-
1
-
-
50549215335
-
Role of lactose and its metabolic products in the induction of the lactose operan in Escherichia coli
-
PMID: 14324815
-
Burstein, C., Cohn, M., Kepes, A., and Monod, J. 1965. Role of lactose and its metabolic products in the induction of the lactose operan in Escherichia coli. Biochim. Biophys. Acta, 95: 634-639. PMID: 14324815.
-
(1965)
Biochim. Biophys. Acta
, vol.95
, pp. 634-639
-
-
Burstein, C.1
Cohn, M.2
Kepes, A.3
Monod, J.4
-
2
-
-
0026711130
-
Leuconostoc Lactis β-galactosidase is encoded by two overlapping genes
-
PMID: 1624440
-
David, S., Stevens, H., van Riel, M., Simons, G., and de Vos, W.M. 1992. Leuconostoc Lactis β-galactosidase is encoded by two overlapping genes. J. Bacteriol, 174(13): 4475-4481, PMID: 1624440.
-
(1992)
J. Bacteriol
, vol.174
, Issue.13
, pp. 4475-4481
-
-
David, S.1
Stevens, H.2
Van Riel, M.3
Simons, G.4
De Vos, W.M.5
-
3
-
-
0017877333
-
Conformational adaptability of the active site of β-galactosidase. Interaction of the enzyme with some substrate analogous effectors
-
PMID:413833
-
Deschavanne, P.J., Viratelle, O.M., and Yon, J.M. 1978. Conformational adaptability of the active site of β-galactosidase. Interaction of the enzyme with some substrate analogous effectors. J. Biol. Chem. 253(3): 833-837. PMID:413833.
-
(1978)
J. Biol. Chem.
, vol.253
, Issue.3
, pp. 833-837
-
-
Deschavanne, P.J.1
Viratelle, O.M.2
Yon, J.M.3
-
4
-
-
0026437258
-
Surface denaturation of proteins: The thermal inactivation of β-galactosidase (Escherichia coli) on wall-liquid surfaces
-
doi: 10.1139/092-009. PMID:1581033
-
Edwards, R.A., and Huber, R.E. 1992. Surface denaturation of proteins: the thermal inactivation of β-galactosidase (Escherichia coli) on wall-liquid surfaces. Biochem. Cell Biol. 70(1): 63-69. doi: 10.1139/092-009. PMID:1581033.
-
(1992)
Biochem. Cell Biol.
, vol.70
, Issue.1
, pp. 63-69
-
-
Edwards, R.A.1
Huber, R.E.2
-
5
-
-
13244281317
-
Coot: Model-building tools for molecular graphics
-
doi:10.1107/S0907444904019158. PMID: 15572765
-
Emsley, P., and Cowtan, K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60(12): 2126-2132. doi:10.1107/S0907444904019158. PMID: 15572765.
-
(2004)
Acta Crystallogr. D Biol. Crystallogr.
, vol.60
, Issue.12
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
-
6
-
-
0002584126
-
Data reduction
-
Compiled by L. Sawyer, N. Isaac, and S. Bailey. CLRC Darsbury Laboratory, Warrington, England
-
Evans, P.R. 1993. Data reduction. In Proceedings of the CCP4 study weekend on data collection and processing. Compiled by L. Sawyer, N. Isaac, and S. Bailey. CLRC Darsbury Laboratory, Warrington, England, pp. 114-122.
-
(1993)
Proceedings of the CCP4 Study Weekend on Data Collection and Processing
, pp. 114-122
-
-
Evans, P.R.1
-
7
-
-
0017875606
-
Amino acid sequence of βgalactosidase. XI. Peptide ordering procedures and the complete sequence
-
PMID:97298
-
Fowler, A.V., and Zabin, I. 1978. Amino acid sequence of βgalactosidase. XI. Peptide ordering procedures and the complete sequence. J. Biol. Chem. 253(15): 5521-5525. PMID:97298.
-
(1978)
J. Biol. Chem.
, vol.253
, Issue.15
, pp. 5521-5525
-
-
Fowler, A.V.1
Zabin, I.2
-
8
-
-
0026668499
-
Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) βgalactosidase from Escherichia coli
-
PMID: 1350782
-
Gebler, J.C., Aebersold, R., and Withers, S.G. 1992. Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) βgalactosidase from Escherichia coli. J. Biol. Chem. 267(16): 11126-11130. PMID: 1350782.
-
(1992)
J. Biol. Chem.
, vol.267
, Issue.16
, pp. 11126-11130
-
-
Gebler, J.C.1
Aebersold, R.2
Withers, S.G.3
-
9
-
-
0025808918
-
Expression and nucleotide sequence of the Clostridium acetobutylicum β-galactosidase gene cloned in Escherichia coli
-
PMID: 1850729
-
Hancock, K.R., Rockman, E., Young, C.A., Pearce, L., Maddox, I.S., and Scott, D.B. 1991, Expression and nucleotide sequence of the Clostridium acetobutylicum β-galactosidase gene cloned in Escherichia coli. J. Bacteriol. 173(10): 3084-3095. PMID: 1850729.
-
(1991)
J. Bacteriol.
, vol.173
, Issue.10
, pp. 3084-3095
-
-
Hancock, K.R.1
Rockman, E.2
Young, C.A.3
Pearce, L.4
Maddox, I.S.5
Scott, D.B.6
-
10
-
-
0015228192
-
2+on the activity of β-galactosidase
-
PMID:5132913
-
2+ on the activity of β-galactosidase. Biochim. Biophys. Acta, 250(3): 530-537. PMID:5132913.
-
(1971)
Biochim. Biophys. Acta
, vol.250
, Issue.3
, pp. 530-537
-
-
Hill, J.A.1
Huber, R.E.2
-
11
-
-
0023132247
-
Strong inhibitory effect of furanoses and sugar lactones on β-galactosidase of Escherichia coli
-
doi:10.1021/bi00380a005. PMID:3109465
-
Huber, R.E., and Brockbank, R.L. 1987. Strong inhibitory effect of furanoses and sugar lactones on β-galactosidase of Escherichia coli. Biochemistry, 26(6): 1526-1531, doi:10.1021/bi00380a005. PMID:3109465.
-
(1987)
Biochemistry
, vol.26
, Issue.6
, pp. 1526-1531
-
-
Huber, R.E.1
Brockbank, R.L.2
-
12
-
-
0020702307
-
Importance of hydroxyls at positions 3, 4, and 6 for binding to the galactose site of β-galactosidase (Escherichia coli)
-
doi:10.1016/0003-9861(83)90409-5. PMID:6402986
-
Huber, R.E., and Gaunt, M.T. 1983. Importance of hydroxyls at positions 3, 4, and 6 for binding to the "galactose" site of β-galactosidase (Escherichia coli). Arch. Biochem. Biophys. 220(1): 263-271, doi:10.1016/0003-9861(83)90409-5. PMID:6402986.
-
(1983)
Arch. Biochem. Biophys.
, vol.220
, Issue.1
, pp. 263-271
-
-
Huber, R.E.1
Gaunt, M.T.2
-
13
-
-
0017170906
-
A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactose
-
doi:10.1021/bi00654a029. PMID:5122
-
Huber, R.E., Kurz, G., and Wallenfels, K. 1976. A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactose. Biochemistry, 15(9): 1994-2001. doi:10.1021/bi00654a029. PMID:5122.
-
(1976)
Biochemistry
, vol.15
, Issue.9
, pp. 1994-2001
-
-
Huber, R.E.1
Kurz, G.2
Wallenfels, K.3
-
14
-
-
0018639041
-
Interaction of divalent cations with ß-galactosidase (Escherichia coli)
-
doi: 10.1021/ bi00586a005. PMID: 114210
-
Huber, R.E., Parfett, C., Woulfe-Flanagan, H., and Thompson, D.J. 1979. Interaction of divalent cations with ß-galactosidase (Escherichia coli). Biochemistry, 18(19): 4090-4095. doi: 10.1021/ bi00586a005. PMID: 114210.
-
(1979)
Biochemistry
, vol.18
, Issue.19
, pp. 4090-4095
-
-
Huber, R.E.1
Parfett, C.2
Woulfe-Flanagan, H.3
Thompson, D.J.4
-
15
-
-
54249116230
-
Genetic regulatory mechanisms in the synthesis of proteins
-
doi: 10. 10.16/S0022-2836(61 )80072-7. PMID: 13718526
-
Jacob, F., and Monod, J. 1961. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3(3): 318-356. doi: 10. 10.16/S0022-2836(61 )80072-7. PMID: 13718526.
-
(1961)
J. Mol. Biol.
, vol.3
, Issue.3
, pp. 318-356
-
-
Jacob, F.1
Monod, J.2
-
16
-
-
0028178377
-
Three-dimensional structure of ß-galactosidase from E. coli
-
doi: 10.1038/369761 a0. PMID: 8008071
-
Jacobson, R.H., Zhang, X.J., DuBose, R.F., and Matthews, B.W. 1994. Three-dimensional structure of ß-galactosidase from E. coli. Nature, 369(6483): 761-766. doi: 10.1038/369761 a0. PMID: 8008071,
-
(1994)
Nature
, vol.369
, Issue.6483
, pp. 761-766
-
-
Jacobson, R.H.1
Zhang, X.J.2
DuBose, R.F.3
Matthews, B.W.4
-
17
-
-
0015527295
-
Lac Repressor-operator interaction. VI. The natural inducer of the lac operon
-
doi:10.1016/0022-2836(72)90253-7. PMID:4562709
-
Jobe, A., and Bourgeois, S. 1972. lac Repressor-operator interaction. VI. The natural inducer of the lac operon. J. Mol. Biol. 69(3): 397-408. doi:10.1016/0022-2836(72)90253-7. PMID:4562709.
-
(1972)
J. Mol. Biol.
, vol.69
, Issue.3
, pp. 397-408
-
-
Jobe, A.1
Bourgeois, S.2
-
18
-
-
0033820067
-
High resolution refinement of ß-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for αcomplementation
-
doi: 10.1110/ps. 9.9.1685. PMID: 11045615
-
Juers, D.H., Jacobson, R.H., Wigley, D., Zhang, X.J., Huber, R.E., Tronrud, D.E., and Matthews, B.W. 2000. High resolution refinement of ß-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for αcomplementation. Protein Sci. 9(9): 1685-1699. doi: 10.1110/ps. 9.9.1685. PMID: 11045615.
-
(2000)
Protein Sci.
, vol.9
, Issue.9
, pp. 1685-1699
-
-
Juers, D.H.1
Jacobson, R.H.2
Wigley, D.3
Zhang, X.J.4
Huber, R.E.5
Tronrud, D.E.6
Matthews, B.W.7
-
19
-
-
0035846526
-
A structural view of the action of Escherichia coli (lacZ) ß-galactosidase
-
doi:10.1021/bi011727i. PMID: 11732897
-
Juers, D.H., Heightman, T.D., Vasella, A., McCarter, J.D., Mackenzie, L., Withers, S.G., and Matthews, B.W. 2001. A structural view of the action of Escherichia coli (lacZ) ß-galactosidase. Biochemistry, 40(49): 14781-14794. doi:10.1021/bi011727i. PMID: 11732897.
-
(2001)
Biochemistry
, vol.40
, Issue.49
, pp. 14781-14794
-
-
Juers, D.H.1
Heightman, T.D.2
Vasella, A.3
McCarter, J.D.4
Mackenzie, L.5
Withers, S.G.6
Matthews, B.W.7
-
20
-
-
0344391955
-
Structural basis for the altered activity of Gly794 variants of Escherichia coli ß-galactosidase
-
doi:10.1021/bi035506j. PMID: 14621996
-
Juers, D.H., Hakda, S., Matthews, B.W., and Huber, R.E. 2003. Structural basis for the altered activity of Gly794 variants of Escherichia coli ß-galactosidase. Biochemistry, 42(46): 1350513511. doi:10.1021/bi035506j. PMID: 14621996.
-
(2003)
Biochemistry
, vol.42
, Issue.46
, pp. 1350513511
-
-
Juers, D.H.1
Hakda, S.2
Matthews, B.W.3
Huber, R.E.4
-
21
-
-
85046526624
-
Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
-
doi:10.1107/S0021889888007903
-
Kabsch, W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21(6): 916-924. doi:10.1107/S0021889888007903.
-
(1988)
J. Appl. Cryst.
, vol.21
, Issue.6
, pp. 916-924
-
-
Kabsch, W.1
-
22
-
-
0002414103
-
Crystallographic computing 5
-
Edited by D. Moras, A.D. Podjarny, and J.C. Thierry. Oxford University Press, Oxford, U.K
-
Leslie, A.G.W. 1991, Crystallographic computing 5. In Chemistry to biology. Edited by D. Moras, A.D. Podjarny, and J.C. Thierry. Oxford University Press, Oxford, U.K. pp. 50-61.
-
(1991)
Chemistry to Biology
, pp. 50-61
-
-
Leslie, A.G.W.1
-
23
-
-
0014211519
-
Synergistic activation of ßgalactosidase by Na and Cs
-
doi: 10.1016/0003-9861(67)90395-5. PMID:4860414
-
Neville, M.C., and Ling, G.N. 1967. Synergistic activation of ßgalactosidase by Na and Cs. Arch. Biochem. Biophys. 118(3): 596-610. doi: 10.1016/0003-9861(67)90395-5. PMID:4860414.
-
(1967)
Arch. Biochem. Biophys.
, vol.118
, Issue.3
, pp. 596-610
-
-
Neville, M.C.1
Ling, G.N.2
-
24
-
-
0029416990
-
Two genes encoding the ß-galactosidase of Lactobacillus sake
-
doi:10.1099/13500872-14112-3059. PMID:8574399
-
Obst, M., Meding, E.R., Vogel, R.F., and Hammes, W.P. 1995. Two genes encoding the ß-galactosidase of Lactobacillus sake. Microbiology, 141(12): 3059-3066. doi:10.1099/13500872-14112-3059. PMID:8574399.
-
(1995)
Microbiology
, vol.141
, Issue.12
, pp. 3059-3066
-
-
Obst, M.1
Meding, E.R.2
Vogel, R.F.3
Hammes, W.P.4
-
25
-
-
0026674313
-
Sequence of the Kluyveromyces lactis ß-galactosidase: Comparison with prokaryotic enzymes and secondary structure analysis
-
doi: 10.1016/03781119(92)90248-N. PMID: 1511885
-
Poch, O., L'Hôte, H., Dallery, V., Debeaux, F., Fleer, R., and Sodoyer, R. 1992. Sequence of the Kluyveromyces lactis ß-galactosidase: comparison with prokaryotic enzymes and secondary structure analysis. Gene, 118(1): 55-63. doi: 10.1016/03781119(92)90248-N. PMID: 1511885.
-
(1992)
Gene
, vol.118
, Issue.1
, pp. 55-63
-
-
Poch, O.1
L'Hôte, H.2
Dallery, V.3
Debeaux, F.4
Fleer, R.5
Sodoyer, R.6
-
26
-
-
0024538226
-
Expression and nucleotide sequence of the Lactobacillus bulgaricus ß-galactosidase gene cloned in Escherichia coli
-
PMID:2492511
-
Schmidt, B.F., Adams, R.M., Requadt, C., Power, S., and Mainzer, S.E. 1989. Expression and nucleotide sequence of the Lactobacillus bulgaricus ß-galactosidase gene cloned in Escherichia coli. J. Bacteriol. 171(2): 625-635. PMID:2492511.
-
(1989)
J. Bacteriol.
, vol.171
, Issue.2
, pp. 625-635
-
-
Schmidt, B.F.1
Adams, R.M.2
Requadt, C.3
Power, S.4
Mainzer, S.E.5
-
27
-
-
0025971587
-
Analysis of the lacZ sequences from two Streptococcus thermophilus strains: Comparison with the Escherichia coli and Lactobacillus bulgaricus ß-galactosidase sequences
-
PMID:1901904
-
Schroeder, C.J., Robert, C., Lenzen, G., McKay, L.L., and Mercenier, A. 1991. Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus ß-galactosidase sequences. J. Gen. Microbiol, 137(2): 369-380. PMID:1901904.
-
(1991)
J. Gen. Microbiol
, vol.137
, Issue.2
, pp. 369-380
-
-
Schroeder, C.J.1
Robert, C.2
Lenzen, G.3
McKay, L.L.4
Mercenier, A.5
-
28
-
-
0022377811
-
Sequence of the ebgA gene of Escherichia coli: Comparison with the lacZ gene
-
PMID:3939707
-
Stokes, H.W., Betts, P.W., and Hall, B.G. 1985. Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ gene. Mol. Biol, Evol. 2(6): 469-477. PMID:3939707.
-
(1985)
Mol. Biol, Evol.
, vol.2
, Issue.6
, pp. 469-477
-
-
Stokes, H.W.1
Betts, P.W.2
Hall, B.G.3
-
30
-
-
2542505756
-
+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of ß-galactosidase
-
doi: 10.1139/004-004. PMID: 15060622
-
+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of ß-galactosidase. Biochem. Cell Biol. 82(2): 275-284. doi: 10.1139/004-004. PMID: 15060622.
-
(2004)
Biochem. Cell Biol.
, vol.82
, Issue.2
, pp. 275-284
-
-
Xu, J.1
McRae, M.A.2
Harron, S.3
Rob, B.4
Huber, R.E.5
-
31
-
-
0028178438
-
Substitutions for Glu-537 of ß-galactosidase from Escherichia coli cause large decreases in catalytic activity
-
PMID:7909660
-
Yuan, J., Martinez-Bilbao, M., and Huber, R.E. 1994. Substitutions for Glu-537 of ß-galactosidase from Escherichia coli cause large decreases in catalytic activity. Biochem. J. 299(Pt 2): 527-531, PMID:7909660.
-
(1994)
Biochem. J.
, vol.299
, Issue.PART 2
, pp. 527-531
-
-
Yuan, J.1
Martinez-Bilbao, M.2
Huber, R.E.3
|