-
1
-
-
0001093159
-
Mutational analysis of protein stability
-
Matthews, B.W. (1991) Mutational analysis of protein stability. Curr. Opin. Struct. Biol. 1, 17-21
-
(1991)
Curr. Opin. Struct. Biol.
, vol.1
, pp. 17-21
-
-
Matthews, B.W.1
-
2
-
-
0027462173
-
Principles of protein stability derived from protein engineering experiments
-
Fersht, A.R. and Serrano, L. (1993) Principles of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3, 75-83
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 75-83
-
-
Fersht, A.R.1
Serrano, L.2
-
3
-
-
0029932580
-
Analysis of protein conformational characteristics related to thermostability
-
Quinol, E., Perez-Pons, J.A., and Mozo-Villarias, A. (1996) Analysis of protein conformational characteristics related to thermostability. Protein Eng. 9, 265-271
-
(1996)
Protein Eng.
, vol.9
, pp. 265-271
-
-
Quinol, E.1
Perez-Pons, J.A.2
Mozo-Villarias, A.3
-
4
-
-
0016257544
-
Distribution of the isopropylmalate pathway to leucine among diverse bacteria
-
Stieglitz, B.I. and Calvo, J.M. (1974) Distribution of the isopropylmalate pathway to leucine among diverse bacteria. J. Bacteriol. 118, 935-941
-
(1974)
J. Bacteriol.
, vol.118
, pp. 935-941
-
-
Stieglitz, B.I.1
Calvo, J.M.2
-
5
-
-
0018821820
-
Phenotypic and genotypic characterization of some thermophilic species of Bacillus
-
Sharp, R.J., Bown, K.J., and Atkinson, A. (1980) Phenotypic and genotypic characterization of some thermophilic species of Bacillus. J. Gen. Microbiol. 117, 201-210
-
(1980)
J. Gen. Microbiol.
, vol.117
, pp. 201-210
-
-
Sharp, R.J.1
Bown, K.J.2
Atkinson, A.3
-
6
-
-
0021762398
-
Cloning of β-isopropylmalate dehydrogenase from Bacillus coagulans in Escherichia coli and purification and properties of the enzyme
-
Sekiguchi, T., Harada, Y., Shishido, K., and Nosoh, Y. (1984) Cloning of β-isopropylmalate dehydrogenase from Bacillus coagulans in Escherichia coli and purification and properties of the enzyme. Biochim. Biophys. Acta 788, 267-273
-
(1984)
Biochim. Biophys. Acta
, vol.788
, pp. 267-273
-
-
Sekiguchi, T.1
Harada, Y.2
Shishido, K.3
Nosoh, Y.4
-
7
-
-
0031567156
-
Crystal structure of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus
-
Wallon, G., Kryger, G., Lovett, S.T., Oshima, T., Ringe, D., and Petsko, G.A. (1997) Crystal structure of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. J. Mol. Biol. 266, 1016-1031
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 1016-1031
-
-
Wallon, G.1
Kryger, G.2
Lovett, S.T.3
Oshima, T.4
Ringe, D.5
Petsko, G.A.6
-
8
-
-
0030484258
-
Crystallization and preliminary x-ray analysis of 3-isopropylmalate dehydrogenase from the moderate facultative thermophile, Bacillus coagulans
-
Tsuchiya, D., Matsumoto, O., Gorai, T., Sekiguchi, T., Nosoh, Y., and Takenaka, A. (1996) Crystallization and preliminary x-ray analysis of 3-isopropylmalate dehydrogenase from the moderate facultative thermophile, Bacillus coagulans. Acta Cryst. D52, 1030-1032
-
(1996)
Acta Cryst.
, vol.D52
, pp. 1030-1032
-
-
Tsuchiya, D.1
Matsumoto, O.2
Gorai, T.3
Sekiguchi, T.4
Nosoh, Y.5
Takenaka, A.6
-
9
-
-
0000293676
-
X-ray diffraction data collection system for modern protein crystallography with a weissenberg camera and an imaging plate using synchrotron radiation
-
Sakabe, N. (1991) X-ray diffraction data collection system for modern protein crystallography with a weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods A303, 448-463
-
(1991)
Nucl. Instrum. Methods
, vol.A303
, pp. 448-463
-
-
Sakabe, N.1
-
10
-
-
0002193613
-
The processing of diffraction data taken on a screenless weissenberg camera for macromolecular crystallography
-
Higashi, T. (1989) The processing of diffraction data taken on a screenless weissenberg camera for macromolecular crystallography. J. Appl. Cryst. 22, 9-18
-
(1989)
J. Appl. Cryst.
, vol.22
, pp. 9-18
-
-
Higashi, T.1
-
11
-
-
0028103275
-
The CCP4 suite: Programs for protein crystallography
-
Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763
-
(1994)
Acta Cryst.
, vol.D50
, pp. 760-763
-
-
-
12
-
-
0026334204
-
Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
-
Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y., and Oshima, T. (1991) Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J. Mol. Biol. 222, 725-738
-
(1991)
J. Mol. Biol.
, vol.222
, pp. 725-738
-
-
Imada, K.1
Sato, M.2
Tanaka, N.3
Katsube, Y.4
Matsuura, Y.5
Oshima, T.6
-
13
-
-
84920325457
-
AMoRe: An automated package for molecular replacement
-
Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Cryst. A50, 157-163
-
(1994)
Acta Cryst.
, vol.A50
, pp. 157-163
-
-
Navaza, J.1
-
14
-
-
0031887010
-
omit profile analysis for molecular replacements
-
in press
-
omit profile analysis for molecular replacements. Acta Cryst. D54, in press
-
(1998)
Acta Cryst.
, vol.D54
-
-
Tsuchiya, D.1
Takenaka, A.2
-
15
-
-
0000858864
-
SQUASH - Combining constraints for macromolecular phase refinement and extension
-
Zhang, K.Y.J. (1993) SQUASH - Combining constraints for macromolecular phase refinement and extension. Acta Cryst. D49, 213-222
-
(1993)
Acta Cryst.
, vol.D49
, pp. 213-222
-
-
Zhang, K.Y.J.1
-
16
-
-
84889120137
-
Improved methods for building protein models in electron density maps and the location of errors in these models
-
Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119
-
(1991)
Acta Cryst.
, vol.A47
, pp. 110-119
-
-
Jones, T.A.1
Zou, J.Y.2
Cowan, S.W.3
Kjeldgaard, M.4
-
18
-
-
0026597444
-
Free-R value: A novel statistical quantity for assessing the accuracy of crystal structures
-
Br̈nger, A.T. (1992) Free-R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
-
(1992)
Nature
, vol.355
, pp. 472-475
-
-
Br̈nger, A.T.1
-
19
-
-
0026655361
-
Stereochemical quality of protein structure coordinates
-
Morris, A.L., MacArthur, M.W., Hutchinson, E.G., and Thornton, J.M. (1992) Stereochemical quality of protein structure coordinates. Proteins 12, 345-364
-
(1992)
Proteins
, vol.12
, pp. 345-364
-
-
Morris, A.L.1
MacArthur, M.W.2
Hutchinson, E.G.3
Thornton, J.M.4
-
20
-
-
0022494658
-
DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae and Thermus thermophilus
-
Sekiguchi, T., Ortega-Cesena, J., Nosoh, Y., Ohashi, S., Tsuda, K., and Kanaya, S. (1986) DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae and Thermus thermophilus. Biochim. Biophys. Acta 867, 36-44
-
(1986)
Biochim. Biophys. Acta
, vol.867
, pp. 36-44
-
-
Sekiguchi, T.1
Ortega-Cesena, J.2
Nosoh, Y.3
Ohashi, S.4
Tsuda, K.5
Kanaya, S.6
-
21
-
-
0001099937
-
Traitement statistique des erreurs dans la determination des structures cristallines
-
Luzzati, P.V. (1952) Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810
-
(1952)
Acta Cryst.
, vol.5
, pp. 802-810
-
-
Luzzati, P.V.1
-
22
-
-
0026240806
-
Ribbons 2.0
-
Carson, M. (1991) Ribbons 2.0. J. Appl. Cryst. 24, 958-961
-
(1991)
J. Appl. Cryst.
, vol.24
, pp. 958-961
-
-
Carson, M.1
-
23
-
-
0021326794
-
High guanine plus cytosine content in third letter of codons of an extreme thermophile
-
Kagawa, Y., Nojima, H., Nukiwa, N., Ishizuka, M., Nakajima, T., Yasuhara, T., Tanaka, T., and Oshima, T. (1984) High guanine plus cytosine content in third letter of codons of an extreme thermophile. J. Biol. Chem. 259, 2956-2960
-
(1984)
J. Biol. Chem.
, vol.259
, pp. 2956-2960
-
-
Kagawa, Y.1
Nojima, H.2
Nukiwa, N.3
Ishizuka, M.4
Nakajima, T.5
Yasuhara, T.6
Tanaka, T.7
Oshima, T.8
-
24
-
-
0023664575
-
The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus subtilis
-
Imai, R., Sekiguchi, T., Nosoh, Y., and Tsuda, K. (1987) The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus subtilis. Nucleic Acids Res. 15, 4988
-
(1987)
Nucleic Acids Res.
, vol.15
, pp. 4988
-
-
Imai, R.1
Sekiguchi, T.2
Nosoh, Y.3
Tsuda, K.4
-
25
-
-
0028774536
-
+: Ligand-induced loop closing and mechanism for cofactor specificity
-
+: ligand-induced loop closing and mechanism for cofactor specificity. Structure 2, 1007-1016
-
(1994)
Structure
, vol.2
, pp. 1007-1016
-
-
Hurley, J.H.1
Dean, A.M.2
-
26
-
-
0028853604
-
Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus
-
Kadono, S., Sakurai, M., Moriyama, H., Sato, M., Hayashi, Y., Oshima, T., and Tanaka, N. (1995) Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus. J. Biochem. 118, 745-752
-
(1995)
J. Biochem.
, vol.118
, pp. 745-752
-
-
Kadono, S.1
Sakurai, M.2
Moriyama, H.3
Sato, M.4
Hayashi, Y.5
Oshima, T.6
Tanaka, N.7
-
27
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis, P.J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950
-
(1991)
J. Appl. Cryst.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
28
-
-
0023430560
-
Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
-
Matthews, B.W., Nicholson, H., and Becktel, W.J. (1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA 84, 6663-6667
-
(1987)
Proc. Natl. Acad. Sci. USA
, vol.84
, pp. 6663-6667
-
-
Matthews, B.W.1
Nicholson, H.2
Becktel, W.J.3
-
29
-
-
0026099553
-
Role of conserved proline residues in stabilizing tryptophan synthase α subunit: Analysis by mutants with alanine or glycine
-
Yutani, K., Hayashi, S., Sugisaki, Y., and Ogasahara, K. (1991) Role of conserved proline residues in stabilizing tryptophan synthase α subunit: analysis by mutants with alanine or glycine. Proteins 9, 90-98
-
(1991)
Proteins
, vol.9
, pp. 90-98
-
-
Yutani, K.1
Hayashi, S.2
Sugisaki, Y.3
Ogasahara, K.4
-
30
-
-
0028130117
-
Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase
-
Watanabe, K., Masuda, T., Ohashi, H., Mihara, H., and Suzuki, Y. (1994) Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Eur. J. Biochem. 226, 277-283
-
(1994)
Eur. J. Biochem.
, vol.226
, pp. 277-283
-
-
Watanabe, K.1
Masuda, T.2
Ohashi, H.3
Mihara, H.4
Suzuki, Y.5
-
31
-
-
0018788367
-
Thermal stability and protein structure
-
Argos, P., Rossmann, M.G., Grau, U.M., Zuber, H., Frank, G., and Tratschin, J.D. (1979) Thermal stability and protein structure. Biochemistry 18, 5698-5703
-
(1979)
Biochemistry
, vol.18
, pp. 5698-5703
-
-
Argos, P.1
Rossmann, M.G.2
Grau, U.M.3
Zuber, H.4
Frank, G.5
Tratschin, J.D.6
-
32
-
-
0027535130
-
Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability
-
Ishikawa, K., Kimura, S., Kanaya, S., Morikawa, K., and Nakamura, H. (1993) Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability. Protein Eng. 6, 85-91
-
(1993)
Protein Eng.
, vol.6
, pp. 85-91
-
-
Ishikawa, K.1
Kimura, S.2
Kanaya, S.3
Morikawa, K.4
Nakamura, H.5
-
33
-
-
0028147704
-
Role of cysteine residues in esterase from Bacillus stearothermophilus and increasing its thermostability by the replacement of cysteines
-
Amaki, Y., Nakano, H., and Yamane, T. (1994) Role of cysteine residues in esterase from Bacillus stearothermophilus and increasing its thermostability by the replacement of cysteines. Appl. Microbiol. Biotechnol. 40, 664-668
-
(1994)
Appl. Microbiol. Biotechnol.
, vol.40
, pp. 664-668
-
-
Amaki, Y.1
Nakano, H.2
Yamane, T.3
-
34
-
-
0018094892
-
Electrostatic effects in proteins
-
Perutz, M.F. (1978) Electrostatic effects in proteins. Science 201, 1187-1191
-
(1978)
Science
, vol.201
, pp. 1187-1191
-
-
Perutz, M.F.1
-
35
-
-
0028994307
-
2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
-
Hennig, M., Darimont, B., Sterner, R., Kirschner, K., and Jansonius, J.N. (1995) 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structures 3, 1295-1306
-
(1995)
Structures
, vol.3
, pp. 1295-1306
-
-
Hennig, M.1
Darimont, B.2
Sterner, R.3
Kirschner, K.4
Jansonius, J.N.5
-
36
-
-
13244249836
-
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks maintaining enzyme stability at extreme temperatures
-
Yip, K.S.P., Stillman, T.J., Britton, K.L., Artymiuk, P.J., Baker, P.J., Sedelnikova, S.E., Engel, P.C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R., and Rice, D.W. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks maintaining enzyme stability at extreme temperatures. Structures 3, 1147-1158
-
(1995)
Structures
, vol.3
, pp. 1147-1158
-
-
Yip, K.S.P.1
Stillman, T.J.2
Britton, K.L.3
Artymiuk, P.J.4
Baker, P.J.5
Sedelnikova, S.E.6
Engel, P.C.7
Pasquo, A.8
Chiaraluce, R.9
Consalvi, V.10
Scandurra, R.11
Rice, D.W.12
-
37
-
-
0027156651
-
Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from thermophilic bacterium Thermus flavus
-
Kelly, C.A., Nishiyama, M., Ohnishi, Y., Beppu, T., and Birktoft, J. (1993) Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from thermophilic bacterium Thermus flavus. Biochemistry 32, 3913-3922
-
(1993)
Biochemistry
, vol.32
, pp. 3913-3922
-
-
Kelly, C.A.1
Nishiyama, M.2
Ohnishi, Y.3
Beppu, T.4
Birktoft, J.5
-
38
-
-
0029936488
-
Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution
-
Tanner, J.N., Hecht, R.M., and Krause, K.L. (1996) Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution. Biochemistry 35, 2597-2609
-
(1996)
Biochemistry
, vol.35
, pp. 2597-2609
-
-
Tanner, J.N.1
Hecht, R.M.2
Krause, K.L.3
-
39
-
-
0023645203
-
Interior and surface of monomeric proteins
-
Miller, S., Janin, J., Lesk, A.M., and Chothia, C. (1987) Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656
-
(1987)
J. Mol. Biol.
, vol.196
, pp. 641-656
-
-
Miller, S.1
Janin, J.2
Lesk, A.M.3
Chothia, C.4
-
40
-
-
0025718955
-
Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
-
Dao-pin, S., Sauer, U., Nicholson, H., and Matthews, B.W. (1991) Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30, 7142-7153
-
(1991)
Biochemistry
, vol.30
, pp. 7142-7153
-
-
Dao-pin, S.1
Sauer, U.2
Nicholson, H.3
Matthews, B.W.4
-
42
-
-
0024972479
-
Capping and α-helix stability
-
Serrano, L. and Fersht, A.R. (1989) Capping and α-helix stability. Nature 342, 296-299
-
(1989)
Nature
, vol.342
, pp. 296-299
-
-
Serrano, L.1
Fersht, A.R.2
-
43
-
-
0024273441
-
Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
-
Nicholson, H., Becktel, W.J., and Matthews, B.W. (1988) Enhanced protein thermostability from designed mutations that interact with α-helix dipoles. Nature 336, 651-656
-
(1988)
Nature
, vol.336
, pp. 651-656
-
-
Nicholson, H.1
Becktel, W.J.2
Matthews, B.W.3
-
44
-
-
0026674251
-
α-Helix stability in proteins: II. Factors that influence stability at an internal position
-
Horovitz, A., Matthews, J.M., and Fersht, A.R. (1992) α-Helix stability in proteins: II. Factors that influence stability at an internal position. J. Mol. Biol. 227, 560-568
-
(1992)
J. Mol. Biol.
, vol.227
, pp. 560-568
-
-
Horovitz, A.1
Matthews, J.M.2
Fersht, A.R.3
-
45
-
-
0025222978
-
A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
-
O'Neil, K.T. and DeGrado, W.F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250, 646-651
-
(1990)
Science
, vol.250
, pp. 646-651
-
-
O'Neil, K.T.1
DeGrado, W.F.2
-
46
-
-
0023368698
-
Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α subunit
-
Yutani, K., Ogasahara, K., Tsujita, T., and Sugino, Y. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α subunit. Proc. Natl. Acad. Sci. USA 84, 4441-4444
-
(1987)
Proc. Natl. Acad. Sci. USA
, vol.84
, pp. 4441-4444
-
-
Yutani, K.1
Ogasahara, K.2
Tsujita, T.3
Sugino, Y.4
-
47
-
-
0027485997
-
Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala→Ser and Val→Thr substitutions in T4 lysozyme
-
Blaber, M., Lindstrom, J.D., Gassner, N., Xu, J., Heinz, D.W., and Matthews, B.W. (1993) Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala→Ser and Val→Thr substitutions in T4 lysozyme. Biochemistry 32, 11363-11373
-
(1993)
Biochemistry
, vol.32
, pp. 11363-11373
-
-
Blaber, M.1
Lindstrom, J.D.2
Gassner, N.3
Xu, J.4
Heinz, D.W.5
Matthews, B.W.6
-
48
-
-
0024295240
-
Contribution of hydrophobic interactions to protein stability
-
Kellis, J.T., Jr., Nyberg, K., Sali, D., and Fersht, A.R. (1988) Contribution of hydrophobic interactions to protein stability. Nature 333, 784-786
-
(1988)
Nature
, vol.333
, pp. 784-786
-
-
Kellis Jr., J.T.1
Nyberg, K.2
Sali, D.3
Fersht, A.R.4
-
49
-
-
0028091179
-
Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
-
Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., and Oshima, T. (1994) Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur. J. Biochem. 220, 275-281
-
(1994)
Eur. J. Biochem.
, vol.220
, pp. 275-281
-
-
Kirino, H.1
Aoki, M.2
Aoshima, M.3
Hayashi, Y.4
Ohba, M.5
Yamagishi, A.6
Wakagi, T.7
Oshima, T.8
-
50
-
-
0027995683
-
Detection, delineation, measurement and display of cavities in macromolecular structures
-
Kleywegt, G.J. and Jones, T.A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst. D50, 178-185
-
(1994)
Acta Cryst.
, vol.D50
, pp. 178-185
-
-
Kleywegt, G.J.1
Jones, T.A.2
-
51
-
-
0028961901
-
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
-
Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W.W., and Rees, D.C. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267, 1463-1469
-
(1995)
Science
, vol.267
, pp. 1463-1469
-
-
Chan, M.K.1
Mukund, S.2
Kletzin, A.3
Adams, M.W.W.4
Rees, D.C.5
-
52
-
-
0028986679
-
Thermal stability of chimeric isopropyl-malate dehydrogenase genes constructed from a thermophile and a mesophile
-
Numata, K., Muro, M., Akutsu, N., Nosoh, Y., Yamagishi, A., and Oshima, T. (1995) Thermal stability of chimeric isopropyl-malate dehydrogenase genes constructed from a thermophile and a mesophile. Protein Eng. 8, 39-45
-
(1995)
Protein Eng.
, vol.8
, pp. 39-45
-
-
Numata, K.1
Muro, M.2
Akutsu, N.3
Nosoh, Y.4
Yamagishi, A.5
Oshima, T.6
-
53
-
-
0028774720
-
The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum
-
Russell, R.J.M., Hough, D.W., Danson, M.J., and Taylor, G.L. (1994) The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum. Structure 2, 1157-1167
-
(1994)
Structure
, vol.2
, pp. 1157-1167
-
-
Russell, R.J.M.1
Hough, D.W.2
Danson, M.J.3
Taylor, G.L.4
-
54
-
-
0030589056
-
Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritina
-
Macedo-Ribeiro, S., Darimont, B., Sterner, R., and Huber, R. (1996) Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritina. Structure 4, 1291-1301
-
(1996)
Structure
, vol.4
, pp. 1291-1301
-
-
Macedo-Ribeiro, S.1
Darimont, B.2
Sterner, R.3
Huber, R.4
-
55
-
-
0029979578
-
Crystal structure at 2.3 Å resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1
-
Knegtel, R.M.A., Wind, R.D., Rozeboom, H.J., Kalk, K.H., Buitelaar, R.M., Dijkhuizen, L., and Dijkstra, B.W. (1996) Crystal structure at 2.3 Å resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Mol. Biol. 256, 611-622
-
(1996)
J. Mol. Biol.
, vol.256
, pp. 611-622
-
-
Knegtel, R.M.A.1
Wind, R.D.2
Rozeboom, H.J.3
Kalk, K.H.4
Buitelaar, R.M.5
Dijkhuizen, L.6
Dijkstra, B.W.7
-
56
-
-
0001767586
-
A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases
-
Suzuki, Y., Oishi, K., Nakano, H., and Nagayama, T. (1987) A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol. 26, 546-551
-
(1987)
Appl. Microbiol. Biotechnol.
, vol.26
, pp. 546-551
-
-
Suzuki, Y.1
Oishi, K.2
Nakano, H.3
Nagayama, T.4
-
57
-
-
0028206870
-
Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606
-
Nakao, M., Nakayama, T., Kakudo, A., Inohara, M., Harada, M., Omura, F., and Shibano, Y. (1994) Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606. Eur. J. Biochem. 220, 293-300
-
(1994)
Eur. J. Biochem.
, vol.220
, pp. 293-300
-
-
Nakao, M.1
Nakayama, T.2
Kakudo, A.3
Inohara, M.4
Harada, M.5
Omura, F.6
Shibano, Y.7
-
58
-
-
0024413884
-
Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution
-
Birktoft, J.J., Rhodes, G., and Banaszak, L.J. (1989) Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution. Biochemistry 28, 6065-6081
-
(1989)
Biochemistry
, vol.28
, pp. 6065-6081
-
-
Birktoft, J.J.1
Rhodes, G.2
Banaszak, L.J.3
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