1990
A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV
Yannariello-Brown J, Madri J. A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV. Biochemical Journal 1990, 265: 383-392. PMID: 2154186, PMCID: PMC1136898, DOI: 10.1042/bj2650383.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell MembraneCells, CulturedChromatography, AffinityChymotrypsinCollagenElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEndothelium, VascularFluorescent Antibody TechniqueImmune SeraMolecular WeightPeptide MappingPhosphoproteinsReceptors, Cell SurfaceReceptors, CollagenConceptsBovine aortic endothelial cellsSDS/PAGENon-equilibrium pH gel electrophoresisCollagen type IVCollagenous domainTwo-dimensional gel systemAortic endothelial cellsAdhesion assaysCell surface populationIndirect immunofluorescence experimentsGlobular NC1 domainCell surface labelingCollagen-binding proteinsChymotryptic peptide mapsEndothelial cellsGlobular domainIntracellular transportMinor isoformIndividual isoformsImmunofluorescence experimentsMolecular massGolgi regionCollagenous regionCell surfacePeptide maps
1982
Type V Collagens of the Human Placenta: Trimer α-Chain Composition, Ultrastructural Morphology and Peptide Analysis
Madri J, Foellmer H, Furthmayr H. Type V Collagens of the Human Placenta: Trimer α-Chain Composition, Ultrastructural Morphology and Peptide Analysis. Collagen And Related Research 1982, 2: 19-29. PMID: 7105646, DOI: 10.1016/s0174-173x(82)80038-1.Peer-Reviewed Original Research