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
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