2020
Recent 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 ResearchMeSH KeywordsAmino Acid SequenceAnimalsCytoskeletonHumansIntermediate Filament ProteinsIntermediate FilamentsLaminsModels, MolecularMutationConceptsIntermediate 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 proteinDomainMolecular Modeling of Pathogenic Mutations in the Keratin 1B Domain
Hinbest AJ, Eldirany SA, Ho M, Bunick CG. Molecular Modeling of Pathogenic Mutations in the Keratin 1B Domain. International Journal Of Molecular Sciences 2020, 21: 6641. PMID: 32927888, PMCID: PMC7555247, DOI: 10.3390/ijms21186641.Peer-Reviewed Original Research
2019
Human keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly
Eldirany SA, Ho M, Hinbest AJ, Lomakin IB, Bunick CG. Human keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly. The EMBO Journal 2019, 38: embj2018100741. PMID: 31036554, PMCID: PMC6545558, DOI: 10.15252/embj.2018100741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCircular DichroismCrystallography, X-RayCytoskeletonDynamic Light ScatteringHumansHydrophobic and Hydrophilic InteractionsIntermediate Filament ProteinsKeratin-1Keratin-10Models, MolecularMutation, MissenseProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondarySkin DiseasesConceptsFilament assemblyN-terminal hydrophobic pocketIntermediate filament assemblyTetramer assemblyÅ structureÅ resolutionCircular dichroism measurementsTetramer formationAssembly mechanismHydrophobic faceHydrophobic pocketSecondary structureOctamer structureEpidermolytic palmoplantar keratodermaKeratin filamentsIntermediate filamentsMutationsPathogenic mutationsTetramer structureDichroism measurementsAtomic resolutionAssemblyBiochemical determinantsKeratin 1/10Tetramer
2016
An ubiquitin-binding molecule can work as an inhibitor of ubiquitin processing enzymes and ubiquitin receptors
Nguyen T, Ho M, Ghosh A, Kim T, Yun S, Lee S, Kim K. An ubiquitin-binding molecule can work as an inhibitor of ubiquitin processing enzymes and ubiquitin receptors. Biochemical And Biophysical Research Communications 2016, 479: 33-39. PMID: 27613091, DOI: 10.1016/j.bbrc.2016.09.010.Peer-Reviewed Original ResearchConceptsUbiquitin processing enzymesUbiquitin receptorsUbiquitin pathwayProcessing enzymesBinding of ubiquitinDiverse biological processesCancer cell migrationBiological roleBiological processesUbiquitinCell migrationEnzymatic activityInteracting surfacesCritical rolePathwayEnzymeRelated diseasesRelevant diseasesInhibitorsReceptorsBindsMoleculesRoleBindingInteraction