2018
Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute
Cooper C, Silkstone G, Simons M, Rajagopal B, Syrett N, Shaik T, Gretton S, Welbourn E, Bülow L, Eriksson N, Ronda L, Mozzarelli A, Eke A, Mathe D, Reeder B. Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute. Free Radical Biology And Medicine 2018, 134: 106-118. PMID: 30594736, PMCID: PMC6597946, DOI: 10.1016/j.freeradbiomed.2018.12.030.Peer-Reviewed Original ResearchConceptsTyrosine residuesΒ-subunitSingle tyrosine mutationsFerryl heme speciesOxidative stressExtracellular proteinsTyrosine mutationWild typePromising mutantsHEK cellsProtein surfaceHeme speciesMutationsMembrane damageRedox-active tyrosine residueHeme reductionOxidative toxicityFerryl speciesFerric HbSubunitsHb additionHeme lossSpeciesProteinFerric form
2008
Towards a novel haemoglobin-based oxygen carrier: Euro-PEG-Hb, physico-chemical properties, vasoactivity and renal filtration
Portörő I, Kocsis L, Hermán P, Caccia D, Perrella M, Ronda L, Bruno S, Bettati S, Micalella C, Mozzarelli A, Varga A, Vas M, Lowe K, Eke A. Towards a novel haemoglobin-based oxygen carrier: Euro-PEG-Hb, physico-chemical properties, vasoactivity and renal filtration. Biochimica Et Biophysica Acta 2008, 1784: 1402-1409. PMID: 18405674, DOI: 10.1016/j.bbapap.2008.03.005.Peer-Reviewed Original Research