1998
The Antiproliferative Agent Didemnin B Uncompetitively Inhibits Palmitoyl Protein Thioesterase †
Meng L, Sin N, Crews C. The Antiproliferative Agent Didemnin B Uncompetitively Inhibits Palmitoyl Protein Thioesterase †. Biochemistry 1998, 37: 10488-10492. PMID: 9671519, DOI: 10.1021/bi9804479.Peer-Reviewed Original ResearchConceptsPalmitoyl-protein thioesterase 1GTP-binding proteinsDynamic protein palmitoylationDidemnin BPalmitoyl-protein thioesterasePalmitoyl proteinsProtein palmitoylationMembrane associationBaculoviral systemMyristoyl-CoAProduct bindsHa-rasBiochemical supportProteinEnzymatic activityBindingInhibition assaysDepalmitoylationPalmitoylationThioesteraseKinetic analysisInhibitionBindsRegulationUncompetitive mode
1996
Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis.
Crews C, Lane W, Schreiber S. Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 4316-4319. PMID: 8633062, PMCID: PMC39533, DOI: 10.1073/pnas.93.9.4316.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCattleConsensus SequenceDepsipeptidesDNA PrimersGTP-Binding ProteinsHumansInfantMolecular Sequence DataMolecular WeightNeuronal Ceroid-LipofuscinosesPeptides, CyclicPolymerase Chain ReactionProtein BindingRatsSequence Homology, Amino AcidThiolester HydrolasesConceptsPalmitoyl-protein thioesteraseInfantile neuronal ceroid lipofuscinosisNeuronal ceroid lipofuscinosisGTP-dependent bindingProgressive loss of brain functionDidemnin BG alpha s subunitProtein synthesis inhibitory activityProteins in vitroCeroid lipofuscinosisSequence similarityPalmitoyl thioesteraseProtein thioesteraseHuman cDNAEF1-alphaS subunitsBrain lysatesH-rasThioesteraseProteinBiological activityLipofuscinosisCDNADidemninInhibitory activity