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Journal Abstract Search

182 related items for PubMed ID: 2242431

  • 1. Effect of hemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins: correlation with a release of hemin.
    Jarolim P, Lahav M, Liu SC, Palek J.
    Blood; 1990 Nov 15; 76(10):2125-31. PubMed ID: 2242431
    [Abstract] [Full Text] [Related]

  • 2. Involvement of methemoglobin (MetHb) formation and hemin loss in the pro-oxidant activity of fish hemoglobins.
    Maestre R, Pazos M, Medina I.
    J Agric Food Chem; 2009 Aug 12; 57(15):7013-21. PubMed ID: 19722582
    [Abstract] [Full Text] [Related]

  • 3. Disintegration of red cell membrane cytoskeleton by hemin.
    Shaklai N, Avissar N, Rabizadeh E, Shaklai M.
    Biochem Int; 1986 Sep 12; 13(3):467-77. PubMed ID: 3790141
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  • 4. Crosslinking of isolated cytoskeletal proteins with hemoglobin: a possible damage inflicted to the red cell membrane.
    Shaklai N, Frayman B, Fortier N, Snyder M.
    Biochim Biophys Acta; 1987 Oct 15; 915(3):406-14. PubMed ID: 3651479
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  • 5. Long-term intercalation of residual hemin in erythrocyte membranes distorts the cell.
    Solar I, Muller-Eberhard U, Shviro Y, Shaklai N.
    Biochim Biophys Acta; 1991 Feb 11; 1062(1):51-8. PubMed ID: 1998709
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  • 6. Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells.
    Kriebardis AG, Antonelou MH, Stamoulis KE, Economou-Petersen E, Margaritis LH, Papassideri IS.
    J Cell Mol Med; 2007 Feb 11; 11(1):148-55. PubMed ID: 17367509
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  • 8. Association of hemin with protein 4.1 as compared to spectrin and actin.
    Solar I, Shaklai N.
    Biochim Biophys Acta; 1989 Aug 07; 983(2):199-204. PubMed ID: 2758057
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  • 12. The role of membrane protein sulfhydryl groups in hydrogen peroxide-mediated membrane damage in human erythrocytes.
    Snyder LM, Fortier NL, Leb L, McKenney J, Trainor J, Sheerin H, Mohandas N.
    Biochim Biophys Acta; 1988 Jan 22; 937(2):229-40. PubMed ID: 3337802
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  • 13. Lipid oxidation in trout muscle is strongly inhibited by a protein that specifically binds hemin released from hemoglobin.
    Cai H, Grunwald EW, Park SY, Lei B, Richards MP.
    J Agric Food Chem; 2013 May 01; 61(17):4180-7. PubMed ID: 23570608
    [Abstract] [Full Text] [Related]

  • 14. Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: possibly related to the rates of hemin release.
    Chiu DT, van den Berg J, Kuypers FA, Hung IJ, Wei JS, Liu TZ.
    Free Radic Biol Med; 1996 May 01; 21(1):89-95. PubMed ID: 8791096
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  • 15. [Molecular interactions of membrane proteins and erythrocyte deformability].
    Boivin P.
    Pathol Biol (Paris); 1984 Jun 01; 32(6):717-35. PubMed ID: 6235477
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  • 16. Melatonin protects human red blood cells from oxidative hemolysis: new insights into the radical-scavenging activity.
    Tesoriere L, D'Arpa D, Conti S, Giaccone V, Pintaudi AM, Livrea MA.
    J Pineal Res; 1999 Sep 01; 27(2):95-105. PubMed ID: 10496145
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  • 17. Role of oxygen and carbon radicals in hemoglobin oxidation.
    Minetti M, Mallozzi C, Scorza G, Scott MD, Kuypers FA, Lubin BH.
    Arch Biochem Biophys; 1993 Apr 01; 302(1):233-44. PubMed ID: 8385900
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  • 18. Impaired deformability of Heinz body-forming red cells.
    Hasegawa S, Rodgers GP, Shio H, Schechter AN, Uyesaka N.
    Biorheology; 1993 Apr 01; 30(3-4):275-86. PubMed ID: 8286728
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  • 19. Hemin-mediated dissociation of erythrocyte membrane skeletal proteins.
    Liu SC, Zhai S, Lawler J, Palek J.
    J Biol Chem; 1985 Oct 05; 260(22):12234-9. PubMed ID: 4044594
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  • 20. Different types of glutathionylation of hemoglobin can exist in intact erythrocytes.
    Mawatari S, Murakami K.
    Arch Biochem Biophys; 2004 Jan 01; 421(1):108-14. PubMed ID: 14678791
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