DESCRIPTION (provided by applicant): Most cellular processes are regulated by reversible protein phosphorylation, which is controlled by protein kinases and phosphatases. Caldera Pharmaceuticals and MedChem Partners propose to develop new probes for characterizing transient protein complexes. MAPK pathways play important roles in cellular differentiation and survival. MAPKs are serine/threonine protein kinases that can phoshorylate both cytoplasmic and nuclear targets. MAPKs are associated with aberrant, chronic or hyper-phosphorylation found in cancerous and other diseased tissues. MAPK complexes are difficult to characterize due to the transient nature of kinase-substrate binding interactions.
PUBLIC HEALTH RELEVANCE: Caldera Pharmaceuticals and MedChem Partners propose to develop new probes for characterizing transient protein complexes. MAPK complexes are difficult to characterize due to the transient nature of kinase-substrate binding interactions.
Public Health Relevance Statement
Caldera Pharmaceuticals and MedChem Partners propose to develop new probes for
characterizing transient protein complexes. MAPK complexes are difficult to characterize
due to the transient nature of kinase-substrate binding interactions.
NIH Spending Category
No NIH Spending Category available.
Project Terms
Active SitesBehaviorBindingBinding SitesBiological AssayCalciumCancerousCell physiologyCellsCharacteristicsChemicalsChronicColorComplexCrystallographyCysteineDataEdetic AcidFluorescenceFluorescent ProbesGoalsIncubatedLabelLeftLibrariesLigandsLigationMAP Kinase GeneMAPK1 geneMAPK14 geneMeasurementMeasuresMetalsModificationMolecularNatureNuclearPathway interactionsPeptidesPharmacologic SubstancePhasePhosphoric Monoester HydrolasesPhosphorusPhosphorylationPhosphotransferasesPlayPositioning AttributePropertyProtein IsoformsProtein KinaseProtein Structure InitiativeProtein-Serine-Threonine KinasesProteinsProtocols documentationReadingRelative (related person)ReportingResearch PersonnelRoleSalesSamplingScanningScreening procedureStructureStructure-Activity RelationshipSubstrate SpecificitySulfurSystemTechnologyTerbiumTestingTissuesUnited States National Institutes of HealthWorkbasecofactorcommercializationdesignin vitro testingin vivointerestmemberprolylglycineprotein complexpublic health relevancesuccess
No Sub Projects information available for 1R43GM090387-01
Publications
Publications are associated with projects, but cannot be identified with any particular year of the project or fiscal year of funding. This is due to the continuous and cumulative nature of knowledge generation across the life of a project and the sometimes long and variable publishing timeline. Similarly, for multi-component projects, publications are associated with the parent core project and not with individual sub-projects.
No Publications available for 1R43GM090387-01
Patents
No Patents information available for 1R43GM090387-01
Outcomes
The Project Outcomes shown here are displayed verbatim as submitted by the Principal Investigator (PI) for this award. Any opinions, findings, and conclusions or recommendations expressed are those of the PI and do not necessarily reflect the views of the National Institutes of Health. NIH has not endorsed the content below.
No Outcomes available for 1R43GM090387-01
Clinical Studies
No Clinical Studies information available for 1R43GM090387-01
News and More
Related News Releases
No news release information available for 1R43GM090387-01
History
No Historical information available for 1R43GM090387-01
Similar Projects
No Similar Projects information available for 1R43GM090387-01