2022
Cell-specific bioorthogonal tagging of glycoproteins
Cioce A, Calle B, Rizou T, Lowery SC, Bridgeman VL, Mahoney KE, Marchesi A, Bineva-Todd G, Flynn H, Li Z, Tastan OY, Roustan C, Soro-Barrio P, Rafiee MR, Garza-Garcia A, Antonopoulos A, Wood TM, Keenan T, Both P, Huang K, Parmeggian F, Snijders AP, Skehel M, Kjær S, Fascione MA, Bertozzi CR, Haslam SM, Flitsch SL, Malaker SA, Malanchi I, Schumann B. Cell-specific bioorthogonal tagging of glycoproteins. Nature Communications 2022, 13: 6237. PMID: 36284108, PMCID: PMC9596482, DOI: 10.1038/s41467-022-33854-0.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsArtificial biosynthetic pathwayTumor-derived cell linesCellular model systemNon-transfected cellsCellular functionsProtein glycosylationBiosynthetic pathwayProteome analysisGlycosylation sitesBioorthogonal tagsCancer developmentCell linesModel systemImportant modulatorIntricate interactionsCo-culture modelGlycoproteinCellsGlycoprotein expressionMouse modelGlycoproteomeGlycosylationTaggingMonoculture
2021
The loss of DHX15 impairs endothelial energy metabolism, lymphatic drainage and tumor metastasis in mice
Ribera J, Portolés I, Córdoba-Jover B, Rodríguez-Vita J, Casals G, González-de la Presa B, Graupera M, Solsona-Vilarrasa E, Garcia-Ruiz C, Fernández-Checa JC, Soria G, Tudela R, Esteve-Codina A, Espadas G, Sabidó E, Jiménez W, Sessa WC, Morales-Ruiz M. The loss of DHX15 impairs endothelial energy metabolism, lymphatic drainage and tumor metastasis in mice. Communications Biology 2021, 4: 1192. PMID: 34654883, PMCID: PMC8519955, DOI: 10.1038/s42003-021-02722-w.Peer-Reviewed Original ResearchConceptsKey cellular processesIntracellular ATP productionCellular processesZebrafish embryosDownstream substratesATP biosynthesisProteome analysisMitochondrial membraneEndothelial cellsDHX15ATP productionRegulatory functionsDifferential expressionComplex IVascular regulatory functionEnergy metabolismVascular biologyTumor metastasisTherapeutical targetGene deficiencyPrimary tumor growthLower oxygen consumptionVascular physiologyDownregulation of VEGFCells
2020
Differential Protein Expression in Striatal D1- and D2-Dopamine Receptor-Expressing Medium Spiny Neurons
Mansuri MS, Peng G, Wilson RS, Lam TT, Zhao H, Williams KR, Nairn AC. Differential Protein Expression in Striatal D1- and D2-Dopamine Receptor-Expressing Medium Spiny Neurons. Proteomes 2020, 8: 27. PMID: 33066078, PMCID: PMC7709116, DOI: 10.3390/proteomes8040027.Peer-Reviewed Original ResearchFluorescence-activated nuclear sortingTranslating Ribosome Affinity PurificationSpecific neuronal cell typesBiological replicatesNeuronal cell typesCell typesRibosome affinity purificationDifferential protein expressionSpecific cell typesMice/Major cell typesNuclear sortingMass spectrometry analysisProteome analysisAffinity purificationNeuronal cell populationsMedium spiny neuronsProteinProteomeProtein expressionSpectrometry analysisCell populationsAdaptive changesNetwork analysisReproducible workflows
2016
The Role of PIWIL4, an Argonaute Family Protein, in Breast Cancer*
Wang Z, Liu N, Shi S, Liu S, Lin H. The Role of PIWIL4, an Argonaute Family Protein, in Breast Cancer*. Journal Of Biological Chemistry 2016, 291: 10646-10658. PMID: 26957540, PMCID: PMC4865913, DOI: 10.1074/jbc.m116.723239.Peer-Reviewed Original ResearchConceptsP-element-induced wimpy testisPIWI-interacting RNAsPIWI proteinsMDA-MB-231 cellsArgonaute family proteinsGermline developmentDiverse organismsWimpy testisFamily proteinsProteome analysisClass II proteinsPIWIL4Potential therapeutic targetStem cellsProteinMHC class II proteinsMigration abilityRNATherapeutic targetPIWIL4 expressionCancer tissuesBreast cancer tissuesCellsKey roleBiogenesis
2006
Proteome analysis of mitochondrial outer membrane from Neurospora crassa
Schmitt S, Prokisch H, Schlunck T, Camp DG, Ahting U, Waizenegger T, Scharfe C, Meitinger T, Imhof A, Neupert W, Oefner PJ, Rapaport D. Proteome analysis of mitochondrial outer membrane from Neurospora crassa. Proteomics 2006, 6: 72-80. PMID: 16294304, DOI: 10.1002/pmic.200402084.Peer-Reviewed Original ResearchConceptsMitochondrial outer membraneOuter membraneOuter membrane vesiclesNeurospora crassaImport machineryEukaryotic cellsGenetic systemOMV proteinsBiosynthetic pathwayProteomic studiesNovel functionProteome analysisIntracellular locationMembrane vesiclesTryptic peptide digestsProteinCrassaNumerous interactionsGel electrophoresisPeptide digestsLC-MS/MSMembraneProteomeOrganellesMitochondria
2003
Mapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies.
Góngora R, Acestor N, Quadroni M, Fasel N, Saravia NG, Walker J. Mapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies. Biomédica 2003, 23: 153-60. PMID: 12872554, DOI: 10.7705/biomedica.v23i2.1207.Peer-Reviewed Original ResearchConceptsProteome mapProteome analysisHeat shock protein familyRibosomal protein S12Comparative proteome analysisPeptide mass spectrometryTwo-dimensional polyacrylamide gel electrophoresisParaflagellar rod proteins 1Shock protein familyProtein expression profilesSpecies/strainsTwo-dimensional electrophoresisProtein expression studiesProtein S12Protein familyBioinformatics approachDistinct proteinsProtein spotsProtein mapsProtein 11Expression studiesExpression profilesUnknown functionDistinct parasite clonesPolyacrylamide gel electrophoresis
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