1985
The 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 ResearchConceptsBinding 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
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