2021
BET proteolysis targeted chimera-based therapy of novel models of Richter Transformation-diffuse large B-cell lymphoma
Fiskus W, Mill CP, Perera D, Birdwell C, Deng Q, Yang H, Lara BH, Jain N, Burger J, Ferrajoli A, Davis JA, Saenz DT, Jin W, Coarfa C, Crews CM, Green MR, Khoury JD, Bhalla KN. BET proteolysis targeted chimera-based therapy of novel models of Richter Transformation-diffuse large B-cell lymphoma. Leukemia 2021, 35: 2621-2634. PMID: 33654205, PMCID: PMC8410602, DOI: 10.1038/s41375-021-01181-w.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAnimalsAntineoplastic Combined Chemotherapy ProtocolsApoptosisBiomarkers, TumorBridged Bicyclo Compounds, HeterocyclicCell ProliferationCell Transformation, NeoplasticGene Expression Regulation, NeoplasticHumansLymphoma, Large B-Cell, DiffuseMicePiperidinesProteinsProteolysisSulfonamidesTumor Cells, CulturedXenograft Model Antitumor AssaysConceptsLarge B-cell lymphomaB-cell lymphomaRichter transformationBET protein inhibitorLymphoma burdenImproved survivalCombination therapyC-Myc levelsEffective therapyNovel therapiesCell lymphomaXenograft modelProtein inhibitorTherapyBET inhibitorsProtein expressionCLLGenetic alterationsLymphomaInhibitorsIRF4Single-cell RNA-seqHuman modelCRISPR knockoutCells
2001
Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival
Princiotta M, Schubert U, Chen W, Bennink J, Myung J, Crews C, Yewdell J. Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 513-518. PMID: 11149939, PMCID: PMC14618, DOI: 10.1073/pnas.98.2.513.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAminopeptidasesAnimalsAntigen PresentationAntigensBoronic AcidsBortezomibCD8-Positive T-LymphocytesCell SurvivalCysteine EndopeptidasesDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDrug ResistanceEndopeptidasesEnzyme ActivationH-2 AntigensLeupeptinsLymphoma, T-CellMiceMultienzyme ComplexesNeoplasm ProteinsOligopeptidesPeptide FragmentsPhenolsProtease InhibitorsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalPyrazinesSelection, GeneticSerine EndopeptidasesSulfonesThymus NeoplasmsTumor Cells, CulturedTumor Suppressor Protein p53TyramineUbiquitinsConceptsII activityLarge proteolytic complexSpecific proteasome inhibitorInhibitor 4Degradation of p53Ala-AlaProteolytic complexPolyubiquitinated proteinsLeu-LeuProteolytic functionActive proteasomesPrimary proteaseProperties of cellsProteolytic systemProteasomeSpecific inhibitorMajor histocompatibility complexPhe-chloromethylketoneProteasome inhibitors
2000
The Selective Proteasome Inhibitors Lactacystin and Epoxomicin Can Be Used to Either Up- or Down-Regulate Antigen Presentation at Nontoxic Doses
Schwarz K, de Giuli R, Schmidtke G, Kostka S, van den Broek M, Kim K, Crews C, Kraft R, Groettrup M. The Selective Proteasome Inhibitors Lactacystin and Epoxomicin Can Be Used to Either Up- or Down-Regulate Antigen Presentation at Nontoxic Doses. The Journal Of Immunology 2000, 164: 6147-6157. PMID: 10843664, PMCID: PMC2507740, DOI: 10.4049/jimmunol.164.12.6147.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAmino Acid SequenceAnimalsAntigen PresentationAntigens, ViralApoptosisCell DivisionCell LineCysteine EndopeptidasesCysteine Proteinase InhibitorsDose-Response Relationship, ImmunologicDown-RegulationGlycoproteinsHumansHybridomasHydrolysisLymphocyte ActivationLymphocytic choriomeningitis virusMiceMice, Inbred BALB CMice, Inbred C57BLMolecular Sequence DataMultienzyme ComplexesNucleoproteinsOligopeptidesPeptide FragmentsProteasome Endopeptidase ComplexT-Lymphocytes, CytotoxicTumor Cells, CulturedUbiquitinsUp-RegulationViral ProteinsConceptsAg presentationProteasome inhibitor lactacystinCellular proliferationProteasome activitySelective inhibitionMHC class IDose-dependent mannerTransplant rejectionAutoimmune diseasesMouse CMVAntigen presentationMost MHC class INontoxic dosesChymotrypsin-like activityClass ISelective proteasome inhibitor lactacystinApoptosis inductionMicroM lactacystinViral proteinsPresentationInhibitionComplete inhibitionLactacystinVivoProliferation
1999
Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
Meng L, Mohan R, Kwok B, Elofsson M, Sin N, Crews C. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10403-10408. PMID: 10468620, PMCID: PMC17900, DOI: 10.1073/pnas.96.18.10403.Peer-Reviewed Original ResearchAnimalsAnti-Inflammatory Agents, Non-SteroidalAntibiotics, AntineoplasticCattleCells, CulturedCysteine EndopeptidasesCysteine Proteinase InhibitorsEndothelium, VascularErythrocytesHeLa CellsHumansKineticsMultienzyme ComplexesOligopeptidesProteasome Endopeptidase ComplexTumor Cells, CulturedTumor Suppressor Protein p53UbiquitinsUmbilical VeinsTotal synthesis of the-potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology
Sin N, Kim K, Elofsson M, Meng L, Auth H, Kwok B, Crews C. Total synthesis of the-potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorganic & Medicinal Chemistry Letters 1999, 9: 2283-2288. PMID: 10465562, DOI: 10.1016/s0960-894x(99)00376-5.Peer-Reviewed Original Research