Featured Publications
BTG1 mutation yields supercompetitive B cells primed for malignant transformation
Mlynarczyk C, Teater M, Pae J, Chin C, Wang L, Arulraj T, Barisic D, Papin A, Hoehn K, Kots E, Ersching J, Bandyopadhyay A, Barin E, Poh H, Evans C, Chadburn A, Chen Z, Shen H, Isles H, Pelzer B, Tsialta I, Doane A, Geng H, Rehman M, Melnick J, Morgan W, Nguyen D, Elemento O, Kharas M, Jaffrey S, Scott D, Khelashvili G, Meyer-Hermann M, Victora G, Melnick A. BTG1 mutation yields supercompetitive B cells primed for malignant transformation. Science 2023, 379: eabj7412. PMID: 36656933, PMCID: PMC10515739, DOI: 10.1126/science.abj7412.Peer-Reviewed Original ResearchConceptsGerminal center B cellsPositive selection signalsB-cell fitnessCell fitnessUnicellular organismsB cellsMulticellular lifeNatural selectionSelection signalsInduction kineticsGatekeeper mechanismAdaptive immune systemAltruistic cooperationNew mouse modelNormal counterpartsHuman lymphomasAntibody affinity maturationCellsInvasive lymphomaClinical outcomesMouse modelImmune systemMalignant transformationSupercompetitorsAffinity maturation
2022
Conformational transitions in BTG1 antiproliferative protein and their modulation by disease mutants
Kots E, Mlynarczyk C, Melnick A, Khelashvili G. Conformational transitions in BTG1 antiproliferative protein and their modulation by disease mutants. Biophysical Journal 2022, 121: 3753-3764. PMID: 35459639, PMCID: PMC9617077, DOI: 10.1016/j.bpj.2022.04.023.Peer-Reviewed Original ResearchConceptsB-cell translocation gene 1Antiproliferative proteinAssociate with transcriptional cofactorsFamily of antiproliferative proteinsWild-typeFunctional interactionsDisease-linked mutationsSomatic missense mutationsCell cycle progressionMarkov state model analysisConformational transitionBinding partnersTranscriptional cofactorCellular partnersCellular processesProtein regionsDisease mutantsMissense mutationsCycle progressionBinding hotspotsBinding proteinFunctional associationEnsemble of conformationsMolecular mechanismsA2-A4
2010
Endoplasmic Reticulum Stress Induces G2 Cell-Cycle Arrest via mRNA Translation of the p53 Isoform p53/47
Bourougaa K, Naski N, Boularan C, Mlynarczyk C, Candeias M, Marullo S, Fåhraeus R. Endoplasmic Reticulum Stress Induces G2 Cell-Cycle Arrest via mRNA Translation of the p53 Isoform p53/47. Molecular Cell 2010, 38: 78-88. PMID: 20385091, DOI: 10.1016/j.molcel.2010.01.041.Peer-Reviewed Original ResearchConceptsMRNA translationOutcome of p53 activationTrans-activation domainP53 downstream pathwaysMDM2 binding siteG2 cell cycle arrestCell cycle arrestEndoplasmic reticulum stressP53 isoformsP53/47P53 activationHomo-oligomerizationP53 pathwayG1 progressionTrans-activationCellular stressDNA repairG1 arrestBiochemical propertiesG2 arrestReticulum stressResponse to different typesDownstream pathwaysAmino acidsP53