Featured Publications
Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
Unbehaun A, Marintchev A, Lomakin IB, Didenko T, Wagner G, Hellen C, Pestova TV. Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing. The EMBO Journal 2007, 26: 3109-3123. PMID: 17568775, PMCID: PMC1914099, DOI: 10.1038/sj.emboj.7601751.Peer-Reviewed Original ResearchDendritic BC1 RNA: Functional Role in Regulation of Translation Initiation
Wang H, Iacoangeli A, Popp S, Muslimov IA, Imataka H, Sonenberg N, Lomakin IB, Tiedge H. Dendritic BC1 RNA: Functional Role in Regulation of Translation Initiation. Journal Of Neuroscience 2002, 22: 10232-10241. PMID: 12451124, PMCID: PMC1828542, DOI: 10.1523/jneurosci.22-23-10232.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrain ChemistryCell-Free SystemCells, CulturedDendritesElectrophoretic Mobility Shift AssayEukaryotic Initiation Factor-4AEukaryotic Initiation FactorsGene Expression RegulationMacromolecular SubstancesNeuronal PlasticityNeuronsPeptide Chain Initiation, TranslationalPoly(A)-Binding ProteinsProtein BiosynthesisRatsRats, Sprague-DawleyRepressor ProteinsRibosomesRNA, MessengerRNA, Small CytoplasmicConceptsLocal protein synthesisBC1 RNATranslation initiationInternal ribosome entry mechanismCap-dependent translation initiationProtein synthesisFunctional roleMessenger RNASmall ribosomal subunitTranslational control mechanismsLevel of initiationDendritic BC1 RNAPlasticity of synapsesRepression pathwaySpecific repressorPreinitiation complexTranslational controlInitiation factorsRibosomal subunitBiochemical experimentsLocal translationInternal initiationRNAEntry mechanismDensity gradient centrifugationCrystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation
Lomakin IB, Dmitriev SE, Steitz TA. Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 116: 528-533. PMID: 30584092, PMCID: PMC6329987, DOI: 10.1073/pnas.1809688116.Peer-Reviewed Original ResearchMeSH KeywordsCell Cycle ProteinsEukaryotic Initiation FactorsHumansOncogene ProteinsProtein MultimerizationProtein Structure, QuaternaryConceptsTranslation initiationHeterodimer formationUnconventional translation initiationNoncanonical translation initiationZinc-binding siteMechanism of regulationUpstream reading framesIon-binding sitesRibosome recyclingReading frameTerminal domainTranslation reinitiationCysteine residuesAtomic detailHeterodimersMCT-1Crystal structureSpecific setReinitiationRibosomesProteinCysteineMRNAResiduesSites
2017
Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1
Lomakin IB, Stolboushkina EA, Vaidya AT, Zhao C, Garber MB, Dmitriev SE, Steitz TA. Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1. Cell Reports 2017, 20: 521-528. PMID: 28723557, PMCID: PMC5551485, DOI: 10.1016/j.celrep.2017.06.025.Peer-Reviewed Original ResearchMeSH KeywordsCell Cycle ProteinsCrystallography, X-RayEukaryotic Initiation FactorsHumansOncogene ProteinsProtein Structure, QuaternaryRibosomesConceptsSmall ribosomal subunitTranslation initiationRibosomal subunitUnconventional translation initiationInitiation factor 1Cancer-related mRNAsTranslational controlHuman ribosomeTerminal domainReinitiation stepsRibosomesDimer interactsFunctional implicationsFactor 1SubunitsCrystal structureStriking similaritySpecific setComplexesHeterodimersProteinOncoproteinInitiationInteractsMRNA