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 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
1981
The carboxyl-terminal domain of human erythrocyte band 3. Description, isolation, and location in the bilayer.
Markowitz S, Marchesi V. The carboxyl-terminal domain of human erythrocyte band 3. Description, isolation, and location in the bilayer. Journal Of Biological Chemistry 1981, 256: 6463-6468. PMID: 7240219, DOI: 10.1016/s0021-9258(19)69187-8.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate bindingBand 3 moleculesCarboxyl-terminal fragmentBand 3NH2-terminal cytoplasmic domainMembrane-spanning domainsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisBand 3 fragmentSulfate-polyacrylamide gel electrophoresisCarboxyl-terminal domainAnion channel proteinCarboxyl-terminal regionPolyacrylamide gel electrophoresisGel electrophoresisSulfate bindingHomogeneous polypeptideCytoplasmic domainIdentical peptide mapsMoleculesMajor transmembraneHuman erythrocyte band 3Channel proteinsBroad bandErythrocyte band 3
1979
Functional proteins of the human red blood cell membrane.
Marchesi V. Functional proteins of the human red blood cell membrane. Seminars In Hematology 1979, 16: 3-20. PMID: 370984.Peer-Reviewed Original Research
1978
The anomalous electrophoretic behavior of the major sialoglycoprotein from the human erythrocyte.
Silverberg M, Marchesi V. The anomalous electrophoretic behavior of the major sialoglycoprotein from the human erythrocyte. Journal Of Biological Chemistry 1978, 253: 95-98. PMID: 618870, DOI: 10.1016/s0021-9258(17)38274-1.Peer-Reviewed Original Research
1977
Molecular features of integral membrane proteins of the human red cell membrane.
Marchesi V. Molecular features of integral membrane proteins of the human red cell membrane. Advances In Pathobiology 1977, 30-41. PMID: 331915.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 ResearchConceptsAmino 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