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 ResearchRecent insight into intermediate filament structure
Eldirany SA, Lomakin IB, Ho M, Bunick CG. Recent insight into intermediate filament structure. Current Opinion In Cell Biology 2020, 68: 132-143. PMID: 33190098, PMCID: PMC7925366, DOI: 10.1016/j.ceb.2020.10.001.Peer-Reviewed Original ResearchConceptsIntermediate filamentsAssembly mechanismVariable N-terminalMultiple cellular processesCentral rod domainIntermediate filament structureCoil 1BCellular processesStudy of keratinsTail domainFilament assemblyRod domainC-terminalN-terminalElectrostatic surfacePathologic mutationsKey playersFilament structureRecent insightsComplex formationProteinHuman tissuesGlial fibrillary acidic proteinAcidic proteinDomainPhysical Association of Eukaryotic Initiation Factor 4G (eIF4G) with eIF4A Strongly Enhances Binding of eIF4G to the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Is Required for Internal Initiation of Translation
Lomakin I, Hellen C, Pestova T. Physical Association of Eukaryotic Initiation Factor 4G (eIF4G) with eIF4A Strongly Enhances Binding of eIF4G to the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Is Required for Internal Initiation of Translation. Molecular And Cellular Biology 2000, 20: 6019-6029. PMID: 10913184, PMCID: PMC86078, DOI: 10.1128/mcb.20.16.6019-6029.2000.Peer-Reviewed Original ResearchConceptsInternal ribosomal entry siteEMCV internal ribosomal entry siteEIF4GAdditional amino-terminal sequenceEukaryotic initiation factor 4GRNA recognition motifEukaryotic initiation factor 4GIInternal ribosomal entryEntry siteComplex formationBeta-globin mRNAAmino-terminal sequenceEncephalomyocarditis virus internal ribosomal entry siteRibosomal entryRecognition motifLike domainMutational analysisPhysical associationInternal initiationHigh-affinity bindingBinding fragmentSpecific interactionsRNASimilar affinitySpecific high-affinity bindingThe fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH
Lomakin IB, Shirokikh NE, Yusupov MM, Hellen C, Pestova TV. The fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH. The EMBO Journal 2005, 25: 196-210. PMID: 16362046, PMCID: PMC1356347, DOI: 10.1038/sj.emboj.7600904.Peer-Reviewed Original ResearchConceptsInitiator tRNA selectionRibosomal subunitTRNA selectionEukaryotic initiation factors eIF1Common evolutionary originSmall ribosomal subunitInitiation factor eIF1Initiation factor IF3Initiation codon selectionCodon-anticodon mismatchesEIF2-bound GTPRelated conformational changesIF3 functionEvolutionary originSmall ribosomalTranslation initiationInitiation complexInitiation factorsFactor bindingInitiation codonTerminal domainHeterologous systemsCodon selectionInitiator tRNAHeterologous subunits
2020
Structural properties of target binding by profilaggrin A and B domains and other S100 fused-type calcium-binding proteins
Hinbest AJ, Kim SR, Eldirany SA, Lomakin IB, Watson J, Ho M, Bunick CG. Structural properties of target binding by profilaggrin A and B domains and other S100 fused-type calcium-binding proteins. Journal Of Dermatological Science 2020, 100: 39-49. PMID: 32893105, PMCID: PMC7752840, DOI: 10.1016/j.jdermsci.2020.08.009.Peer-Reviewed Original ResearchAmino Acid SequenceAnnexin A2Binding SitesCrystallography, X-RayFilaggrin ProteinsHumansHydrophobic and Hydrophilic InteractionsIntermediate Filament ProteinsIntermediate FilamentsKeratinocytesKeratinsMolecular Docking SimulationMutationProtein BindingProtein Conformation, alpha-HelicalProtein DomainsProtein PrecursorsRecombinant ProteinsS100 ProteinsCrystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts.
Lomakin IB, Hinbest AJ, Ho M, Eldirany SA, Bunick CG. Crystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts. The Yale Journal Of Biology And Medicine 2020, 93: 3-17. PMID: 32226330, PMCID: PMC7087056.Peer-Reviewed Original Research
2017
EIF1AX and NRAS Mutations Co-occur and Cooperate in Low-Grade Serous Ovarian Carcinomas
Etemadmoghadam D, Azar WJ, Lei Y, Moujaber T, Garsed DW, Kennedy CJ, Fereday S, Mitchell C, Chiew YE, Hendley J, Sharma R, Harnett PR, Li J, Christie EL, Patch AM, George J, Au-Yeung G, Mir Arnau G, Holloway TP, Semple T, Pearson JV, Waddell N, Grimmond SM, Köbel M, Rizos H, Lomakin IB, Bowtell DDL, deFazio A. EIF1AX and NRAS Mutations Co-occur and Cooperate in Low-Grade Serous Ovarian Carcinomas. Cancer Research 2017, 77: 4268-4278. PMID: 28646021, DOI: 10.1158/0008-5472.can-16-2224.Peer-Reviewed Original ResearchConceptsLow-grade serous ovarian carcinomaSerous ovarian carcinomaRAS pathway mutationsRAS pathway activationCoexpression of mutantWhole-genome sequencingTranslational regulatorOvarian cancerOvarian carcinomaPoor responseInitiation fidelityN-terminusGenome sequencingCancer ResMutational eventsPathway activationPathway mutationsClonogenic survivalMutationsRecurrent mutationsProteinChemotherapy