References related to Artifical Blood

  1. Cooper,C.E., Silkstone, G. G. A., Simons, M., Rajagopal, B. S., Syrett, N. Shaik, T., Gretton, S. Welbourn, E., Bulow, L., Leiva-Eriksson, N.,  Ronda, L.,  Mozzarelli, A., Eke, A., Mathe, D. Reeder, B. J., “Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute” Free Rad. Biol. Med. (2019) 134, 106-118

  2. Silkstone, G. G. A., Simons, M., Rajagopal, B. S., Shaik, T., Reeder, B. J., and Cooper, C. E. “Novel Redox Active Tyrosine Mutations Enhance the Regeneration of Functional Oxyhemoglobin from Methemoglobin: Implications for Design of Blood Substitutes”. Adv. Exp. Med. Biol. (2018)1072, 221-225.

  3. Simons, M., Gretton, S., Silkstone, G.G.A, Rajagopal, B.S., Allen-Baume, V., Syrett, N., Shaik, T., Eriksson, N., Ronda, L., Mozzarelli, A., Strader, M.B., Alayash, A.I., Reeder, B.J. & Cooper, C.E. “Comparison of the oxidative reactivity of recombinant fetal and adult human hemoglobin: implications for the design of hemoglobin-based oxygen carriers” Bioscience Reports. In Press.

  4. Alomari, E., Ronda, L., Bruno, S., Paredi, G., Marchetti, M., Bettati, S., Olivari, D., Fumagalli,F.,  Novelli, D., Ristagno G., Latini, R. Cooper, C.E., Reeder, B.J., Mozzarelli, A. “High- and low-affinity PEGylated hemoglobin-based oxygen carriers: differential oxidative stress in a Guinea pig transfusion model” Free Rad. Biol. Med. In Press.

  5. Reeder, B.J. Forum Review: “Redox and peroxidase activities of the hemoglobin superfamily - relevancy to health and disease.” Antioxid. Redox. Sign. (2017) 26(14) 763-776

  6. Silkstone, G., Silkstone, R.S., Wilson, M.T., Simons, M., Bulow, L., Kallberg, K., Ratanaspo, K., Ronda, L., Mozzarelli, A., Reeder, B.J., Cooper, C.E. “Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design” Biochem J. (2016) 473, 3371-3383

  7. Silkstone, R.S., Silkstone, G., Baath, J.A., Rajagopal, B., Nicholls, P., Reeder, B.J., Ronda, L., Bulow, L., Cooper, C.E. “The betaLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute.” Adv. Exp. Med. Biol. (2016) 876, 455-460

  8. Cooper, C.E., Schaer, D., Buehler, P.W., Wilson, M.T.,  Reeder, B.J., Silkstone, G.,  Svistunenko, D.A., Bulow, L., and  Alayash, A. "Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine beta-145"   Antioxidants & Redox Signaling  (2013) 18, 2246-2273

  9. Reeder B.J., Svistunenko D.A. Cooper, C.E. and Wilson M.T. “Engineering tyrosine-based electron flow pathways in proteins: the case of Aplysia myoglobin” J. Am. Chem Soc. (2012) 134, 7741-7749.

  10. Reeder, B.J. Comprehensive Invited Review: “The redox activity of hemoglobins: From physiological functions to pathologic mechanisms.” Antioxid. Redox. Sign. (2010) 13(7) 1087-1123

  11. Gaucher-Di Stasio, C., Paternotte, E., Prin-Mathieuc, C., Reeder, B.J., Poitevin, G., Labrude, P., Stoltz,  J., Copper, C.E., Menu, P. ”The importance of the effect of shear stress on endothelial cells in determining the performance of hemoglobin based oxygen carriers” Biomaterials (2009) 30(4), 445-451

  12. Reeder, B.J., Grey, M., Silaghi-Dumitrescu, R., Svistunenko, D.A., Bülow, L., Cooper, C.E. & Wilson, M.T “Tyrosine residues as redox cofactors in human hemoglobin: Implications for engineering non toxic blood substitutes” J. Biol. Chem (2008) 283(45), 30780-30787

  13. Reeder, B.J., Hider, R.C. & Wilson, M.T “Iron chelators can protect against oxidative stress through ferryl heme reduction” Free Rad. Biol. Med.(2008) 44(3) 264-273

  14. Reeder, B.J., Cutruzzola, F., Bigotti, M.  Hider, R.C. & Wilson, M.T “Tyrosine as a redox-active center in electron transfer to ferryl heme in globins” Free Rad. Biol. Med. (2008) 44(3) 274-283

  15. Wilson, M.T. & Reeder, B.J. “Oxygen binding haem proteins” Exp. Physiol. (2008) 93(1) 128-132

  16. Reeder, B.J. & Wilson, M.T. “Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease states” Current Med. Chem. (2005) 12(23), 2741-2751

  17. Reeder, B.J., Svistunenko, D.A., Cooper, C.E., and Wilson, M.T. “The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology”. Antioxid. Redox. Sign. (2004) 6(6), 954-966

  18. Reeder, B.J. & Wilson, M.T. “Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid” Biochem. J. (1998) 330(3), 1317-1323

  19. Rogers, M.S., Patel, R.P., Reeder, B.J, Sarti, P., Wilson, M.T. & Alayash, A.I. “Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes” Biochem. J.  (1995) 318(3), 827-833

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