2024
Mechanistic Basis for the Translation Inhibition of Cutibacterium acnes by Clindamycin
Lomakin I, Devarkar S, Grada A, Bunick C. Mechanistic Basis for the Translation Inhibition of Cutibacterium acnes by Clindamycin. Journal Of Investigative Dermatology 2024, 144: 2553-2561.e3. PMID: 39122144, DOI: 10.1016/j.jid.2024.07.013.Peer-Reviewed Original ResearchNetwork of water-mediated interactionsCutibacterium acnesPeptide bond formationNascent peptideWater-mediated interactionsTranslational inhibitionAntibiotic resistanceCryogenic electron microscopyA-resolutionMechanistic basesAntibiotic-based therapiesRRNAAminoacyl groupRibosomeAcne pathogenesisAcne therapyAntibiotic stewardshipClindamycinIncreased resistanceAcne vulgarisClinical targetsAcneAntibioticsPeptideTRNA
2023
Structural basis for translation inhibition by MERS-CoV Nsp1 reveals a conserved mechanism for betacoronaviruses
Devarkar S, Vetick M, Balaji S, Lomakin I, Yang L, Jin D, Gilbert W, Chen S, Xiong Y. Structural basis for translation inhibition by MERS-CoV Nsp1 reveals a conserved mechanism for betacoronaviruses. Cell Reports 2023, 42: 113156. PMID: 37733586, DOI: 10.1016/j.celrep.2023.113156.Peer-Reviewed Original ResearchConceptsMERS-CoV nsp1Translation inhibitionRibosomal subunitΒ-CoVsModest sequence conservationMRNA entry channelEssential pathogenicity factorHost gene expressionHuman 40S ribosomal subunitSARS-CoV-2 nsp1Cryogenic electron microscopySequence conservationNon-structural protein 1Terminal domainPathogenicity factorsStructural basisGene expressionDevelopment of antiviralsNSP1Entry channelProtein 1Potential therapeutic targetSubunitsExtensive interactionsTherapeutic target