Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity.
暂无分享,去创建一个
K. Britton | T. J. Stillman | D. Rice | P. Baker | A. Rob | Abdul Rob
[1] P. Karplus,et al. Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. , 1994, Journal of molecular biology.
[2] M. McPherson,et al. The glutamate dehydrogenase gene of Clotridium symbiosum , 1992 .
[3] K. Britton,et al. Subunit assembly and active site location in the structure of glutamate dehydrogenase , 1992, Proteins.
[4] K. Britton,et al. The partial amino acid sequence of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity. , 1991, Biochimica et biophysica acta.
[5] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[6] J. Kuriyan,et al. X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[7] B. Snedecor,et al. Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus , 1991, Journal of bacteriology.
[8] W. Kabsch,et al. Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607 , 1991, Nature.
[9] B. Plapp,et al. An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme. , 1991, Biochemistry.
[10] F. Quiocho,et al. High specificity of a phosphate transport protein determined by hydrogen bonds , 1990, Nature.
[11] P. Billard,et al. Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis. , 1990, Biochemistry.
[12] R. Schirmer,et al. Cloning and sequencing of mammalian glutathione reductase cDNA. , 1990, European journal of biochemistry.
[13] R. Feeney,et al. A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme. , 1990, Biochemical and biophysical research communications.
[14] Nigel S. Scrutton,et al. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering , 1990, Nature.
[15] R. Amelunxen,et al. Nucleotide sequences of genes encoding heat-stable and heat-labile glyceraldehyde-3-phosphate dehydrogenases; amino acid sequence and protein thermostability. , 1989, Gene.
[16] J L Sussman,et al. Refined crystal structure of dogfish M4 apo-lactate dehydrogenase. , 1989, Journal of molecular biology.
[17] L. Banaszak,et al. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. , 1989, Biochemistry.
[18] Israel Hanukoglu,et al. cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. , 1989, European journal of biochemistry.
[19] S. Silver,et al. Nucleotide sequence of a chromosomal mercury resistance determinant from a Bacillus sp. with broad-spectrum mercury resistance , 1989, Journal of bacteriology.
[20] T. Ohshima,et al. Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases. , 1988, Biochemistry.
[21] H. Schreuder,et al. Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate. , 1988, Journal of molecular biology.
[22] H. Kagamiyama,et al. Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. , 1987, The Journal of biological chemistry.
[23] P. Karplus,et al. Refined structure of glutathione reductase at 1.54 A resolution. , 1987, Journal of molecular biology.
[24] P C Moody,et al. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. , 1987, Journal of molecular biology.
[25] J. Hofsteenge,et al. Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. , 1982, Biochimica et biophysica acta.
[26] T. A. Jones,et al. Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution. , 1981, Journal of molecular biology.
[27] C. Brändén,et al. Relation between structure and function of α/β–protejns , 1980, Quarterly Reviews of Biophysics.
[28] H. Berendsen,et al. The α-helix dipole and the properties of proteins , 1978, Nature.
[29] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[30] S. Taylor. Amino acid sequence of dogfish muscle lactate dehydrogenase. , 1977, The Journal of biological chemistry.
[31] Michael G. Rossmann,et al. Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.
[32] H. Jörnvall. Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes. , 1970, European journal of biochemistry.
[33] A. Cerami,et al. Cloning, sequencing, and demonstration of polymorphism in trypanothione reductase from Crithidia fasciculata. , 1992, Molecular and biochemical parasitology.
[34] R. Wierenga,et al. INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS , 1985 .
[35] E. Baker,et al. Hydrogen bonding in globular proteins. , 1984, Progress in biophysics and molecular biology.
[36] H. Goodman,et al. Nopaline synthase: transcript mapping and DNA sequence. , 1982, Journal of molecular and applied genetics.