Inhibition of erythrocyte's catalase, glutathione peroxidase or peroxiredoxin 2 - Impact on cytosol and membrane.

[1]  L. Belo,et al.  Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis. , 2019, Biochimica et biophysica acta. Biomembranes.

[2]  M. H. Hadwan,et al.  Simple spectrophotometric assay for measuring catalase activity in biological tissues , 2018, BMC Biochemistry.

[3]  T. Ganz,et al.  Peroxiredoxin-2: A Novel Regulator of Iron Homeostasis in Ineffective Erythropoiesis. , 2018, Antioxidants & redox signaling.

[4]  C. Cooper,et al.  The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane , 2017, Free radical biology & medicine.

[5]  Simone Bayer,et al.  Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane , 2016, Free radical research.

[6]  Pranjal Chandra,et al.  Biomarkers of oxidative stress in erythrocytes as a function of human age. , 2015, World journal of methodology.

[7]  A. Santos-Silva,et al.  Peroxiredoxin 2, glutathione peroxidase, and catalase in the cytosol and membrane of erythrocytes under H2O2-induced oxidative stress , 2015, Free radical research.

[8]  He Li,et al.  Erythrocyte membrane model with explicit description of the lipid bilayer and the spectrin network. , 2014, Biophysical journal.

[9]  S. Foote,et al.  Treatment of Erythrocytes with the 2-Cys Peroxiredoxin Inhibitor, Conoidin A, Prevents the Growth of Plasmodium falciparum and Enhances Parasite Sensitivity to Chloroquine , 2014, PloS one.

[10]  S. Perrotta,et al.  Membrane association of peroxiredoxin-2 in red cells is mediated by the N-terminal cytoplasmic domain of band 3. , 2013, Free radical biology & medicine.

[11]  A. D’Alessandro,et al.  Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics , 2012, Haematologica.

[12]  J. Loscalzo,et al.  Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. , 2011, Antioxidants & redox signaling.

[13]  L. Zolla,et al.  Peroxiredoxin‐2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions , 2011, Transfusion.

[14]  L. Zolla,et al.  Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions. , 2011, Biochimie.

[15]  S. Rhee,et al.  Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells. , 2010, Antioxidants & redox signaling.

[16]  Philip W. Kuchel,et al.  Glutathione Synthesis and Turnover in the Human Erythrocyte , 2010, The Journal of Biological Chemistry.

[17]  Y. Ravindranath,et al.  The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism. , 2010, Free radical biology & medicine.

[18]  A. Slawin,et al.  Optimisation of Conoidin A, a Peroxiredoxin Inhibitor , 2010, ChemMedChem.

[19]  Albert J R Heck,et al.  Quantitative erythrocyte membrane proteome analysis with Blue-native/SDS PAGE. , 2010, Journal of proteomics.

[20]  J. Cullen,et al.  Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue , 2010, Nature Protocols.

[21]  S. Müller,et al.  IDENTIFICATION OF CONOIDIN A AS A COVALENT INHIBITOR OF PEROXIREDOXIN II. , 2009, Organic & biomolecular chemistry.

[22]  L. Belo,et al.  Linkage of cytosolic peroxiredoxin 2 to erythrocyte membrane imposed by hydrogen peroxide-induced oxidative stress. , 2009, Blood cells, molecules & diseases.

[23]  M. Trujillo,et al.  The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2. , 2009, Archives of biochemistry and biophysics.

[24]  R. Vitorino,et al.  Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis. , 2008, Blood cells, molecules & diseases.

[25]  M. Çimen,et al.  Free radical metabolism in human erythrocytes. , 2008, Clinica chimica acta; international journal of clinical chemistry.

[26]  C. Winterbourn,et al.  The High Reactivity of Peroxiredoxin 2 with H2O2 Is Not Reflected in Its Reaction with Other Oxidants and Thiol Reagents* , 2007, Journal of Biological Chemistry.

[27]  C. Winterbourn,et al.  Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. , 2007, Blood.

[28]  J. Umbreit.  Methemoglobin—It's not just blue: A concise review , 2007, American journal of hematology.

[29]  Sang Yeol Lee,et al.  Two Enzymes in One Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function , 2004, Cell.

[30]  J J Strain,et al.  The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": the FRAP assay. , 1996, Analytical biochemistry.

[31]  L. Borg,et al.  A spectrophotometric method for determination of catalase activity in small tissue samples. , 1988, Analytical biochemistry.

[32]  N. Shaklai,et al.  The association of human erythrocyte catalase with the cell membrane. , 1981, Archives of biochemistry and biophysics.

[33]  O. Griffith,et al.  Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. , 1980, Analytical biochemistry.

[34]  M. Uchiyama,et al.  Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. , 1978, Analytical biochemistry.

[35]  D. W. Allen,et al.  Increased membrane binding of erythrocyte catalase in hereditary spherocytosis and in metabolically stressed normal cells. , 1977, Blood.

[36]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[37]  L. Flohé,et al.  Glutathione peroxidase: A selenoenzyme , 1973, FEBS letters.

[38]  J. Dodge,et al.  The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. , 1963, Archives of biochemistry and biophysics.