2008
The Relevance of Research on Red Cell Membranes to the Understanding of Complex Human Disease: A Personal Perspective
Marchesi VT. The Relevance of Research on Red Cell Membranes to the Understanding of Complex Human Disease: A Personal Perspective. Annual Review Of Pathology Mechanisms Of Disease 2008, 3: 1-9. PMID: 18039128, DOI: 10.1146/annurev.pathmechdis.3.121806.154321.Peer-Reviewed Original ResearchConceptsCell membrane proteinsMembrane proteinsHuman cell membrane proteinsHuman diseasesRed blood cell membrane proteinsComplex human diseasesMolecular biological studiesRed cell membraneRecombinant DNAMolecular analysisCell membraneHuman erythrocyte membranesService of researchBiological studiesProteinErythrocyte membranesMembrane
2005
An alternative interpretation of the amyloid Aβ hypothesis with regard to the pathogenesis of Alzheimer's disease
Marchesi VT. An alternative interpretation of the amyloid Aβ hypothesis with regard to the pathogenesis of Alzheimer's disease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 9093-9098. PMID: 15967987, PMCID: PMC1166615, DOI: 10.1073/pnas.0503181102.Peer-Reviewed Original ResearchAmino Acid MotifsAmino Acid SequenceAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesCell MembraneCentral Nervous SystemDimerizationEndopeptidasesHumansLipid BilayersMembrane GlycoproteinsMembrane ProteinsModels, BiologicalMolecular Sequence DataNeuronsPeptide HydrolasesPeptidesPresenilin-1Protein BindingSequence Homology, Amino AcidSodium Dodecyl SulfateTemperature
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 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
1984
Structure and function of the erythrocyte membrane skeleton.
Marchesi V. Structure and function of the erythrocyte membrane skeleton. Progress In Clinical And Biological Research 1984, 159: 1-12. PMID: 6236465.Peer-Reviewed Original Research
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
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
Functional components of surface membranes: potential targets for pharmacological manipulation.
Marchesi V. Functional components of surface membranes: potential targets for pharmacological manipulation. Pharmacological Reviews 1978, 30: 371-81. PMID: 392535.Peer-Reviewed Original ResearchRecent 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 Research
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 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