1993
In vitro assembly of multiprotein complexes containing alpha, beta, and gamma tubulin, heat shock protein HSP70, and elongation factor 1 alpha.
Marchesi V, Ngo N. In vitro assembly of multiprotein complexes containing alpha, beta, and gamma tubulin, heat shock protein HSP70, and elongation factor 1 alpha. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3028-3032. PMID: 8464918, PMCID: PMC46230, DOI: 10.1073/pnas.90.7.3028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCentrifugation, Density GradientCHO CellsCricetinaeElectrophoresis, Polyacrylamide GelHeat-Shock ProteinsHeLa CellsHumansImmunoblottingMacromolecular SubstancesMitosisModels, StructuralMolecular WeightNocodazolePeptide Elongation Factor 1Peptide Elongation FactorsRibonucleoproteinsTubulinConceptsElongation factor 1 alphaHeat shock protein Hsp70Multiprotein complexesShock protein Hsp70Factor 1 alphaGamma-tubulinProtein Hsp70Regulation of mitosisPresence of ATPDistinct complexesMitotic centrosomesActin isoformsSucrose gradient ultracentrifugationVitro assemblyTubulin isoformsLow abundanceCHO cellsHSP70Degrees C incubationProteinCognate formIsoformsSmall precursorsHigh-speed centrifugationComplexes
1985
Stabilizing Infrastructure of Cell Membranes
Marchesi V. Stabilizing Infrastructure of Cell Membranes. Annual Review Of Cell And Developmental Biology 1985, 1: 531-561. PMID: 3916322, DOI: 10.1146/annurev.cb.01.110185.002531.Peer-Reviewed Original ResearchSite specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains.
Georgatos S, Weaver D, Marchesi V. Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains. Journal Of Cell Biology 1985, 100: 1962-1967. PMID: 3158665, PMCID: PMC2113597, DOI: 10.1083/jcb.100.6.1962.Peer-Reviewed Original Research
1982
The membrane skeleton as a potential target for toxic agents.
Marchesi V. The membrane skeleton as a potential target for toxic agents. Mead Johnson Symposium On Perinatal And Developmental Medicine 1982, 13-6. PMID: 6765455.Peer-Reviewed Original Research
1978
Functional components of surface membranes: potential targets for pharmacological manipulation.
Marchesi V. Functional components of surface membranes: potential targets for pharmacological manipulation. Pharmacological Reviews 1978, 30: 371-81. PMID: 392535.Peer-Reviewed Original Research
1977
Phosphorylation in membranes of intact human erythrocytes.
Shapiro D, Marchesi V. Phosphorylation in membranes of intact human erythrocytes. Journal Of Biological Chemistry 1977, 252: 508-517. PMID: 188816, DOI: 10.1016/s0021-9258(17)32746-1.Peer-Reviewed Original ResearchConceptsIntact human erythrocytesStudy of phosphorylationPattern of phosphorylationHuman erythrocytesIntact cell systemMembrane proteinsLipid phosphorylationIntracellular portionIntact cellsPolyacrylamide gel electrophoresisMembrane phosphorylationPhosphorylationMembrane sialoglycoproteinGlycophorin AGlycophorin A.Gel electrophoresisPhosphate exchangeCell system
1967
Inactivation of adenosine triphosphatase and disruption of red cell membrances by trypsin: protective effect of adenosine triphosphate.
Marchesi V, Palade G. Inactivation of adenosine triphosphatase and disruption of red cell membrances by trypsin: protective effect of adenosine triphosphate. Proceedings Of The National Academy Of Sciences Of The United States Of America 1967, 58: 991-995. PMID: 4228851, PMCID: PMC335737, DOI: 10.1073/pnas.58.3.991.Peer-Reviewed Original Research