4 Analysis of Protein Function by Mutagenesis
暂无分享,去创建一个
[1] B. Matthews,et al. Control of enzyme activity by an engineered disulfide bond. , 1994, Science.
[2] S. Benkovic,et al. A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei. , 1989, Biochemistry.
[3] C. Wong. Enzymatic catalysts in organic synthesis. , 1989, Science.
[4] M. Karplus,et al. Hidden thermodynamics of mutant proteins: a molecular dynamics analysis. , 1989, Science.
[5] A. Warshel,et al. How do serine proteases really work? , 1989, Biochemistry.
[6] S. Benkovic,et al. Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: separation of binding and catalysis. , 1989, Biochemistry.
[7] J. Kirsch,et al. Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. , 1989, Science.
[8] J. Bollinger,et al. Mechanism-based inhibition of a mutant Escherichia coli ribonucleotide reductase (cysteine-225----serine) by its substrate CDP. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[9] J. Gouaux,et al. Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanism. , 1989, Biochemistry.
[10] E. Kantrowitz,et al. A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase. , 1989, Biochemistry.
[11] S. Benkovic,et al. Probing the functional role of threonine-113 of Escherichia coli dihydrofolate reductase for its effect on turnover efficiency, catalysis, and binding. , 1989, Biochemistry.
[12] E. Haber,et al. Innovative approaches to plasminogen activator therapy. , 1989, Science.
[13] S. Benkovic,et al. Insights into Enzymic Catalysis from Studies on Dihydrofolate Reductases , 1989 .
[14] J A Wozniak,et al. Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. , 1990, Science.
[15] B. Matthews,et al. Enhanced protein thermostability from designed mutations that interact with α-helix dipoles , 1990, Nature.
[16] M. Ptashne,et al. Converting a eukaryotic transcriptional inhibitor into an activator , 1988, Cell.
[17] J. Shiver,et al. Site-directed mutagenesis of the charged residues near the carboxy terminus of the colicin E1 ion channel. , 1988, Biochemistry.
[18] T. Poulos,et al. The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. , 1988, Biochemistry.
[19] K. Nagai,et al. Coordinated amino acid changes in homologous protein families. , 1988, Protein engineering.
[20] G. Petsko,et al. Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. , 1988, Biochemistry.
[21] J. Knowles,et al. Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli. , 1988, Biochemistry.
[22] W. Lipscomb,et al. Escherichia coli aspartate transcarbamylase: the relation between structure and function. , 1988, Science.
[23] Brian W. Matthews,et al. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3 , 1988, Nature.
[24] A. Warshel,et al. Why ion pair reversal by protein engineering is unlikely to succeed , 1988, Nature.
[25] Z. Blum,et al. Enzymes and Curvature , 1988 .
[26] R. Sauer,et al. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. , 1988, Science.
[27] M J Sternberg,et al. Analysis and prediction of the location of catalytic residues in enzymes. , 1988, Protein engineering.
[28] J. Kirsch,et al. Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. , 1988, Biochemistry.
[29] J. Gerlt,et al. Identification of residues involved in a conformational change accompanying substitutions for glutamate-43 in staphylococcal nuclease. , 1988, Biochemistry.
[30] J. Wells,et al. Dissecting the catalytic triad of a serine protease , 1988, Nature.
[31] F. Blasi,et al. Artificial exon shuffling between tissue-type plasminogen activator (t-PA) and urokinase (u-PA): a comparative study on the fibrinolytic properties of t-PA/u-PA hybrid proteins. , 1988, Biochemistry.
[32] A. Fersht. Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis. , 1988, Biochemistry.
[33] A. Fersht,et al. Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism. , 1988, Biochemistry.
[34] S. Benkovic,et al. Insights into enzyme function from studies on mutants of dihydrofolate reductase. , 1988, Science.
[35] S. Cullen,et al. Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[36] A. Clarke. Protein structure, folding and design , 1988 .
[37] E. Kantrowitz,et al. A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies. , 1988, Biochemistry.
[38] J. S. Miles,et al. Site-directed mutagenesis and 1H NMR spectroscopy of an interdomain segment in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. , 1988, Biochemistry.
[39] P. Schimmel,et al. Complementary use of chemical modification and site-directed mutagenesis to probe structure-activity relationships in enzymes. , 1988, Progress in nucleic acid research and molecular biology.
[40] S. Benner,et al. Interpreting the behavior of enzymes: purpose or pedigree? , 1988, CRC critical reviews in biochemistry.
[41] B. Matthews,et al. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[42] R M Stroud,et al. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. , 1988, Science.
[43] A. Fersht,et al. Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis. , 1987, Biochemistry.
[44] M. Sternberg,et al. A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons. , 1987, Journal of molecular biology.
[45] Alan R. Fersht,et al. Prediction of electrostatic effects of engineering of protein charges , 1987, Nature.
[46] B. Matthews,et al. Genetic and structural analysis of the protein stability problem. , 1987, Biochemistry.
[47] J. Gerlt. Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis , 1987 .
[48] R J Leatherbarrow,et al. Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships. , 1987, Biochemistry.
[49] J. Gerlt,et al. Site-directed mutants of staphylococcal nuclease. Detection and localization by 1H NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43. , 1987, Biochemistry.
[50] A. Fersht,et al. Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase. , 1987, Biochemistry.
[51] B. Matthews,et al. Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. , 1987, Journal of molecular biology.
[52] J. Wells,et al. Engineering enzyme specificity by "substrate-assisted catalysis". , 1987, Science.
[53] S. Benkovic,et al. Probing the functional role of phenylalanine-31 of Escherichia coli dihydrofolate reductase by site-directed mutagenesis. , 1987, Biochemistry.
[54] B. Matthews,et al. Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein. , 1987, Biochemistry.
[55] S. Benkovic,et al. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. , 1987, Biochemistry.
[56] M. Sternberg,et al. Prediction of protein secondary structure and active sites using the alignment of homologous sequences. , 1987, Journal of molecular biology.
[57] J. Knowles. Tinkering with enzymes: what are we learning? , 1987, Science.
[58] H. K. Schachman,et al. Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. , 1987, Analytical biochemistry.
[59] W. Rutter,et al. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. , 1987, Biochemistry.
[60] A. Ashkenazi,et al. Primary structure and biochemical properties of an M2 muscarinic receptor. , 1987, Science.
[61] N. Xuong,et al. An engineered disulfide bond in dihydrofolate reductase. , 1987, Biochemistry.
[62] L. Regan,et al. Polypeptide sequences essential for RNA recognition by an enzyme. , 1987, Science.
[63] P. Brick,et al. Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. , 1987, Journal of molecular biology.
[64] R. Bott,et al. Designing substrate specificity by protein engineering of electrostatic interactions. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[65] A. Lesk,et al. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. , 1987, Journal of molecular biology.
[66] G. Petsko,et al. Control of oligomeric enzyme thermostability by protein engineering. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[67] B. Matthews,et al. Structure and thermal stability of phage T4 lysozyme. , 1987, Methods in enzymology.
[68] D. Estell. Artifacts in the application of linear free energy analysis. , 1987, Protein engineering.
[69] R. Dixon,et al. cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[70] G. Rose. Comment: Protein hydrophobicity: Is it the sum of its parts? , 1987, Proteins.
[71] J. Knowles,et al. The development of enzyme catalytic efficiency: an experimental approach. , 1987, Cold Spring Harbor symposia on quantitative biology.
[72] P. Brick,et al. Structure of a mutant of tyrosyl-tRNA synthetase with enhanced catalytic properties , 1987, Nature.
[73] H. K. Schachman,et al. Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[74] P. Hargrave,et al. Molecular biology of the visual pigments , 1986, Vision Research.
[75] Tadayuki Imanaka,et al. A new way of enhancing the thermostability of proteases , 1986, Nature.
[76] J. Knowles,et al. Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate. , 1986, Biochemistry.
[77] M. Mishina,et al. Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor , 1986, Nature.
[78] M Levitt,et al. The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure , 1986, Science.
[79] W. Fitch,et al. Molecular evolution of pancreatic-type ribonucleases. , 1986, Molecular biology and evolution.
[80] A. Fersht,et al. Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase. , 1986, Biochemistry.
[81] S J Oatley,et al. Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. , 1986, Science.
[82] J. Richards,et al. Site-saturation studies of beta-lactamase: production and characterization of mutant beta-lactamases with all possible amino acid substitutions at residue 71. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[83] K. Matsushima,et al. There is more than one interleukin 1. , 1986, Immunology today.
[84] R. Sauer,et al. Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3 , 1986 .
[85] D. Shortle,et al. Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation , 1986, Proteins.
[86] A. Fersht,et al. Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[87] M. Ptashne,et al. Changing the binding specificity of a represser by redesigning an α-helix , 1985, Nature.
[88] P. Schimmel,et al. Amino acid replacements that compensate for a large polypeptide deletion in an enzyme. , 1985, Science.
[89] C. March,et al. Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs , 1985, Nature.
[90] W Gilbert,et al. Genes-in-pieces revisited. , 1985, Science.
[91] A M Lesk,et al. Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family. , 1985, Journal of molecular biology.
[92] E. Vanin,et al. Processed pseudogenes: characteristics and evolution. , 1984, Annual review of genetics.
[93] A. C. Webb,et al. Nucleotide sequence of human monocyte interleukin 1 precursor cDNA. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[94] L. J. Perry,et al. Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation. , 1984, Science.
[95] E. Brown,et al. Substituting an α-helix switches the sequence-specific DNA interactions of a repressor , 1984, Cell.
[96] J. Nathans,et al. Isolation and nucleotide sequence of the gene encoding human rhodopsin. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[97] S. Benkovic,et al. Folates and pterins , 1984 .
[98] J. Kraut,et al. Directed mutagenesis of dihydrofolate reductase. , 1983, Science.
[99] R. Doolittle. Similar amino acid sequences: chance or common ancestry? , 1981, Science.
[100] T. Miyata,et al. Extraordinarily high evolutionary rate of pseudogenes: evidence for the presence of selective pressure against changes between synonymous codons. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[101] H. Jörnvall,et al. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[102] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[103] A. Lesk,et al. How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. , 1980, Journal of molecular biology.
[104] S. Mizel,et al. Revised nomenclature for antigen-nonspecific T cell proliferation and helper factors. , 1979, Molecular immunology.
[105] M. Anderson,et al. Chemical Recognition in Biology , 1980, Molecular Biology, Biochemistry and Biophysics.
[106] P. Bhargava,et al. A new pyrimidine-specific ribonuclease from bovine seminal plasma that is active on both single and double-stranded polyribonucleotides and that can distinguish between Mg2+-containing and Mg2+-depleted naturally occurring RNAs. , 1979, Journal of molecular biology.
[107] F. A. Cotton,et al. Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[108] H. Jörnvall. Differences between Alcohol Dehydeogenases , 1977 .
[109] G. Fermi,et al. Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. , 1975, Journal of molecular biology.
[110] G A Rogers,et al. Synthesis and evaluation of a model for the so-called "charge-relay" system of the serine esterases. , 1974, Journal of the American Chemical Society.
[111] C. Chothia,et al. Hydrophobic bonding and accessible surface area in proteins , 1974, Nature.
[112] W. Fitch,et al. The information content of protein amino acid sequences. , 1974, Annual review of biochemistry.
[113] S. Waley,et al. Refolding of triose phosphate isomerase. , 1973, The Biochemical journal.
[114] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[115] T H Jukes,et al. Evolutionary Clock: Nonconstancy of Rate in Different Species , 1972, Science.
[116] H Formanek,et al. The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin. , 1971, European journal of biochemistry.
[117] R. Huber,et al. Structures of deoxy- and carbonmonoxy-erythrocruorin. , 1970, Journal of molecular biology.
[118] J. Kraut,et al. Structure of Subtilisin BPN′ at 2.5 Å Resolution , 1969, Nature.
[119] M. Kimura. Evolutionary Rate at the Molecular Level , 1968, Nature.
[120] Harold C. Mack,et al. THE PLASMA PROTEINS , 1960 .