2022
Retro-2 alters Golgi structure
Yue X, Gim B, Zhu L, Tan C, Qian Y, Graham M, Liu X, Lee I. Retro-2 alters Golgi structure. Scientific Reports 2022, 12: 14975. PMID: 36056100, PMCID: PMC9438350, DOI: 10.1038/s41598-022-19415-x.Peer-Reviewed Original ResearchConceptsRetro-2Golgi apparatusGolgi structureER exit site proteinGolgi structural proteinsGolgi stacksER exitGolgi organizationIndividual cisternaeGolgiStructural proteinsProtein secretionPerinuclear areaUltra-structural studiesEM tomographyVesicular profilesHuman lung cellsPartial disassemblySyntaxin5ProteinCultured human lung cellsCell depletionDisassemblyUltrastructureCells
2019
Parasite‐Derived Vesicular‐Mediated Protein Export by the Human Pathogen Babesia microti
Mamoun C, Thekkiniath J, Kilian N, Lawres L, Gewirtz M, Abraham A, Graham M, Liu X, Ledizet M. Parasite‐Derived Vesicular‐Mediated Protein Export by the Human Pathogen Babesia microti. The FASEB Journal 2019, 33: 649.2-649.2. DOI: 10.1096/fasebj.2019.33.1_supplement.649.2.Peer-Reviewed Original ResearchMajor morphogenetic changesImmunoelectron microscopy analysisB. microtiProtein exportPhylum ApicomplexaMorphogenetic changesSecreted proteinsCell fractionationIntraerythrocytic developmentCanonical motifsExport systemPlasma membraneErythrocyte cytoplasmMajor immunodominant antigenBabesia microtiParasitophorous vacuoleHost erythrocyteWorldwide geographic distributionMalaria-like illnessGeographic distributionMalaria parasitesCell environmentProteinFASEB JournalFull-text articles
2014
Membrane adhesion dictates Golgi stacking and cisternal morphology
Lee I, Tiwari N, Dunlop MH, Graham M, Liu X, Rothman JE. Membrane adhesion dictates Golgi stacking and cisternal morphology. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1849-1854. PMID: 24449908, PMCID: PMC3918774, DOI: 10.1073/pnas.1323895111.Peer-Reviewed Original ResearchConceptsFK506-binding protein (FKBP) domainsGolgi cisternaeGolgi matrix proteinsClass of proteinsCisternal morphologyCisternal maturationProtein domainsGolgi membranesGolgi stacksRegulatory proteinsGolgiMatrix proteinsMembrane adhesionMembrane transportProtein 55Adhesive processHeLa cellsAdhesive proteinsProteinGolginsCargo transportAncient formCisternaeQuantitative electron microscopyMitochondria
2012
Nuclear localization of Klotho in brain: an anti-aging protein
German D, Khobahy I, Pastor J, Kuro-o M, Liu X. Nuclear localization of Klotho in brain: an anti-aging protein. Neurobiology Of Aging 2012, 33: 1483.e25-1483.e30. PMID: 22245317, PMCID: PMC3328593, DOI: 10.1016/j.neurobiolaging.2011.12.018.Peer-Reviewed Original ResearchConceptsExtracellular domainNuclear membraneSingle-pass transmembrane proteinMultiple fibroblast growth factor receptorsFibroblast growth factor receptorNuclear functionsPrecise cellular localizationTransmembrane proteinGrowth factor receptorNuclear localizationPlasma membraneTransmembrane formCellular localizationCell typesCultured cellsAnti-aging proteinCell membraneImmunoelectron microscopyLigand affinityWhole animalFactor receptorAntioxidant enzymesProteinKlotho proteinGenes