-
3
-
-
0025270551
-
Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate. NADP+ ternary complex. Substrate binding and a model for the transition state
-
Bystroff, C., Oatley, S.J., and Kraut, J. 1990. Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate. NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29: 3263-3277.
-
(1990)
Biochemistry
, vol.29
, pp. 3263-3277
-
-
Bystroff, C.1
Oatley, S.J.2
Kraut, J.3
-
4
-
-
0031443372
-
Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
-
Cameron, C.E. and Benkovic, S.J. 1997. Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36: 15792-15800.
-
(1997)
Biochemistry
, vol.36
, pp. 15792-15800
-
-
Cameron, C.E.1
Benkovic, S.J.2
-
5
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
6
-
-
0028438718
-
13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase
-
13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase. J. Biomol. NMR 4: 349-366.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 349-366
-
-
Falzone, C.J.1
Cavanagh, J.2
Cowart, M.3
Palmer, A.G.4
Matthews, C.R.5
Benkovic, S.J.6
Wright, P.E.7
-
7
-
-
0028049327
-
Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis
-
Falzone, C.J., Wright, P.E., and Benkovic, S.J. 1994b. Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis. Biochemistry 33: 439-442.
-
(1994)
Biochemistry
, vol.33
, pp. 439-442
-
-
Falzone, C.J.1
Wright, P.E.2
Benkovic, S.J.3
-
8
-
-
0023668190
-
Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
-
Fierke, C.A., Johnson, K.A., and Benkovic, S.J. 1987. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26: 4085-4092.
-
(1987)
Biochemistry
, vol.26
, pp. 4085-4092
-
-
Fierke, C.A.1
Johnson, K.A.2
Benkovic, S.J.3
-
9
-
-
0027998347
-
Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function
-
Gekko, K., Kunori, Y., Takeuchi, H., Ichihara, S., and Kodama, M. 1994. Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function. J. Biochem. 116: 34-41.
-
(1994)
J. Biochem.
, vol.116
, pp. 34-41
-
-
Gekko, K.1
Kunori, Y.2
Takeuchi, H.3
Ichihara, S.4
Kodama, M.5
-
10
-
-
0028335096
-
Structural mechanisms for domain movements in proteins
-
Gerstein, M., Lesk, A.M., and Chothia, C. 1994. Structural mechanisms for domain movements in proteins. Biochemistry 33: 6739-6749.
-
(1994)
Biochemistry
, vol.33
, pp. 6739-6749
-
-
Gerstein, M.1
Lesk, A.M.2
Chothia, C.3
-
11
-
-
9444245493
-
Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
-
Grzesiek, S. and Bax, A. 1992a. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114: 6291-6293.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 6291-6293
-
-
Grzesiek, S.1
Bax, A.2
-
12
-
-
44049117010
-
Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
-
-. 1992b. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96: 432-440.
-
(1992)
J. Magn. Reson.
, vol.96
, pp. 432-440
-
-
-
13
-
-
0027569483
-
15N-enriched proteins
-
15N-enriched proteins. J. Biomol. NMR 3: 185-204.
-
(1993)
J. Biomol. NMR
, vol.3
, pp. 185-204
-
-
-
15
-
-
0024652645
-
Nobel lecture in physiology or medicine - 1988. Selective inhibitors of dihydrofolate reductase
-
Hitchings Jr., G.H. 1989. Nobel lecture in physiology or medicine-1988. Selective inhibitors of dihydrofolate reductase. In Vitro Cell Dev. Biol. 25: 303-310.
-
(1989)
In Vitro Cell Dev. Biol.
, vol.25
, pp. 303-310
-
-
Hitchings G.H., Jr.1
-
16
-
-
0026225733
-
13C-labeled protein using constant-time evolution
-
13C-labeled protein using constant-time evolution. J. Biomol. NMR 1: 299-304.
-
(1991)
J. Biomol. NMR
, vol.1
, pp. 299-304
-
-
Ikura, M.1
Kay, L.E.2
Bax, A.3
-
17
-
-
34249765651
-
NMRView: A computer program for the visualization and analysis of NMR data
-
Johnson, B.A. and Blevins, R.A. 1994. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 603-614
-
-
Johnson, B.A.1
Blevins, R.A.2
-
18
-
-
0029881007
-
MOLMOL: A program for display and analysis of macromolecular structures
-
Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
-
(1996)
J. Mol. Graphics
, vol.14
, pp. 51-55
-
-
Koradi, R.1
Billeter, M.2
Wüthrich, K.3
-
19
-
-
0026757079
-
Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization
-
Li, L., Falzone, C.J., Wright, P.E., and Benkovic, S.J. 1992. Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization. Biochemistry 31: 7826-7833.
-
(1992)
Biochemistry
, vol.31
, pp. 7826-7833
-
-
Li, L.1
Falzone, C.J.2
Wright, P.E.3
Benkovic, S.J.4
-
21
-
-
0017785773
-
Dihydrofolate reductase: X-ray structure of the binary complex with methotrexate
-
Matthews, D.A., Alden, R.A., Bolin, J.T., Freer, S.T., Hamlin, R., Xuong, N., Kraut, J., Poe, M., Williams, M., and Hoogsteen, K. 1977. Dihydrofolate reductase: X-ray structure of the binary complex with methotrexate. Science 197: 452-455.
-
(1977)
Science
, vol.197
, pp. 452-455
-
-
Matthews, D.A.1
Alden, R.A.2
Bolin, J.T.3
Freer, S.T.4
Hamlin, R.5
Xuong, N.6
Kraut, J.7
Poe, M.8
Williams, M.9
Hoogsteen, K.10
-
22
-
-
0032485627
-
Deletion of a highly motional residue affects formation of the Michaelis complex for Escherichia coli dihydrofolate reductase
-
Miller, G.P. and Benkovic, S.J. 1998a. Deletion of a highly motional residue affects formation of the Michaelis complex for Escherichia coli dihydrofolate reductase. Biochemistry 37: 6327-6335.
-
(1998)
Biochemistry
, vol.37
, pp. 6327-6335
-
-
Miller, G.P.1
Benkovic, S.J.2
-
23
-
-
0032485865
-
Strength of an interloop hydrogen bond determines the kinetic pathway in catalysis by Escherichia coli dihydrofolate reductase
-
-. 1998b. Strength of an interloop hydrogen bond determines the kinetic pathway in catalysis by Escherichia coli dihydrofolate reductase. Biochemistry 37: 6336-6342.
-
(1998)
Biochemistry
, vol.37
, pp. 6336-6342
-
-
-
24
-
-
0035969953
-
Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase
-
Miller, G.P., Wahnon, D.C., and Benkovic, S.J. 2001. Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase. Biochemistry 40: 867-875.
-
(2001)
Biochemistry
, vol.40
, pp. 867-875
-
-
Miller, G.P.1
Wahnon, D.C.2
Benkovic, S.J.3
-
25
-
-
0035072684
-
Anisotropic rotational diffusion in model-free analysis for a ternary-DHFR complex
-
Osborne, M.J. and Wright, P.E. 2001. Anisotropic rotational diffusion in model-free analysis for a ternary-DHFR complex. J. Biomol. NMR 19: 209-230.
-
(2001)
J. Biomol. NMR
, vol.19
, pp. 209-230
-
-
Osborne, M.J.1
Wright, P.E.2
-
26
-
-
0035928796
-
Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
-
Osborne, M.J., Schnell, J., Benkovic, S.J., Dyson, H.J., and Wright, P.E. 2001. Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism. Biochemistry 40: 9846-9859.
-
(2001)
Biochemistry
, vol.40
, pp. 9846-9859
-
-
Osborne, M.J.1
Schnell, J.2
Benkovic, S.J.3
Dyson, H.J.4
Wright, P.E.5
-
27
-
-
0033955055
-
Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
-
Radkiewicz, J.L. and Brooks III, C.L. 2000. Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase. J. Am. Chem. Soc. 122: 225-231.
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 225-231
-
-
Radkiewicz, J.L.1
Brooks C.L. III2
-
28
-
-
0031015737
-
Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
-
Sawaya, M.R. and Kraut, J. 1997. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence. Biochemistry 36: 586-603.
-
(1997)
Biochemistry
, vol.36
, pp. 586-603
-
-
Sawaya, M.R.1
Kraut, J.2
-
29
-
-
0347610773
-
13C nuclear magnetic resonance chemical shifts
-
13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113: 5490-5492.
-
(1991)
J. Am. Chem. Soc.
, vol.113
, pp. 5490-5492
-
-
Spera, S.1
Bax, A.2
-
30
-
-
0026410969
-
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
-
Wishart, D.S., Sykes, B.D., and Richards, F.M. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222: 311-333.
-
(1991)
J. Mol. Biol.
, vol.222
, pp. 311-333
-
-
Wishart, D.S.1
Sykes, B.D.2
Richards, F.M.3
-
32
-
-
0029364052
-
15N chemical shift referencing in biomolecular NMR
-
15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 135-140
-
-
Wishart, D.S.1
Bigam, C.G.2
Yao, J.3
Abildgaard, F.4
Dyson, H.J.5
Oldfield, E.6
Markley, J.L.7
Sykes, B.D.8
-
33
-
-
43949167657
-
HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- and β-carbon resonances in proteins
-
Wittekind, M. and Mueller, L. 1993. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- and β-carbon resonances in proteins. J. Magn. Reson. 101: 201-205.
-
(1993)
J. Magn. Reson.
, vol.101
, pp. 201-205
-
-
Wittekind, M.1
Mueller, L.2
|