Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution.
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M. Wilce | J. Guss | D. Dooley | J M Guss | H C Freeman | M C Wilce | D M Dooley | V Kumar | I Harvey | M A McGuirl | V M Zubak | H. C. Freeman | I. Harvey | M. McGuirl | V. Kumar | V. M. Zubak | V. Kumar | V. Kumar | M.C.J. Wilce | Vinay Kumar | David M. Dooley | Hans C. Freeman | Ian Harvey
[1] Doreen E. Brown,et al. Intramolecular electron transfer in the oxidation of amines by methylamine oxidase from Arthrobacter P1 , 1996, JBIC Journal of Biological Inorganic Chemistry.
[2] E. Agostinelli,et al. Half-of-the-sites reactivity of bovine serum amine oxidase. Reactivity and chemical identity of the second site. , 1996, European journal of biochemistry.
[3] M. R. Parsons,et al. Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. , 1995, Structure.
[4] H. Eklund,et al. Copper amine oxidase: a novel use for a tyrosine. , 1995, Structure.
[5] J. Klinman,et al. Model Studies of Topaquinone-Dependent Amine Oxidases. 1. Oxidation of Benzylamine by Topaquinone Analogs , 1995 .
[6] J. Klinman,et al. Model Studies of Topaquinone-Dependent Amine Oxidases. 2. Characterization of Reaction Intermediates and Mechanism , 1995 .
[7] M. McPherson,et al. Cloning and Molecular Analysis of the Pea Seedling Copper Amine Oxidase (*) , 1995, The Journal of Biological Chemistry.
[8] G J Kleywegt,et al. Where freedom is given, liberties are taken. , 1995, Structure.
[9] J. Klinman,et al. Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. , 1994, The Journal of biological chemistry.
[10] D. Dooley,et al. Purification and Characterization of Pea Seedling Amine Oxidase for Crystallization Studies , 1994, Plant physiology.
[11] Y. Ozaki,et al. Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion‐dependent autooxidation of a specific tyrosyl residue , 1994, FEBS letters.
[12] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[13] A. Korn,et al. Torsion angle differences as a means of pinpointing local polypeptide chain trajectory changes for identical proteins in different conformational states. , 1994, Protein engineering.
[14] D. Dooley,et al. Structure of the Topa-semiquinone Catalytic Intermediate of Amine Oxidase as Revealed by Magnetic Interactions with Exchangeable 2H and 1H Nuclei , 1994 .
[15] M. Lazdunski,et al. Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. , 1994, The Journal of biological chemistry.
[16] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[17] J. Janin,et al. Orientation of non-crystallographic symmetry axes in protein crystals. , 1993, Acta crystallographica. Section D, Biological crystallography.
[18] C. Orengo,et al. Alpha plus beta folds revisited: some favoured motifs. , 1993, Structure.
[19] D. Dooley,et al. Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase. , 1993, The Journal of biological chemistry.
[20] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[21] J. Guss,et al. Crystallization and preliminary crystallographic characterization of the copper-containing amine oxidase from pea seedlings. , 1993, Journal of molecular biology.
[22] R. Medda,et al. Lentil seedling amine oxidase: interaction with carbonyl reagents. , 1992, Biochemistry international.
[23] D. Grandjean,et al. Structure of tris(3,3',4,4'-tetramethyl-2,2',5,5'-tetraselenafulvalenium) phosphododecatungstate: (TMTSF)3PW12O40 , 1991 .
[24] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[25] N. Sakabe. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation , 1991 .
[26] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[27] P. Knowles,et al. A Cu(I)-semiquinone state in substrate-reduced amine oxidases , 1991, Nature.
[28] A T Brünger,et al. Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.
[29] P. Knowles,et al. Studies on the active site of pig plasma amine oxidase. , 1989, The Biochemical journal.
[30] M. Artico,et al. Spectroscopic studies of the reaction between bovine serum amine oxidase (copper-containing) and some hydrazides and hydrazines. , 1988, The Biochemical journal.
[31] D. Dooley,et al. Cu(II) coordination chemistry of amine oxidases: pulsed EPR studies of histidine imidazole, water, and exogenous ligand coordination , 1987 .
[32] R. Read. Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .
[33] D. Dooley,et al. X-ray absorption spectroscopic studies of the copper (II) sites in bovine plasma amine oxidase , 1985 .
[34] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[35] G. Floris,et al. Essential sulfhydryl groups in diamine oxidase from Euphorbia characias latex. , 1983, Archives of biochemistry and biophysics.
[36] K. Watanabe,et al. Electron spin resonance studies of bovine plasma amine oxidase. Probing of the environment about the substrate-liberated sulfhydryl groups in the active site. , 1980, The Journal of biological chemistry.
[37] H. Schenk,et al. Computing in Crystallography , 1978 .
[38] R. Abeles,et al. Studies on the mechanism of action of plasma amine oxidase. , 1978, Biochemistry.
[39] P. Knowles,et al. Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity. , 1976, The Biochemical journal.
[40] B. Matthews. Solvent content of protein crystals. , 1968, Journal of molecular biology.
[41] V. Luzzati,et al. Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .
[42] J. Klinman,et al. Quinoenzymes in biology. , 1994, Annual review of biochemistry.
[43] D. Dooley,et al. Purification and characterization of pea seedling amine oxidase for crystallizaiton studies , 1994 .
[44] G J Barton,et al. ALSCRIPT: a tool to format multiple sequence alignments. , 1993, Protein engineering.
[45] V. Davidson. Principles and Applications of Quinoproteins , 1993 .
[46] C. E. Cote,et al. Coordination chemistry of copper-containing amine oxidases: nuclear magnetic relaxation dispersion studies of copper binding, solvent-water exchange, substrate and inhibitor binding, and protein aggregation , 1991 .
[47] A. Finazzi-Agro’. Copper-Containing Amine Oxidases , 1989 .
[48] David Eisenberg,et al. Generalized method of determining heavy-atom positions using the difference Patterson function , 1987 .