Possible Importance of Proteolytic Systems as Secondary Antioxidant Defenses During Ischemia-Reperfusion Injury

[1]  C. Chow.  Cellular Antioxidant Defense Mechanisms , 2019 .

[2]  A. Goldberg,et al.  Studies of the ATP dependence of protein degradation in cells and cell extracts. , 2008, Ciba Foundation symposium.

[3]  S. W. Lin,et al.  Protein damage and degradation by oxygen radicals. II. Modification of amino acids. , 1987, The Journal of biological chemistry.

[4]  K. Davies,et al.  Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. , 1987, The Journal of biological chemistry.

[5]  K. Davies.  Protein damage and degradation by oxygen radicals. I. general aspects. , 1987, The Journal of biological chemistry.

[6]  S. W. Lin,et al.  Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. , 1987, The Journal of biological chemistry.

[7]  A. Goldberg,et al.  Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells. , 1987, The Journal of biological chemistry.

[8]  A. Goldberg,et al.  Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. , 1987, The Journal of biological chemistry.

[9]  B. Halliwell.  Superoxide and superoxide dismutase in chemistry, biology and medicine : (Proceedings of the fourth international conference) , 1987 .

[10]  A. Goldberg,et al.  Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin. , 1986, The Journal of biological chemistry.

[11]  K. Davies,et al.  Uric acid-iron ion complexes. A new aspect of the antioxidant functions of uric acid. , 1986, The Biochemical journal.

[12]  E. Stadtman,et al.  Inactivation of Escherichia coli glutamine synthetase by xanthine oxidase, nicotinate hydroxylase, horseradish peroxidase, or glucose oxidase: effects of ferredoxin, putidaredoxin, and menadione. , 1985, Archives of biochemistry and biophysics.

[13]  R. Dean,et al.  Endogenous free radical generation may influence proteolysis in mitochondria. , 1985, Biochemical and biophysical research communications.

[14]  J. McCord,et al.  Oxygen-derived free radicals in postischemic tissue injury. , 1985, The New England journal of medicine.

[15]  A. Rivett,et al.  Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. , 1985, The Journal of biological chemistry.

[16]  I. Zs.-Nagy,et al.  Hydroxyl free radical reactions with amino acids and proteins studied by electron spin resonance spectroscopy and spin-trapping. , 1984, Biochimica et biophysica acta.

[17]  I. Ohad,et al.  Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[18]  E. Stadtman,et al.  Oxidative inactivation of glutamine synthetase subunits. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[19]  K. Schilling,et al.  Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin. , 1984, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[20]  M. Edelman,et al.  Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[21]  E. Shinar,et al.  The analogous mechanisms of enzymatic inactivation induced by ascorbate and superoxide in the presence of copper. , 1983, The Journal of biological chemistry.

[22]  R. Levine.  Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system. , 1983, The Journal of biological chemistry.

[23]  R. Levine.  Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue. , 1983, The Journal of biological chemistry.

[24]  B. Demple,et al.  Inducible repair of oxidative DNA damage in Escherichia coli , 1983, Nature.

[25]  A. Sevanian,et al.  The influence of phospholipase A2 and glutathione peroxidase on the elimination of membrane lipid peroxides. , 1983, Archives of biochemistry and biophysics.

[26]  A. Spector,et al.  H2O2-induced uncoupling of bovine lens Na+,K+-ATPase. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[27]  G. Boguta,et al.  Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen. , 1983, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[28]  M. J. Coon,et al.  Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[29]  J. Lunec,et al.  Fluorescence changes in human gamma-globulin induced by free-radical activity. , 1983, Biochimica et biophysica acta.

[30]  E. Melloni,et al.  Proteolysis of human reticulocyte membrane proteins: evidence for a physiological role of the acid endopeptidases. , 1982, Archives of biochemistry and biophysics.

[31]  J. M. Davies,et al.  MEMBRANE EFFECTS OF VITAMIN E DEFICIENCY: BIOENERGETIC AND SURFACE CHARGE DENSITY STUDIES OF SKELETAL MUSCLE AND LIVER MITOCHONDRIA * , 1982, Annals of the New York Academy of Sciences.

[32]  G. Brooks,et al.  Free radicals and tissue damage produced by exercise. , 1982, Biochemical and biophysical research communications.

[33]  E. Land,et al.  Charge transfer between tryptophan and tyrosine in proteins , 1982 .

[34]  A. Hipkiss,et al.  ATP-independent proteolysis of globin cyanogen bromide peptides in rabbit reticulocyte cell-free extracts. , 1982, European journal of biochemistry.

[35]  B. Ames,et al.  Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[36]  E. Stadtman,et al.  Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[37]  A. De Flora,et al.  Identification of proteolytic activities in the cytosolic compartment of mature human erythrocytes. , 1980, European journal of biochemistry.

[38]  M. Müller,et al.  Determination and characteristics of energy-dependent proteolysis in rabbit reticulocytes. , 1980, Acta biologica et medica Germanica.

[39]  M. Müller,et al.  Nitrogen economy and the metabolism of serine and glycine in reticulocytes of rabbits. , 1980, European journal of biochemistry.

[40]  A. Hipkiss,et al.  Breakdown of aberrant protein in rabbit reticulocytes decreases with cell age. , 1980, The Biochemical journal.

[41]  A Ciechanover,et al.  Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[42]  A. De Flora,et al.  Isolation and partial characterization of three acidic proteinases in erythrocyte membranes. , 1979, The Biochemical journal.

[43]  C. Tannert,et al.  The Lipoxygenase of Reticulocytes , 1979 .

[44]  W. Pryor.  Free Radicals in Biology , 1976 .

[45]  G. Adams,et al.  Selective free radical reactions with proteins and enzymes: the inactivation of alpha-chymotrypsin. , 1974, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[46]  P. Hochstein,et al.  GLUTATHIONE PEROXIDASE: THE PRIMARY AGENT FOR THE ELIMINATION OF HYDROGEN PEROXIDE IN ERYTHROCYTES. , 1963, Biochemistry.

[47]  W. Garrison,et al.  Radiation-induced oxidation of protein in aqueous solution. , 1962, Radiation research.

[48]  I. Sizer,et al.  The oxidation of tyramine, tyrosine, and related compounds by peroxidase. , 1959, The Journal of biological chemistry.

[49]  E. Stadtman.  Oxidation of proteins by mixed-function oxidation systems: implication in protein turnover, ageing and neutrophil function , 1986 .

[50]  R. Dean,et al.  Free radicals, lipids and protein degradation , 1986 .

[51]  J. McCord.  Superoxide radical: A likely link between reperfusion injury and inflammation , 1986 .

[52]  K. Davies,et al.  Intracellular proteolytic systems may function as secondary antioxidant defenses: an hypothesis. , 1986, Journal of free radicals in biology & medicine.

[53]  K. Davies,et al.  Conservation of vitamin C by uric acid in blood. , 1985, Journal of free radicals in biology & medicine.

[54]  A. Sevanian,et al.  Phospholiphase A2 dependent release of fatty acids from peroxidized membranes , 1985 .

[55]  H. Krutzsch,et al.  OH radical-induced crosslinks of methionine peptides. , 1984, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[56]  A. Ciechanover,et al.  Mechanisms of intracellular protein breakdown. , 1982, Annual review of biochemistry.

[57]  D. Evered,et al.  Protein degradation in health and disease. , 1980 .

[58]  H. Schuessler,et al.  Oxygen effect in the radiolysis of proteins. I. Lactate dehydrogenase. , 1980, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[59]  A. Goldberg,et al.  Studies of the Pathway for Protein Degradation in Escherichia coli and Mammalian Cells , 1979 .

[60]  H. Holzer,et al.  Biological Functions of Proteinases , 1979, Colloquium der Gesellschaft für Biologische Chemie 26.–28. April 1979 in Mosbach/Baden.

[61]  I. Fridovich.  CHAPTER 6 – Oxygen Radicals, Hydrogen Peroxide, and Oxygen Toxicity , 1976 .

[62]  Steven J. Steindel,et al.  4 Lactate Dehydrogenase , 1975 .

[63]  A. Goldberg,et al.  Intracellular protein degradation in mammalian and bacterial cells. , 1974, Annual review of biochemistry.

[64]  G. Adams,et al.  On the mechanism of the radiation-induced inactivation of ribonuclease in dilute aqueous solution. , 1971, International journal of radiation biology and related studies in physics, chemistry, and medicine.