysesMass Spectrum AnalysisMetabolic GlycosylationMethodologyMethylglyoxalModificationNIGMSNational Institute of General Medical SciencesNational Institutes of HealthOxidantsOxidation-ReductionOxidizing AgentsPeptide FragmentsPeptidesPhasePhosphorylationPositionPositioning AttributePost-Translational Modification Protein/Amino Acid BiochemistryPost-Translational Modification SitePost-Translational ModificationsPost-Translational Protein ModificationPost-Translational Protein ProcessingPosttranslational Modification SitePosttranslational ModificationsPosttranslational Protein ProcessingPreparationProlineProtein ModificationProtein PhosphorylationProteinsProteomicsPyruvaldehydePyruvic AldehydeRedoxReproducibilityResearchResearch PersonnelResearch ResourcesResearchersResolutionResourcesSamplingSerineServicesSignal TransductionSignal Transduction SystemsSignalingSiteSlideSoftwareSouth CarolinaSpatial DistributionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpectroscopy, Mass, Matrix-Assisted Laser Desorption-IonizationStressSulfonic AcidsSystemTechnologyThreonineTissue imagingTissuesTrainingTreatment EfficacyTyrosineUbiquitinUnited States National Institutes of HealthUpdatebalancebalance functionbasebasesbio-markersbiologic markerbiological signal transductionbiomarkercomplementationcomputerized data processingconsultationconsultscostcrosslinkdata acquisitiondata acquisitionsdata interpretationdata processingdevelopmentaldisulfide bonddrug resistantelectron acceptorelectron transferexperienceexperimentexperimental researchexperimental studyexperimentsglycationglycosylationimaging capabilitiesimaging mass spectrometryimprovedin vivoinstrumentinstrumentationintervention efficacymass spectrometric imagingmatrix assisted laser desorption ionizationnanonew technologynon-enzymatic glycosylationnonenzymatic glycosylationnovelnovel technologiesoxidationoxidation reduction reactionpersonnelpreparationsprogramsprotein expressionresistance to Drugresistance to therapyresistant to Drugresistant to therapyresolutionsresponsesuccesstherapeutic efficacytherapeutic resistancetherapy efficacytherapy resistanttranslational studytreatment resistance
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Full Description

Proteomics Core – Project Summary
The broad objective of the Proteomics Core in the SC COBRE in Oxidants, Redox Balance, and Stress Signaling

(Redox COBRE) is to provide state-of-the-art, mass spectrometry (MS)-based proteomic capabilities to enable

elucidation of redox signaling mechanisms underlying disease, therapeutic efficacy of cells and drugs, and

therapeutic resistance. The Core provides expertise, technical assistance, instrumentation, and interpretation of

analytical results for quantitative proteomic experiments and the characterization of redox-sensitive post-

translational modifications. During Phase I and II, acquisition of the Orbitrap Elite ETD MS and Orbitrap Fusion

Lumos ETD/UVPD MS nano-LC-MS/MS systems (NIH S10 OD010731 and S10 OD025126, PI: Lauren Ball)

permitted detection of challenging modifications using complementary peptide fragmentation approaches (ETD

and EThcD) and the development of advanced, quantitative proteomic workflows as needed by COBRE

investigators. During Phase III, the Core will further develop and update these capabilities to reflect rapid

advances in instrumentation, software, and methodologies relevant to redox proteomics. Additionally, in

response to the needs of COBRE-affiliated investigators, proteomic tissue imaging capabilities using MALDI-

Imaging MS (IMS) will be provided to discern the spatial distribution of enzymatically-digested peptides within

tissue biospecimens on slides for the discovery of putative biomarkers and mechanisms underlying disease

progression. Detection of disease-specific proteins and redox-sensitive post-translational modifications by LC-

MS/MS and IMS has raised the need for targeted proteomic capabilities to verify these findings and further

advance translational studies. Providing this complement of proteomic technologies will build on the successes

of the Core and position the Core to establish a comprehensive, independent resource. The Core has leveraged

previous investments made by the NIGMS during Phase I and II of the COBRE program, the OD and NIGMS for

Shared Instrumentation Grants, the NCI Cancer Center Support Grant, and long-standing, strong institutional

commitment to develop into a successful institutional resource critical to the needs of Redox COBRE

investigators. At present there are 19 COBRE-affiliated users of the Proteomics Core that are PIs of 15 active

NIH awards that rely on the LC-MS/MS capabilities, five of these awards also depend on IMS capabilities.

Grant Number: 5P30GM140964-05
NIH Institute/Center: NIH

Principal Investigator: Lauren Ball

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