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
Site 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 ResearchThe binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions.
Georgatos S, Marchesi V. The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions. Journal Of Cell Biology 1985, 100: 1955-1961. PMID: 3158664, PMCID: PMC2113610, DOI: 10.1083/jcb.100.6.1955.Peer-Reviewed Original ResearchMeSH KeywordsAnkyrinsBinding SitesBinding, CompetitiveCytoskeletonErythrocyte MembraneHumansImmunologic TechniquesMacromolecular SubstancesMembrane ProteinsVimentinConceptsBinding of vimentinProtein 4.1Membrane vesiclesAnti-ankyrin antibodiesErythrocyte membrane skeletonHuman erythrocyte membrane vesiclesIntermediate filament proteinsErythrocyte membrane vesiclesMajor attachment siteMembrane skeletonPlasma membraneBinding functionsAnkyrinFilament proteinsCytoplasmic fragmentsBand 4.5Glycophorin ASpectrinVesiclesAttachment sitesHuman erythrocyte membranesBand 3
1984
Isolation of spectrin subunits and reassociation in vitro. Analysis by fluorescence polarization.
Yoshino H, Marchesi V. Isolation of spectrin subunits and reassociation in vitro. Analysis by fluorescence polarization. Journal Of Biological Chemistry 1984, 259: 4496-4500. PMID: 6707015, DOI: 10.1016/s0021-9258(17)43074-2.Peer-Reviewed Original ResearchMeSH KeywordsFluorescence PolarizationHumansKineticsMacromolecular SubstancesMicroscopy, ElectronPeptidesSpectrinTemperatureUreaConceptsFluorescence anisotropy changesFluorescence polarizationEventual dissociationGood yieldsDEAE-cellulose column chromatographyOligomeric speciesMonomer stateColumn chromatographyNeutral salt solutionsElectron microscopyAcrylamide gel electrophoresisSalt solutionLow-angle shadowingM ureaTryptophan residuesBeta subunitPure alphaSpectrinSubdomain structureSpectrin moleculesSubunitsLow concentrationsErythrocyte spectrinSpectrin subunitsGel electrophoresis
1983
The red cell membrane skeleton: recent progress.
Marchesi V. The red cell membrane skeleton: recent progress. Blood 1983, 61: 1-11. PMID: 6293625, DOI: 10.1182/blood.v61.1.1.bloodjournal6111.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
1977
Molecular Features of Glycophorin A: The Major Sialoglycoprotein of the Human Erythrocyte Membrane
MARCHESI V. Molecular Features of Glycophorin A: The Major Sialoglycoprotein of the Human Erythrocyte Membrane. Biochemical Society Transactions 1977, 5: 59-59. PMID: 892207, DOI: 10.1042/bst0050059.Peer-Reviewed Original Research
1975
Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
Tomita M, Marchesi V. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1975, 72: 2964-2968. PMID: 1059087, PMCID: PMC432899, DOI: 10.1073/pnas.72.8.2964.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBinding SitesBlood ProteinsErythrocytesGlycoproteinsHexosesHumansMacromolecular SubstancesMolecular WeightOligosaccharidesProtein BindingSialic AcidsConceptsAmino acid sequenceAmino acidsThreonine/serine residuesComplete amino acid sequenceClustering of residuesHydrophilic amino acidsMembrane proteinsSerine residuesTransmembrane orientationOligosaccharide attachment sitesNH2 terminusHuman erythrocyte glycophorinNonpolar residuesEdman degradation techniqueOligosaccharide chainsMajor sialoglycoproteinAttachment sitesHuman erythrocyte membranesResiduesMore complex unitsGlycophorinTerminal segmentGlycosidic bondSequenceUnique structure