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
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
Recent Membrane Research and its Implications for Clinical Medicine
Marchesi V. Recent Membrane Research and its Implications for Clinical Medicine. Annual Review Of Medicine 1978, 29: 593-603. PMID: 348048, DOI: 10.1146/annurev.me.29.020178.003113.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell MembraneErythrocytesGlycophorinsGlycoproteinsHumansLipidsMembrane ProteinsSpectrinConceptsMembrane proteinsIntegral membrane proteinsMammalian cell membranesSpecific amino acid sequencesAmino acid sequenceMacromolecular complexesAcid sequenceCell membraneMolecular organizationRecognition sitesSuch glycoproteinsSpecific interactionsSurface membraneProteinMembrane researchLikely candidateTransport sitesMajor componentPeptide backboneMembraneCellsComplexesPolypeptideSitesSequenceSome molecular features of integral membrane proteins.
Marchesi V. Some molecular features of integral membrane proteins. Birth Defects 1978, 14: 127-38. PMID: 346076.Peer-Reviewed Original ResearchThe 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 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 ResearchPhosphorylation 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 systemMolecular 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
1971
Glycoproteins: Isolation from Cell Membranes with Lithium Diiodosalicylate
Marchesi V, Andrews E. Glycoproteins: Isolation from Cell Membranes with Lithium Diiodosalicylate. Science 1971, 174: 1247-1248. PMID: 5133448, DOI: 10.1126/science.174.4015.1247.Peer-Reviewed Original Research
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