Major glycoprotein of the human erythrocyte membrane: Evidence for an amphipathic molecular structure1
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Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization
2014, Journal of Biological ChemistryCitation Excerpt :Physiological concentrations of free zinc ions generally exceed copper ion concentrations by magnitudes (42, 43) due to the high number of copper chelation sites provided by proteins (44, 45). To validate the specificity of APLP1 oligomerization upon zinc exposure, we also tested APLP1-CFP in combination with glycophorin A-YFP (GypA), another single-pass transmembrane protein localized to the plasma membrane (46). Whereas a low basal level of FRET was observed due to random plasma membrane encounters between APLP1-CFP and GypA-YFP (Fig. 3E), the presence of zinc prompted a slight decrease in the nonspecific FRET signal indicative of fewer encounters of APLP1 and GypA (likely due to the increased APLP1-YFP oligomerization that lowered the number of freely diffusing APLP1 entities).
Reaction of ozone with glycophorin in solution and in lipid vesicles
1992, Archives of Biochemistry and Biophysics
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Human Erythrocyte Glycophorin (1).
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Present address: Baylor College of Medicine and the Methodist Hospital, Department of Internal Medicine, Houston, Texas 77025.