Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.
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Michael A Hough | S. Antonyuk | R. Strange | S. Hasnain | J. Valentine | P. A. Doucette | Richard W Strange | Svetlana V Antonyuk | S Samar Hasnain | Peter A Doucette | Joan Selverstone Valentine | M. Hough
[1] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[2] 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.
[3] G J Kleywegt,et al. Efficient rebuilding of protein structures. , 1996, Acta crystallographica. Section D, Biological crystallography.
[4] S. Hasnain,et al. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A. , 2003, Structure.
[5] J. Valentine,et al. Misfolded CuZnSOD and amyotrophic lateral sclerosis , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[6] T. Lyons,et al. The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis , 2000, JBIC Journal of Biological Inorganic Chemistry.
[7] Borries Demeler,et al. Dissociation of Human Copper-Zinc Superoxide Dismutase Dimers Using Chaotrope and Reductant , 2004, Journal of Biological Chemistry.
[8] A. Nersissian,et al. Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis* , 2000, The Journal of Biological Chemistry.
[9] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[10] V. Culotta,et al. A Gain of Superoxide Dismutase (SOD) Activity Obtained with CCS, the Copper Metallochaperone for SOD1* , 1999, The Journal of Biological Chemistry.
[11] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[12] A. Vagin,et al. MOLREP: an Automated Program for Molecular Replacement , 1997 .
[13] John A Tainer,et al. ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. , 2003, Journal of molecular biology.
[14] G. N. Ramachandran,et al. Stereochemistry of polypeptide chain configurations. , 1963, Journal of molecular biology.
[15] S. Antonyuk,et al. Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg , 2005, Protein science : a publication of the Protein Society.
[16] J. Rumfeldt,et al. Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[17] Gareth E. Derbyshire,et al. A low-profile monolithic multi-element Ge detector for X-ray fluorescence applications , 1999 .
[18] J. Valentine. Do oxidatively modified proteins cause ALS? , 2002, Free radical biology & medicine.
[19] L. Ellerby,et al. Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[20] L. Tibell,et al. Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[21] 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.
[22] J. Haines,et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis , 1993, Nature.
[23] 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.
[24] P. Lansbury,et al. A possible therapeutic target for Lou Gehrig's disease. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[25] Peter Briggs,et al. A graphical user interface to the CCP4 program suite. , 2003, Acta crystallographica. Section D, Biological crystallography.
[26] I. Bertini,et al. The Unusually Stable Quaternary Structure of Human Cu,Zn-Superoxide Dismutase 1 Is Controlled by Both Metal Occupancy and Disulfide Status* , 2004, Journal of Biological Chemistry.
[27] R. Strange,et al. Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function. , 2000, Journal of molecular biology.
[28] J. Valentine,et al. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. , 2005, Annual review of biochemistry.
[29] Thomas V. O'Halloran,et al. Metallochaperones, an Intracellular Shuttle Service for Metal Ions* , 2000, The Journal of Biological Chemistry.
[30] J. Thompson,et al. Decreased Zinc Affinity of Amyotrophic Lateral Sclerosis‐Associated Superoxide Dismutase Mutants Leads to Enhanced Catalysis of Tyrosine Nitration by Peroxynitrite , 1997, Journal of neurochemistry.
[31] R. Casareno,et al. The Copper Chaperone for Superoxide Dismutase* , 1997, The Journal of Biological Chemistry.
[32] M. J. Ellis,et al. A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler. , 2005, Journal of synchrotron radiation.
[33] R. Casareno,et al. The Copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide Dismutase* , 1998, The Journal of Biological Chemistry.
[34] 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.
[35] V. Culotta,et al. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[36] G. Sheldrick,et al. SHELXL: high-resolution refinement. , 1997, Methods in enzymology.
[37] W. Burmeister,et al. Structural changes in a cryo-cooled protein crystal owing to radiation damage. , 2000, Acta crystallographica. Section D, Biological crystallography.
[38] Jeffrey D. Rothstein,et al. From charcot to lou gehrig: deciphering selective motor neuron death in als , 2001, Nature Reviews Neuroscience.
[39] 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.
[40] T. O’Halloran,et al. Copper Stabilizes a Heterodimer of the yCCS Metallochaperone and Its Target Superoxide Dismutase* , 2001, The Journal of Biological Chemistry.
[41] Sarah A. Boswell,et al. Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. , 2004, Biochemistry.
[42] A. Tiwari,et al. Aberrantly Increased Hydrophobicity Shared by Mutants of Cu,Zn-Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis*♦ , 2005, Journal of Biological Chemistry.
[43] S S Hasnain,et al. Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal. , 1999, Journal of molecular biology.
[44] 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.
[45] V S Lamzin,et al. Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.
[46] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[47] 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.