2019
Non-invasive and real-time measurement of microvascular barrier in intact lungs
Engler AJ, Raredon MSB, Le AV, Yuan Y, Oczkowicz YA, Kan EL, Baevova P, Niklason LE. Non-invasive and real-time measurement of microvascular barrier in intact lungs. Biomaterials 2019, 217: 119313. PMID: 31280072, PMCID: PMC6863174, DOI: 10.1016/j.biomaterials.2019.119313.Peer-Reviewed Original ResearchEpac agonist improves barrier function in iPSC-derived endothelial colony forming cells for whole organ tissue engineering
Yuan Y, Engler AJ, Raredon MS, Le A, Baevova P, Yoder MC, Niklason LE. Epac agonist improves barrier function in iPSC-derived endothelial colony forming cells for whole organ tissue engineering. Biomaterials 2019, 200: 25-34. PMID: 30754017, DOI: 10.1016/j.biomaterials.2019.02.005.Peer-Reviewed Original Research
2017
Bioengineered lungs generated from human iPSCs‐derived epithelial cells on native extracellular matrix
Ghaedi M, Le AV, Hatachi G, Beloiartsev A, Rocco K, Sivarapatna A, Mendez JJ, Baevova P, Dyal RN, Leiby KL, White ES, Niklason LE. Bioengineered lungs generated from human iPSCs‐derived epithelial cells on native extracellular matrix. Journal Of Tissue Engineering And Regenerative Medicine 2017, 12: e1623-e1635. PMID: 29024475, PMCID: PMC5991621, DOI: 10.1002/term.2589.Peer-Reviewed Original ResearchConceptsEpithelial progenitor cellsProgenitor cellsStem cellsEpithelial cellsLung progenitor cellsLung epithelial cellsHuman lungHuman-derived cellsReliable cell sourceNative extracellular matrixEarly stepsExtracellular matrixRat lungImportant early stepHuman iPSCLung regenerationLung tissue regenerationHuman lung tissueIPSCsLung scaffoldsCell sourceCellsEpithelial markersLung transplantationTissue regenerationControlled gas exchange in whole lung bioreactors
Engler AJ, Le AV, Baevova P, Niklason LE. Controlled gas exchange in whole lung bioreactors. Journal Of Tissue Engineering And Regenerative Medicine 2017, 12: e119-e129. PMID: 28083925, PMCID: PMC5975638, DOI: 10.1002/term.2408.Peer-Reviewed Original Research
2016
Comparative biology of decellularized lung matrix: Implications of species mismatch in regenerative medicine
Balestrini JL, Gard AL, Gerhold KA, Wilcox EC, Liu A, Schwan J, Le AV, Baevova P, Dimitrievska S, Zhao L, Sundaram S, Sun H, Rittié L, Dyal R, Broekelmann TJ, Mecham RP, Schwartz MA, Niklason LE, White ES. Comparative biology of decellularized lung matrix: Implications of species mismatch in regenerative medicine. Biomaterials 2016, 102: 220-230. PMID: 27344365, PMCID: PMC4939101, DOI: 10.1016/j.biomaterials.2016.06.025.Peer-Reviewed Original ResearchConceptsHuman endothelial cellsCell-matrix interactionsLung regenerationEndothelial cellsKey matrix proteinsComparative biologyCell adhesion moleculeMatrix proteinsLung extracellular matrixCell healthExtracellular matrixResidual DNASpecies mismatchRat lung scaffoldsRegenerative medicineAdhesion moleculesLung scaffoldsPrimate tissuesCellsVascular cell adhesion moleculeLung engineeringLung matrixLess expressionPulmonary cellsProfound effect
2008
Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum
Elliott D, McIntosh M, Hosgood H, Chen S, Zhang G, Baevova P, Joiner K. Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 2463-2468. PMID: 18263733, PMCID: PMC2268159, DOI: 10.1073/pnas.0711067105.Peer-Reviewed Original Research
2007
Traffic to the Malaria Parasite Food Vacuole A NOVEL PATHWAY INVOLVING A PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING PROTEIN *
McIntosh M, Vaid A, Hosgood H, Vijay J, Bhattacharya A, Sahani M, Baevova P, Joiner K, Sharma P. Traffic to the Malaria Parasite Food Vacuole A NOVEL PATHWAY INVOLVING A PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING PROTEIN *. Journal Of Biological Chemistry 2007, 282: 11499-11508. PMID: 17289673, DOI: 10.1074/jbc.m610974200.Peer-Reviewed Original ResearchConceptsFYVE proteinFood vacuolesFYVE domain-containing proteinsDomain-containing proteinsZinc finger motifsParasite food vacuoleHigher eukaryotesEndosomal proteinFinger motifSecretory pathwayParasite cytosolDeletion mutantsDomain familyEndocytic organellesRegulatory proteinsKey residuesMutagenesis studiesPeptide domainBinding proteinLysosomal compartmentNovel pathwayFunctional roleProteinKey ligandPathway
2004
The Plasmodium falciparum Vps4 homolog mediates multivesicular body formation
Yang M, Coppens I, Wormsley S, Baevova P, Hoppe H, Joiner K. The Plasmodium falciparum Vps4 homolog mediates multivesicular body formation. Journal Of Cell Science 2004, 117: 3831-3838. PMID: 15252121, DOI: 10.1242/jcs.01237.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateAnimalsCell ProliferationCholesterolCloning, MolecularCOS CellsCytoplasmCytosolDNAElectroporationEndosomal Sorting Complexes Required for TransportEndosomesFibroblastsGreen Fluorescent ProteinsHumansHydrolysisImmunoblottingLipoproteins, LDLMicroscopy, ElectronMutationPhylogenyPlasmodium falciparumProtein Structure, TertiaryProtozoan ProteinsSubcellular FractionsToxoplasmaTransfectionTransgenesConceptsMultivesicular bodiesCOS cellsRelated parasite Toxoplasma gondiiUnique secretory organellesClass E genesMultivesicular body formationEndosomal multivesicular bodiesHost cell invasionLarge vesicular structuresPlasmodium falciparum homologP. falciparumVps4 functionEndosomal intermediatesApicomplexan familyPhylogenetic boundariesATP bindingSecretory organellesEarly endosomesParasite Toxoplasma gondiiP. falciparum trophozoitesATP hydrolysisInternal membranesT. gondiiBody formationCell invasion