Refined structure of glutathione reductase at 1.54 A resolution.
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[1] P. Stephens,et al. Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12. , 1983, European journal of biochemistry.
[2] R. Perham,et al. Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. , 1986, Biochemistry.
[3] David J. Worthington,et al. Glutathione Reductase from Human Erythrocytes , 1976 .
[4] J. L. Smith,et al. Structural heterogeneity in protein crystals. , 1986, Biochemistry.
[5] Michael G. Rossmann,et al. Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.
[6] C. Chothia,et al. Principles of protein–protein recognition , 1975, Nature.
[7] T. Bhat,et al. An analysis of side-chain conformation in proteins. , 2009, International journal of peptide and protein research.
[8] M. Karplus,et al. Molecular dynamics simulations of native and substrate-bound lysozyme. A study of the average structures and atomic fluctuations. , 1986, Journal of molecular biology.
[9] G. Schulz,et al. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase. , 1983, Journal of molecular biology.
[10] R. C. Agarwal. A new least‐squares refinement technique based on the fast Fourier transform algorithm: erratum , 1978 .
[11] R. Huber,et al. The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors , 1983 .
[12] C. J. Fritchie,et al. Geometry of the unperturbed flavin nucleus. The crystal structure of 10‐methylisoalloxazine , 1973 .
[13] R. Schirmer,et al. FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure. , 1985, European journal of biochemistry.
[14] G. Schulz,et al. On the geometry of leukocyte NADPH‐oxidase, a membrane flavoenzyme , 1983, FEBS letters.
[15] R. Wierenga,et al. INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS , 1985 .
[16] M. Karplus,et al. Restraints in temperature-factor refinement for macromolecules: an evaluation by molecuar dynamics , 1985 .
[17] E. Baker,et al. Hydrogen bonding in globular proteins. , 1984, Progress in biophysics and molecular biology.
[18] R. Parthasarathy,et al. Conformational variability of NAD+ in the free and bound states: a nicotinamide sandwich in NAD+ crystals. , 1984, Science.
[19] H. Scheraga,et al. Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids , 1975 .
[20] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[21] R. Schirmer,et al. Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. , 1982, European journal of biochemistry.
[22] G. Schulz,et al. Structural relationship between glutathione reductase and lipoamide dehydrogenase. , 1984, Journal of molecular biology.
[23] G. Schulz,et al. Three-dimensional structure of glutathione reductase at 2 A resolution. , 1981, Journal of molecular biology.
[24] J. Kraut,et al. Refinement of the crystal structure of adenosine‐5'‐phosphate , 1963 .
[25] W. Kauzmann. Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.
[26] Talapady N. Bhat,et al. OMITMAP: An electron density map suitable for the examination of errors in a macromolecular model , 1984 .
[27] W. Saenger. Structure and function of nucleosides and nucleotides. , 1973, Angewandte Chemie.
[28] B. Finzel,et al. Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 A resolution. , 1985, Journal of molecular biology.
[29] V. Luzzati,et al. Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .
[30] R. Schirmer,et al. Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. , 1977, European journal of biochemistry.
[31] R J Read,et al. Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution. , 1983, Biochemistry.
[32] G. Schulz,et al. The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. , 1983, The Journal of biological chemistry.
[33] I. G. Young,et al. Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon. , 1981, European journal of biochemistry.
[34] C. Chothia,et al. Helix to helix packing in proteins. , 1981, Journal of molecular biology.
[35] G. N. Ramachandran,et al. Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.
[36] Hans Frauenfelder,et al. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics , 1979, Nature.
[37] A. Kossiakoff. The application of neutron crystallography to the study of dynamic and and hydration properties of proteins. , 1985, Annual review of biochemistry.
[38] C. Venkatachalam. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units , 1968, Biopolymers.
[39] M. Levitt,et al. Conformation of amino acid side-chains in proteins. , 1978, Journal of molecular biology.
[40] W. Hendrickson. Stereochemically restrained refinement of macromolecular structures. , 1985, Methods in enzymology.
[41] G. Schulz,et al. FAD-binding site of glutathione reductase. , 1982, Journal of molecular biology.
[42] R. Huber,et al. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. , 1984, Journal of molecular biology.
[43] M F Schmid,et al. Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution. , 1986, Journal of molecular biology.
[44] A. Tulinsky,et al. Comparison of the independent solvent structures of dimeric alpha-chymotrypsin with themselves and with gamma-chymotrypsin. , 1985, The Journal of biological chemistry.
[45] V. Luzzati,et al. Resolution d'un structure cristalline lorsque les positions d'une partie des atoms sont connues: traitement statistique , 1953 .
[46] G. Schulz,et al. The structure of the flavoenzyme glutathione reductase , 1978, Nature.
[47] J. Thornton. Disulphide bridges in globular proteins. , 1981, Journal of molecular biology.
[48] T. Eyck,et al. Efficient structure-factor calculation for large molecules by the fast Fourier transform , 1977 .
[49] N. Brown,et al. Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase. , 1983, Biochemistry.
[50] L. Delbaere,et al. Protein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution. , 1979, Journal of molecular biology.
[51] R. J. Abraham,et al. Electrostatic potentials of the alpha helix dipole and of elastase , 1986 .
[52] P. Y. Chou,et al. β-turns in proteins☆ , 1977 .
[53] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[54] P. Coudron,et al. Hydrogen bonding between flavin and protein: a resonance Raman study. , 1983, Biochemistry.
[55] M. James,et al. Structure and refinement of penicillopepsin at 1.8 A resolution. , 1983, Journal of molecular biology.
[56] D E Tronrud,et al. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin. , 1989, European journal of biochemistry.
[57] H. Scheraga,et al. Chain reversals in proteins. , 1973, Biochimica et biophysica acta.
[58] D E Tronrud,et al. Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor. , 1983, Biochemistry.
[59] G. Schulz,et al. Crystals of human erythrocyte glutathione reductase , 1975, FEBS letters.
[60] R. Huber,et al. Structural basis of the activation and action of trypsin , 1978 .