Jimin Wang, PhD
Research ScientistCards
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Research
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2026
Dual site targeting of the bacterial 70S ribosome by tetracyclines
Devarkar S, Lomakin I, Wang J, Grada A, Bunick C. Dual site targeting of the bacterial 70S ribosome by tetracyclines. Nature Communications 2026, 17: 4452. PMID: 42156748, PMCID: PMC13186991, DOI: 10.1038/s41467-026-72788-9.Peer-Reviewed Original ResearchConceptsNascent peptide exit tunnelStructural comparisonPeptide exit tunnelHigh-resolution cryo-electron microscopyBacterial 70S ribosomeThreat of antibiotic resistanceSpecies-specific differencesCryo-electron microscopyExit tunnelDecoding centerBacterial ribosomeEscherichia coliAntibiotic resistanceStructural basisRibosomeBacterial diseasesTetracyclineSubunitMechanism of actionLyme diseaseRational designMRNACutibacteriumTetracycline classModel-dependent and model-independent visualization of hydrogen atoms in high-resolution cryoEM maps
Wang J. Model-dependent and model-independent visualization of hydrogen atoms in high-resolution cryoEM maps. Acta Crystallographica Section D, Structural Biology 2026, 82: 533-549. PMID: 41954135, DOI: 10.1107/s2059798326002512.Peer-Reviewed Original ResearchConceptsExperimental electrostatic potentialH atomsNon-H atomsAtomic partial chargesX-rayCharge-densityPartial chargesCD mapHydrogen atomsModel-independent methodElectron-densityElectrostatic potentialEDS mappingCD profilesAtomsHydrogen signalModel-independentModel dependenceHydrogenCryoEM mapExperimental mapsStructural modelResolutionCryoEMComputational Evolution of Anti-PD‑1 Antibodies Induces Structural Refolding for High-Affinity Interactions
Shi Y, Kim Y, Liu P, Wang J, Tang S, Batista V. Computational Evolution of Anti-PD‑1 Antibodies Induces Structural Refolding for High-Affinity Interactions. Biochemistry 2026, 65: 517-520. PMID: 41671420, DOI: 10.1021/acs.biochem.5c00574.Peer-Reviewed Original Research
2025
Visualizing the translation landscape in human cells at high resolution
Zheng W, Zhang Y, Wang J, Wang S, Chai P, Bailey E, Zhu C, Guo W, Devarkar S, Wu S, Lin J, Zhang K, Liu J, Lomakin I, Xiong Y. Visualizing the translation landscape in human cells at high resolution. Nature Communications 2025, 16: 10757. PMID: 41315256, PMCID: PMC12663405, DOI: 10.1038/s41467-025-65795-9.Peer-Reviewed Original ResearchConceptsTranslational landscapeHuman cellsCryo-focused ion beamHigh-resolution structuresHuman 80S ribosomesSingle-particle cryo-electron microscopyCryo-EM approachCryo-electron microscopyRibosome structurePurified ribosomesConsensus structureRibosomeE siteA-resolutionIon beamCryo-EMProtein synthesisNative ribosomesStructure of macromoleculesNative environmentPolyamine bindingCycloheximideEnvironment of ionsCellsPolyaminesAtomistic modulation of MIF‐2 structure, catalysis, and biological signaling via cysteine residues and a small molecule, Ebselen
Widjaja V, D'Orazio S, Das P, Rajendran D, Takada X, Shi Y, Varghese I, Lam Y, DaSilva N, Wang J, Batista V, Bhandari V, Lisi G. Atomistic modulation of MIF‐2 structure, catalysis, and biological signaling via cysteine residues and a small molecule, Ebselen. Protein Science 2025, 34: e70344. PMID: 41099614, PMCID: PMC12529878, DOI: 10.1002/pro.70344.Peer-Reviewed Original ResearchConceptsMIF-2Small moleculesBiological functionsMolecular dynamics simulationsMIF trimerMacrophage migration inhibitory factorNuclear magnetic resonanceRegulation of macrophage migration inhibitory factorD-dopachrome tautomeraseSelenylsulfide bondAllosteric crosstalkAllosteric switchDynamics simulationsAllosteric pathwaysBiochemical functionsConformational transitionCysteine residuesProximal cysteineStructural biologyBiological signalsQuaternary structureAllosteric mechanismSignaling activityCatalysisD-dopachromeStructural Basis for Differential Jak2 and Jak3 Kinase Selectivity of Ruxolitinib and Delgocitinib
Wang J, Bunick C. Structural Basis for Differential Jak2 and Jak3 Kinase Selectivity of Ruxolitinib and Delgocitinib. Journal Of Investigative Dermatology 2025, 146: 287-290. PMID: 40825469, DOI: 10.1016/j.jid.2025.08.004.Peer-Reviewed Original ResearchStructural Insights: What Makes Some PDE4 Inhibitors More Effective in Inflammatory Dermatoses.
Issa N, Wang J, Hanly A, Ho M, Obagi S, Damiani G, Del Rosso J, Kang Y, Bunick C. Structural Insights: What Makes Some PDE4 Inhibitors More Effective in Inflammatory Dermatoses. The Journal Of Clinical And Aesthetic Dermatology 2025, 18: 18-21. PMID: 40778010, PMCID: PMC12327561.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsA Triple-Action Inhibitory Mechanism of Allosteric TYK2-Specific Inhibitors
Wang J, Lomakin I, Batista V, Bunick C. A Triple-Action Inhibitory Mechanism of Allosteric TYK2-Specific Inhibitors. Journal Of Investigative Dermatology 2025, 145: 3158-3173. PMID: 40378946, DOI: 10.1016/j.jid.2025.04.025.Peer-Reviewed Original ResearchJak-signal transducer and activatorAutoinhibited statePseudokinase domainIFN-induced gene expressionAtomic resolution structuresPhosphorylation of downstream proteinsAdenosine triphosphate bindingTyk2 kinaseTriphosphate bindingKinase domainActive stateResolution structureKinase activityTYK2Gene expressionStructural basisDownstream proteinsAllosteric drugsSteric clashesAllosteric inhibitorsInhibition mechanismMechanistic hypothesesKinaseBindingProteinMechanistic insight into O=O bond formation upon model‐independent visualization of the coordination geometry and ligand composition of Mn4Ca cofactor in dark‐adapted photosystem II structures
Wang J. Mechanistic insight into O=O bond formation upon model‐independent visualization of the coordination geometry and ligand composition of Mn4Ca cofactor in dark‐adapted photosystem II structures. Acta Crystallographica Section D, Structural Biology 2025, 81: 291-309. PMID: 40349162, DOI: 10.1107/s2059798325003699.Peer-Reviewed Original ResearchConceptsOxygen-evolving centerX-ray crystal structureCoordination geometryLigand compositionPhotosystem II samplesLigand sitesManganese ionsMn(III) ionO bond formationX-rayOxidation of waterDark-adapted photosystem IIPhotosystem II structureBond lengthsPhotosystem IIOxidation numberOxidation stateSpectroscopic studiesPSII samplesII structureElectron densityIonsMechanistic insightOxidationOxygenPDE4 Inhibitors: Bridging Molecular Insights With Clinical Impact.
Issa N, Obagi S, Damiani G, Wang J, Bunick C. PDE4 Inhibitors: Bridging Molecular Insights With Clinical Impact. Journal Of Drugs In Dermatology 2025, 24: 631-633. PMID: 40465498, DOI: 10.36849/jdd.9089.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsPhosphodiesterase-4 inhibitorPhosphodiesterase-4Cyclic adenosine monophosphateClinical impactContraindications to systemic therapyEffective suppression of inflammationInhibition of phosphodiesterase-4Minimal systemic side effectsChronic inflammatory skin diseaseSystemic side effectsInflammatory skin diseaseTherapeutic decision-makingSuppression of inflammationMessenger cyclic adenosine monophosphateClinically meaningful guidanceCombination regimensSystemic therapyRefractory casesTreatment landscapeTargeted therapyLichen planusSkin erythemaAtopic dermatitisSeborrheic dermatitisSide effects
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