2001
The ubiquitin‐proteasome pathway and proteasome inhibitors
Myung J, Kim K, Crews C. The ubiquitin‐proteasome pathway and proteasome inhibitors. Medicinal Research Reviews 2001, 21: 245-273. PMID: 11410931, PMCID: PMC2556558, DOI: 10.1002/med.1009.Peer-Reviewed Original ResearchConceptsUbiquitin-proteasome pathwayComplex biochemical machineryHuman diseasesDiverse cellular processesImportant cellular substratesMajor cellular networksCellular processesBiochemical machineryProtein degradationNatural proteasome inhibitorsCellular substratesCentral playerIntracellular processesMode of actionProteasome inhibitorsPathwayMolecular probesInhibitorsPotential therapeutic agentProteasomeImportant componentMachineryRegulationTherapeutic agents
1994
GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha.
Crews CM, Collins JL, Lane WS, Snapper ML, Schreiber SL. GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha. Journal Of Biological Chemistry 1994, 269: 15411-15414. PMID: 8195179, DOI: 10.1016/s0021-9258(17)40692-2.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnti-Infective AgentsCarrier ProteinsCattleChromatography, AffinityDepsipeptidesGuanosine TriphosphateHumansIndicators and ReagentsKineticsMolecular Sequence DataPeptide Elongation Factor 1Peptide Elongation FactorsPeptides, CyclicProtein Synthesis InhibitorsSequence Homology, Amino AcidConceptsEF-1 alphaPotential antineoplastic drugElongation factor 1 alphaDidemnin BProtein synthesisAntiproliferative activityG1 cell cycle progressionGTP-dependent bindingFactor 1 alphaClinical trialsCell cycle progressionImmunosuppressive activityAntineoplastic drugsPeptide sequence analysisElongation factorMode of actionUndefined mechanismPresence of GTPGTPase activityCycle progressionNanomolar concentrationsSequence analysisAlphaMarine natural productsIntracellular targets
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