Dissociation of Human Copper-Zinc Superoxide Dismutase Dimers Using Chaotrope and Reductant
暂无分享,去创建一个
Borries Demeler | Xiaohang Cao | P. John Hart | J. Valentine | P. Hart | J. Hansen | P. A. Doucette | Lisa J. Whitson | B. Demeler | Joan Selverstone Valentine | Jeffrey C. Hansen | V. Schirf | Virgil Schirf | Peter A. Doucette | Xiaohang Cao | L. J. Whitson | Xiaohang Cao | Joan Selverstone Valentine | P. Hart | Jeffrey C. Hansen
[1] T. O’Halloran,et al. Oxygen‐induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS , 2004, The EMBO journal.
[2] J Günter Grossmann,et al. Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[3] A. Chakrabartty,et al. Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis*[boxs] , 2004, Journal of Biological Chemistry.
[4] S. Tu,et al. Kinetic mechanism and quaternary structure of Aminobacter aminovorans NADH:flavin oxidoreductase: an unusual flavin reductase with bound flavin. , 2004, Biochemistry.
[5] Jennifer Stine Elam,et al. Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS , 2003, Nature Structural Biology.
[6] Michael A Hough,et al. The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. , 2003, Journal of molecular biology.
[7] J. Valentine,et al. Misfolded CuZnSOD and amyotrophic lateral sclerosis , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[8] A. Tiwari,et al. Familial Amyotrophic Lateral Sclerosis Mutants of Copper/Zinc Superoxide Dismutase Are Susceptible to Disulfide Reduction* , 2003, The Journal of Biological Chemistry.
[9] I. Bertini,et al. Structure and dynamics of copper‐free SOD: The protein before binding copper , 2002, Protein science : a publication of the Protein Society.
[10] D. Borchelt,et al. Fibrillar Inclusions and Motor Neuron Degeneration in Transgenic Mice Expressing Superoxide Dismutase 1 with a Disrupted Copper-Binding Site , 2002, Neurobiology of Disease.
[11] Robert H. Brown,et al. Decreased Metallation and Activity in Subsets of Mutant Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis* 210 , 2002, The Journal of Biological Chemistry.
[12] Robert H. Brown,et al. Familial Amyotrophic Lateral Sclerosis-associated Mutations Decrease the Thermal Stability of Distinctly Metallated Species of Human Copper/Zinc Superoxide Dismutase* , 2002, The Journal of Biological Chemistry.
[13] A. Lamb,et al. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone , 2001, Nature Structural Biology.
[14] A. Rosato,et al. Backbone dynamics of human Cu,Zn superoxide dismutase and of its monomeric F50E/G51E/E133Q mutant: the influence of dimerization on mobility and function. , 2000, Biochemistry.
[15] L. T. Hall,et al. X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery. , 2000, Biochemistry.
[16] J. García de la Torre,et al. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. , 2000, Biophysical journal.
[17] P. Selvin,et al. A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry. , 1999, Analytical biochemistry.
[18] M. Ferraroni,et al. The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited. , 1999, Journal of molecular biology.
[19] R M Esnouf,et al. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. , 1999, Acta crystallographica. Section D, Biological crystallography.
[20] M Bolognesi,et al. Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase. , 1999, Journal of molecular biology.
[21] L. Bruijn,et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. , 1998, Science.
[22] Marco Di Benedetto,et al. Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?. , 1998, Biochemistry.
[23] T. Lyons,et al. The dark side of dioxygen biochemistry. , 1998, Current opinion in chemical biology.
[24] A. Pesce,et al. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. , 1997, Journal of molecular biology.
[25] R. Casareno,et al. The Copper Chaperone for Superoxide Dismutase* , 1997, The Journal of Biological Chemistry.
[26] G. Rotilio,et al. The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins. , 1996, The Biochemical journal.
[27] J. Tainer,et al. Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[28] W. Hung,et al. Intense Superoxide Dismutase‐1 Immunoreactivity in Intracytoplasmic Hyaline Inclusions of Familial Amyotrophic Lateral Sclerosis with Posterior Column Involvement , 1996, Journal of neuropathology and experimental neurology.
[29] D. Eisenberg,et al. Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase. , 1996, Biochemistry.
[30] D. Bredesen,et al. Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis , 1996, Science.
[31] I. Bertini,et al. Synthesis and characterization of a monomeric mutant Cu/Zn superoxide dismutase with partially reconstituted enzymic activity. , 1995, European journal of biochemistry.
[32] K. Davies. Oxidative stress: the paradox of aerobic life. , 1995, Biochemical Society symposium.
[33] G. Rotilio,et al. Isolation of an active and heat‐stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli , 1995, FEBS letters.
[34] M. Bolognesi,et al. Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 A resolution. , 1995, Acta crystallographica. Section D, Biological crystallography.
[35] R. Schlapbach,et al. Oxidants in mitochondria: from physiology to diseases. , 1995, Biochimica et biophysica acta.
[36] D. Borchelt,et al. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[37] J. Hansen,et al. Analytical ultracentrifugation of complex macromolecular systems. , 1994, Biochemistry.
[38] Joan C. Han,et al. A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol. , 1994, Analytical biochemistry.
[39] K. Inouye,et al. Dissociation of dimer of bovine erythrocyte Cu,Zn-superoxide dismutase and activity of the monomer subunit: effects of urea, temperature, and enzyme concentration. , 1994, Journal of biochemistry.
[40] E. Gratton,et al. Molten globule monomers in human superoxide dismutase. , 1993, Biophysical chemistry.
[41] M. Pericak-Vance,et al. Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. , 1993, Science.
[42] J. Haines,et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis , 1993, Nature.
[43] E. Gratton,et al. Denaturation of human Cu/Zn superoxide dismutase by guanidine hydrochloride: a dynamic fluorescence study. , 1992, Biochemistry.
[44] J. Tainer,et al. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[45] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[46] G. Whitesides,et al. SELECTIVE REDUCTION OF DISULFIDES BY TRIS(2-CARBOXYETHYL) PHOSPHINE , 1991 .
[47] K. Asada,et al. Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution. , 1991, Journal of biochemistry.
[48] G. Habermehl,et al. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha. , 1989, The Biochemical journal.
[49] I. Fridovich. Superoxide dismutases: an adaptation to a paramagnetic gas , 1989 .
[50] Peter A. Kollman,et al. Electrostatic recognition between superoxide and copper, zinc superoxide dismutase , 1983, Nature.
[51] J. Richardson,et al. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. , 1980, Journal of molecular biology.
[52] I. Fridovich,et al. Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents. , 1979, Biochemistry.
[53] G. Rotilio,et al. Dissociation of Cu–Zn superoxide dismutase into monomers by urea , 1978, FEBS letters.
[54] K. V. van Holde,et al. Boundary analysis of sedimentation‐velocity experiments with monodisperse and paucidisperse solutes , 1978 .
[55] J. V. Bannister,et al. Active subunits from superoxide dismutase. , 1978, Biochemical and biophysical research communications.
[56] G. Rotilio,et al. On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germ. , 1978, Biochemistry.
[57] R. Hill,et al. Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond. , 1974, The Journal of biological chemistry.
[58] G. Rotilio,et al. Enzyme activity of superoxide dismutase protomers , 1974, FEBS letters.
[59] I. Fridovich,et al. Isozymes of superoxide dismutase from wheat germ. , 1973, Biochimica et biophysica acta.
[60] J. Fee. Studies on the reconstitution of bovine erythrocyte superoxide dismutase. IV. Preparation and some properties of the enzyme in which Co(II) is substituted for Zn(II). , 1973, The Journal of biological chemistry.
[61] I. Fridovich,et al. On the stability of bovine superoxide dismutase. The effects of metals. , 1973, The Journal of biological chemistry.
[62] I. Fridovich,et al. The role of superoxide radical in a nonenzymatic hydroxylation. , 1972, Archives of biochemistry and biophysics.
[63] H. F. Deutsch,et al. Subunit structure of human superoxide dismutase. , 1972, The Journal of biological chemistry.
[64] R. Carrico,et al. The presence of zinc in human cytocuprein and some properties of the apoprotein. , 1970, The Journal of biological chemistry.
[65] J. Kirkwood,et al. Proteins, amino acids and peptides as ions and dipolar ions , 1943 .
[66] I. Bertini,et al. A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase , 2005, European Biophysics Journal.
[67] P. Sadler,et al. Medicinal Inorganic Chemistry , 1999 .
[68] S. Cannistraro,et al. Incoherent neutron scattering of copper azurin: a comparison with molecular dynamics simulation results , 1999, European Biophysics Journal.
[69] J. Hansen,et al. Identification and interpretation of complexity in sedimentation velocity boundaries. , 1997, Biophysical journal.
[70] Arthur J. Rowe,et al. Analytical ultracentrifugation in biochemistry and polymer science , 1992 .