Structure of Cu2(indomethacin)4 and the reaction with superoxide in aprotic systems.

[1]  G. Weissmann,et al.  Ceruloplasmin. A scavenger of superoxide anion radicals. , 1979, The Journal of biological chemistry.

[2]  U. Weser,et al.  Functional aspects of the superoxide dismutative action of Cu-penicillamine. , 1979, Biochimica et biophysica acta.

[3]  U. Weser,et al.  Involvement of superoxide in the catalytic cycle of diamine oxidase. , 1978, Biochimica et biophysica acta.

[4]  S. Zienau,et al.  Pulse radiolytically generated superoxide and Cu(II)-salicylates. , 1978, Biochemical and biophysical research communications.

[5]  U. Weser,et al.  Superoxide dismutase activity of copper-penicillamine: possible involvement of Cu(I) stabilized sulphur radical. , 1977, Biochemical and biophysical research communications.

[6]  A. Azzi,et al.  Hepatic microsomal dealkylations. Inhibition by a tyrosine-copper (II) complex provided with superoxide dismutase activity. , 1977, The Journal of biological chemistry.

[7]  U. Weser,et al.  Reactivity of superoxide dismutase‐active Cu(II) complexes on the rate of adrenochrome formation , 1976, FEBS letters.

[8]  R. Nalbandyan,et al.  Some properties of erythrocuprein treated by organic solvents. , 1976, Biochimica et biophysica acta.

[9]  U. Weser,et al.  Copper(I) and copper(II) in complexes of biochemical significance studied by X-ray photoelectron spectroscopy. , 1976, Biochimica et biophysica acta.

[10]  U. Weser,et al.  Inhibition of nitroblue tetrazolium reduction by cuprein (superoxide dismutase), Cu(tyr)2 and Cu(lys)2 , 1976, FEBS letters.

[11]  W. Bors,et al.  Superoxide dismutase activity of low molecular weight Cu2+‐chelates studied by pulse radiolysis , 1974, FEBS letters.

[12]  R. Cammack,et al.  "Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide. , 1973, Biochemical and biophysical research communications.

[13]  C. Djerassi,et al.  A study on purified bovine erythrocuprein. , 1971, Biochimica et biophysica acta.

[14]  R. Doedens,et al.  Crystal and molecular structure of copper(II) formate monourea , 1970 .

[15]  I. Fridovich,et al.  Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). , 1969, The Journal of biological chemistry.

[16]  D. Babel,et al.  Halbautomatische Messung des Temperaturverlaufs der magnetischen Suszeptibilität mit einer registrierenden Waage , 1967 .

[17]  E. N. Maslen,et al.  The crystal structure of Cu(II) succinate dihydrate , 1966 .

[18]  L. Packer,et al.  Effect of light on lipid peroxidation in chloroplasts. , 1965, Biochemical and biophysical research communications.

[19]  F. Hanic,et al.  The crystal structure of monopyridinecopper(II) acetate , 1964 .

[20]  E. G. Hill,et al.  The thiobarbituric acid reaction and the autoxidations of polyunsaturated fatty acid methyl esters. , 1962, Archives of biochemistry and biophysics.

[21]  F. Schoening,et al.  A new type of copper complex as found in the crystal structure of cupric acetate, Cu2(CH3COO)4.2H2O , 1953 .

[22]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[23]  M. H. Jones,et al.  The relationship of some copper (II) complexes of facultative tetrathioethers to the coordination environment in the "blue" copper proteins. , 1978, Bioinorganic chemistry.

[24]  A. Wendel,et al.  Reactivity of antiinflammatory and superoxide dismutase active Cu(II)-salicylates. , 1978, Bioinorganic chemistry.

[25]  J. Sorenson.  Copper chelates as possible active forms of the antiarthritic agents. , 1976, Journal of medicinal chemistry.

[26]  W. Bors,et al.  Superoxide dismutase activity of Cu(Tyr)2 and Cu, Co-erythrocuprein. , 1975, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

[27]  U. Weser.  Structural aspects and biochemical function of erythrocuprein , 1973 .

[28]  C. Kennard,et al.  1037. The crystal structure of monopyridinecopper(II) acetate , 1961 .

[29]  L. Pauling.  The Nature Of The Chemical Bond , 1939 .