2015
Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter
Lee Y, Min CK, Kim TG, Song HK, Lim Y, Kim D, Shin K, Kang M, Kang JY, Youn HS, Lee JG, An JY, Park KR, Lim JJ, Kim JH, Kim JH, Park ZY, Kim YS, Wang J, Kim DH, Eom SH. Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter. EMBO Reports 2015, 16: 1318-1333. PMID: 26341627, PMCID: PMC4662854, DOI: 10.15252/embr.201540436.Peer-Reviewed Original ResearchConceptsN-terminal domainMitochondrial calcium uniporterCalcium uniporterHuman mitochondrial calcium uniporterMitochondrial calcium uptake 1CaMKII phosphorylation siteDominant negative effectCell linesMitochondrial calcium uptakePhosphorylation sitesNovel foldDeletion mutantsMCU functionÅ resolutionTumor suppressorHeLa cell lineUniporterMutantsUptake 1Calcium uptakeS92SuppressorOncogeneRegulatorDomain
2009
Structural Basis for Functional Tetramerization of Lentiviral Integrase
Hare S, Di Nunzio F, Labeja A, Wang J, Engelman A, Cherepanov P. Structural Basis for Functional Tetramerization of Lentiviral Integrase. PLOS Pathogens 2009, 5: e1000515. PMID: 19609359, PMCID: PMC2705190, DOI: 10.1371/journal.ppat.1000515.Peer-Reviewed Original ResearchConceptsDimer-dimer interface
2008
A regulatable switch mediates self-association in an immunoglobulin fold
Calabrese MF, Eakin CM, Wang JM, Miranker AD. A regulatable switch mediates self-association in an immunoglobulin fold. Nature Structural & Molecular Biology 2008, 15: 965-971. PMID: 19172750, PMCID: PMC2680708, DOI: 10.1038/nsmb.1483.Peer-Reviewed Original ResearchMeSH KeywordsAmyloidAmyloidosisBeta 2-MicroglobulinCopperCrystallography, X-RayElectron Spin Resonance SpectroscopyHumansHydrophobic and Hydrophilic InteractionsImmunoglobulinsIn Vitro TechniquesModels, BiologicalModels, MolecularMultiprotein ComplexesProtein FoldingProtein Interaction Domains and MotifsProtein Structure, QuaternaryRenal Dialysis