-
1
-
-
0000450916
-
The oxygen equilibrium of hemoglobin and its structural interpretation
-
Pauling, L. (1935) The oxygen equilibrium of hemoglobin and its structural interpretation Proc. Natl. Acad. Sci. U. S. A. 21, 181-191
-
(1935)
Proc. Natl. Acad. Sci. U. S. A.
, vol.21
, pp. 181-191
-
-
Pauling, L.1
-
2
-
-
78651189765
-
On the natue of allosteric transitions: A plausible model
-
Monod, J., Wyman, J., and Changeux, J. P. (1965) On the natue of allosteric transitions: a plausible model J. Mol. Biol. 12, 88-118
-
(1965)
J. Mol. Biol.
, vol.12
, pp. 88-118
-
-
Monod, J.1
Wyman, J.2
Changeux, J.P.3
-
3
-
-
0013863816
-
Comparison of experimental binding data and theoretical models in proteins containing subunits
-
Koshland, D. E., Nemethy, G., and Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits Biochemistry 5, 365-385
-
(1966)
Biochemistry
, vol.5
, pp. 365-385
-
-
Koshland, D.E.1
Nemethy, G.2
Filmer, D.3
-
4
-
-
33745299907
-
Role of Na+ and K+ in enzyme function
-
Page, M. J. and Di Cera, E. (2006) Role of Na+ and K+ in enzyme function Physiol. Rev. 86, 1049-1092
-
(2006)
Physiol. Rev.
, vol.86
, pp. 1049-1092
-
-
Page, M.J.1
Di Cera, E.2
-
5
-
-
48249141040
-
Allostery and cooperativity revisited
-
Cui, Q. and Karplus, M. (2008) Allostery and cooperativity revisited Protein Sci. 17, 1295-1307
-
(2008)
Protein Sci.
, vol.17
, pp. 1295-1307
-
-
Cui, Q.1
Karplus, M.2
-
6
-
-
47649125643
-
Allosteric regulation and catalysis emerge via a common route
-
DOI 10.1038/nchembio.98, PII NCHEMBIO98
-
Goodey, N. M. and Benkovic, S. J. (2008) Allosteric regulation and catalysis emerge via a common route Nat. Chem. Biol. 4, 474-482 (Pubitemid 352019763)
-
(2008)
Nature Chemical Biology
, vol.4
, Issue.8
, pp. 474-482
-
-
Goodey, N.M.1
Benkovic, S.J.2
-
7
-
-
32344434479
-
The changing landscape of protein allostery
-
DOI 10.1016/j.sbi.2006.01.003, PII S0959440X06000042
-
Swain, J. F. and Gierasch, L. M. (2006) The changing landscape of protein allostery Curr. Opin. Struct. Biol. 16, 102-108 (Pubitemid 43221878)
-
(2006)
Current Opinion in Structural Biology
, vol.16
, Issue.1
, pp. 102-108
-
-
Swain, J.F.1
Gierasch, L.M.2
-
8
-
-
68149157248
-
The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways
-
del Sol, A., Tsai, C. J., Ma, B. Y., and Nussinov, R. (2009) The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways Structure 17, 1042-1050
-
(2009)
Structure
, vol.17
, pp. 1042-1050
-
-
Del Sol, A.1
Tsai, C.J.2
Ma, B.Y.3
Nussinov, R.4
-
9
-
-
0021658956
-
Allostery without conformational change. A plausible model
-
Cooper, A. and Dryden, D. T. (1984) Allostery without conformational change. A plausible model Eur. Biophys. J. 11, 103-109
-
(1984)
Eur. Biophys. J.
, vol.11
, pp. 103-109
-
-
Cooper, A.1
Dryden, D.T.2
-
10
-
-
33748363077
-
Dynamically driven protein allostery
-
DOI 10.1038/nsmb1132, PII NSMB1132
-
Popovych, N., Sun, S., Ebright, R. H., and Kalodimos, C. G. (2006) Dynamically driven protein allostery Nat. Struct. Mol. Biol. 13, 831-838 (Pubitemid 44338778)
-
(2006)
Nature Structural and Molecular Biology
, vol.13
, Issue.9
, pp. 831-838
-
-
Popovych, N.1
Sun, S.2
Ebright, R.H.3
Kalodimos, C.G.4
-
11
-
-
77952788560
-
Substrate-modulated thermal fluctuations affect long-range allosteric signaling in protein homodimers: Exemplified in CAP
-
Toncrova, H. and McLeish, T. C. (2010) Substrate-modulated thermal fluctuations affect long-range allosteric signaling in protein homodimers: exemplified in CAP Biophys. J. 98, 2317-2326
-
(2010)
Biophys. J.
, vol.98
, pp. 2317-2326
-
-
Toncrova, H.1
McLeish, T.C.2
-
12
-
-
67650649489
-
IMP Dehydrogenase: Structure, mechanism and inhibition
-
Hedstrom, L. (2009) IMP Dehydrogenase: structure, mechanism and inhibition Chem. Rev. 109, 2903-2928
-
(2009)
Chem. Rev.
, vol.109
, pp. 2903-2928
-
-
Hedstrom, L.1
-
13
-
-
0029899127
-
Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid
-
DOI 10.1016/S0092-8674(00)81275-1
-
Sintchak, M. D., Fleming, M. A., Futer, O., Raybuck, S. A., Chambers, S. P., Caron, P. R., Murcko, M., and Wilson, K. P. (1996) Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid Cell 85, 921-930 (Pubitemid 26192142)
-
(1996)
Cell
, vol.85
, Issue.6
, pp. 921-930
-
-
Sintchak, M.D.1
Fleming, M.A.2
Futer, O.3
Raybuck, S.A.4
Chambers, S.P.5
Caron, P.R.6
Murcko, M.A.7
Wilson, K.P.8
-
14
-
-
0347297575
-
Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site
-
DOI 10.1074/jbc.M208330200
-
Prosise, G. L., Wu, J. Z., and Luecke, H. (2002) Crystal Structure of Tritrichomonas foetus Inosine Monophosphate Dehydrogenase in Complex with the Inhibitor Ribavirin Monophosphate Reveals a Catalysis-dependent Ion-binding Site J. Biol. Chem. 277, 50654-50659 (Pubitemid 36042226)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.52
, pp. 50654-50659
-
-
Prosise, G.L.1
Zhen Wu, J.2
Luecke, H.3
-
15
-
-
0037417754
-
The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase
-
DOI 10.1021/bi0271401
-
Gan, L., Seyedsayamdost, M. R., Shuto, S., Matsuda, A., Petsko, G. A., and Hedstrom, L. (2003) The immunosuppressive agent mizoribine monophosphate forms a transition state analog complex with IMP dehydrogenase Biochemistry 42, 857-863 (Pubitemid 36159515)
-
(2003)
Biochemistry
, vol.42
, Issue.4
, pp. 857-863
-
-
Gan, L.1
Seyedsayamdost, M.R.2
Shuto, S.3
Matsuda, A.4
Petsko, G.A.5
Hedstrom, L.6
-
16
-
-
0033528674
-
Acid-base catalysis in the chemical mechanism of inosine monophosphate dehydrogenase
-
Markham, G. D., Bock, C. L., and Schalk-Hihi, C. (1999) Acid-base catalysis in the chemical mechanism of inosine monophosphate dehydrogenase Biochemistry 38, 4433-4440
-
(1999)
Biochemistry
, vol.38
, pp. 4433-4440
-
-
Markham, G.D.1
Bock, C.L.2
Schalk-Hihi, C.3
-
17
-
-
0030025627
-
Monovalent cation activation and kinetic mechanism of inosine 5′-monophosphate dehydrogenase
-
Xiang, B., Taylor, J. C., and Markham, G. D. (1996) Monovalent cation activation and kinetic mechanism of inosine 5′-monophosphate dehydrogenase J. Biol. Chem. 271, 1435-1440
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 1435-1440
-
-
Xiang, B.1
Taylor, J.C.2
Markham, G.D.3
-
18
-
-
0033616611
-
Crystal structure of human type II inosine monophosphate dehydrogenase: Implications for ligand binding and drug design
-
DOI 10.1073/pnas.96.7.3531
-
Colby, T. D., Vanderveen, K., Strickler, M. D., Markham, G. D., and Goldstein, B. M. (1999) Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design Proc. Natl. Acad. Sci. U. S. A. 96, 3531-3536 (Pubitemid 29168943)
-
(1999)
Proceedings of the National Academy of Sciences of the United States of America
, vol.96
, Issue.7
, pp. 3531-3536
-
-
Colby, T.D.1
Vanderveen, K.2
Strickler, M.D.3
Markham, G.D.4
Goldstein, B.M.5
-
19
-
-
0034163710
-
Monovalent cation activation in Escherichia coli inosine 5'- monophosphate dehydrogenase
-
DOI 10.1006/abbi.1999.1644
-
Kerr, K. M., Cahoon, M. C., Bosco, D. A., and Hedstrom, L. (2000) Monovalent cation activation in Escherichia coli IMP dehydrogenase Arch. Biochem. Biophys. 375, 131-137 (Pubitemid 30133630)
-
(2000)
Archives of Biochemistry and Biophysics
, vol.375
, Issue.1
, pp. 131-137
-
-
Kerr, K.M.1
Cahoon, M.2
Bosco, D.A.3
Hedstrom, L.4
-
20
-
-
0037027331
-
+ orients the active site loop for catalysis
-
DOI 10.1021/bi0203785
-
Gan, L., Petsko, G. A., and Hedstrom, L. (2002) Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5′-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis Biochemistry 41, 13309-13317 (Pubitemid 35244721)
-
(2002)
Biochemistry
, vol.41
, Issue.44
, pp. 13309-13317
-
-
Gan, L.1
Petsko, G.A.2
Hedstrom, L.3
-
21
-
-
0037435776
-
Crystal structures of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: A structural basis for the random-in ordered-out kinetic mechanism
-
DOI 10.1016/S0022-2836(02)01383-9
-
Prosise, G. L. and Luecke, H. (2003) Crystal Structures of Tritrichomonas foetus Inosine Monophosphate Dehydrogenase in Complex with Substrate, Cofactor and Analogs: A Structural Basis for the Random-in Ordered-out Kinetic Mechanism J. Mol. Biol. 326, 517-527 (Pubitemid 36279345)
-
(2003)
Journal of Molecular Biology
, vol.326
, Issue.2
, pp. 517-527
-
-
Prosise, G.L.1
Luecke, H.2
-
22
-
-
0030868928
-
Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex
-
DOI 10.1021/bi9708850
-
Whitby, F. G., Luecke, H., Kuhn, P., Somoza, J. R., Huete-Perez, J. A., Philips, J. D., Hill, C. P., Fletterick, R. J., and Wang, C. C. (1997) Crystal structure of Tritrichomonas foetus inosine-5′-monophosphate dehydrogenase and the enzyme-product complex Biochemistry 36, 10666-10674 (Pubitemid 27382556)
-
(1997)
Biochemistry
, vol.36
, Issue.35
, pp. 10666-10674
-
-
Whitby, F.G.1
Luecke, H.2
Kuhn, P.3
Somoza, J.R.4
Huete-Perez, J.A.5
Phillips, J.D.6
Hill, C.P.7
Fletterick, R.J.8
Wang, C.C.9
-
23
-
-
33748519900
-
IMP dehydrogenase: structural schizophrenia and an unusual base
-
DOI 10.1016/j.cbpa.2006.08.005, PII S1367593106001128, Analytical Techniques/Mechanisms
-
Hedstrom, L. and Gan, L. (2006) IMP dehydrogenase: structural schizophrenia and an unusual base Curr. Opin. Chem. Biol. 10, 520-525 (Pubitemid 44375060)
-
(2006)
Current Opinion in Chemical Biology
, vol.10
, Issue.5
, pp. 520-525
-
-
Hedstrom, L.1
Gan, L.2
-
24
-
-
0030868374
-
Allosteric properties of inosine monophosphate dehydrogenase revealed through the thermodynamics of binding of inosine 5'-monophosphate and mycophenolic acid. Temperature dependent heat capacity of binding as a signature of ligand-coupled conformational equilibria
-
DOI 10.1021/bi9708040
-
Bruzzese, F. J. and Connelly, P. R. (1997) Allosteric properties of inosine monophosphate dehydrogenase revealed through the thermodynamics of binding of inosine 5′-monphosphate and mycophenolic acid. Temperature dependent heat capacity of binding as a signature of ligand coupled conformational equilibria Biochemistry 36, 10428-10438 (Pubitemid 27374135)
-
(1997)
Biochemistry
, vol.36
, Issue.34
, pp. 10428-10438
-
-
Bruzzese, F.J.1
Connelly, P.R.2
-
25
-
-
0029741196
-
Conformational changes and stabilization of inosine 5'monophosphate dehydrogenase associated with ligand binding and inhibition by mycophenolic acid
-
DOI 10.1074/jbc.271.32.19421
-
Nimmesgern, E., Fox, T., Fleming, M. A., and Thomson, J. A. (1996) Conformational changes and stabilization of inosine 5′-monophosphate dehydrogenase associated with ligand binding and inhibition by mycophenolic acid J. Biol. Chem. 271, 19421-19427 (Pubitemid 26271615)
-
(1996)
Journal of Biological Chemistry
, vol.271
, Issue.32
, pp. 19421-19427
-
-
Nimmesgern, E.1
Fox, T.2
Fleming, M.A.3
Thomson, J.A.4
-
26
-
-
78650323744
-
The Cys319 loop modulates the transition between dehydrogenase and hydrolase conformations in IMP dehydrogenase
-
Josephine, H. R., Ravichandran, K. R., and Hedstrom, L. (2010) The Cys319 loop modulates the transition between dehydrogenase and hydrolase conformations in IMP dehydrogenase Biochemistry 49, 10674-10681
-
(2010)
Biochemistry
, vol.49
, pp. 10674-10681
-
-
Josephine, H.R.1
Ravichandran, K.R.2
Hedstrom, L.3
-
27
-
-
0017063188
-
Studies on inosine monophosphate dehydrogenase. Steady state kinetics
-
Heyde, E., Nagabhushanam, A., Vonarx, M., and Morrison, J. (1976) Studies on inosine monophosphate dehydrogenase. Steady state kinetics Biochim. Biophys. Acta 429, 645-660
-
(1976)
Biochim. Biophys. Acta
, vol.429
, pp. 645-660
-
-
Heyde, E.1
Nagabhushanam, A.2
Vonarx, M.3
Morrison, J.4
-
28
-
-
77950442655
-
The structural basis of Cryptosporidium -specific IMP dehydrogenase inhibitor selectivity
-
MacPherson, I. S., Kirubakaran, S., Gorla, S. K., Riera, T. V., DAquino, J. A., Zhang, M., Cuny, G. D., and Hedstrom, L. (2010) The structural basis of Cryptosporidium -specific IMP dehydrogenase inhibitor selectivity J. Am. Chem. Soc. 132, 1230-1231
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 1230-1231
-
-
MacPherson, I.S.1
Kirubakaran, S.2
Gorla, S.K.3
Riera, T.V.4
Daquino, J.A.5
Zhang, M.6
Cuny, G.D.7
Hedstrom, L.8
-
29
-
-
49749141064
-
A kinetic alignment of orthologous inosine-5′-monophosphate dehydrogenases
-
Riera, T. V., Wang, W., Josephine, H. R., and Hedstrom, L. (2008) A kinetic alignment of orthologous inosine-5′-monophosphate dehydrogenases Biochemistry 47, 8689-8696
-
(2008)
Biochemistry
, vol.47
, pp. 8689-8696
-
-
Riera, T.V.1
Wang, W.2
Josephine, H.R.3
Hedstrom, L.4
-
30
-
-
4644273163
-
Cryptosporidium parvum IMP dehydrogenase: Identification of functional, structural, and dynamic properties that can be exploited for drug design
-
DOI 10.1074/jbc.M407121200
-
Umejiego, N. N., Li, C., Riera, T., Hedstrom, L., and Striepen, B. (2004) Cryptosporidium parvum IMP dehydrogenase: Identification of functional, structural and dynamic properties that can be exploited for drug design J. Biol. Chem. 279, 40320-40327 (Pubitemid 39287617)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.39
, pp. 40320-40327
-
-
Umejiego, N.N.1
Li, C.2
Riera, T.3
Hedstrom, L.4
Striepen, B.5
-
31
-
-
4644298282
-
Substitution of the Conserved Arg-Tyr Dyad Selectively Disrupts the Hydrolysis Phase of the IMP Dehydrogenase Reaction
-
DOI 10.1021/bi035823q
-
Guillén Schlippe, Y. V., Riera, T. V., Seyedsayamdost, M. R., and Hedstrom, L. (2004) Substitution of the Conserved Arg-Tyr Dyad Selectively Disrupts the Hydrolysis Phase of the IMP Dehydrogenase Reaction Biochemistry 43, 4511-4521 (Pubitemid 38500580)
-
(2004)
Biochemistry
, vol.43
, Issue.15
, pp. 4511-4521
-
-
Schlippe, Y.V.G.1
Riera, T.V.2
Seyedsayamdost, M.R.3
Hedstrom, L.4
-
32
-
-
0001655657
-
Finite Representation of an Infinite Bulk System - Solvent Boundary Potential for Computer-Simulations
-
Beglov, D. and Roux, B. (1994) Finite Representation of an Infinite Bulk System-Solvent Boundary Potential for Computer-Simulations J. Chem. Phys. 100, 9050-9063
-
(1994)
J. Chem. Phys.
, vol.100
, pp. 9050-9063
-
-
Beglov, D.1
Roux, B.2
-
33
-
-
0141682863
-
Absolute binding free energies: A quantitative approach for their calculation
-
Boresch, S., Tettinger, F., Leitgeb, M., and Karplus, M. (2003) Absolute binding free energies: A quantitative approach for their calculation J. Phys. Chem. B 107, 9535-9551
-
(2003)
J. Phys. Chem. B
, vol.107
, pp. 9535-9551
-
-
Boresch, S.1
Tettinger, F.2
Leitgeb, M.3
Karplus, M.4
-
34
-
-
58149512801
-
Random walk in orthogonal space to achieve efficient free-energy simulation of complex systems
-
Zheng, L., Chen, M., and Yang, W. (2008) Random walk in orthogonal space to achieve efficient free-energy simulation of complex systems Proc. Natl. Acad. Sci. U. S. A. 105, 20227-20232
-
(2008)
Proc. Natl. Acad. Sci. U. S. A.
, vol.105
, pp. 20227-20232
-
-
Zheng, L.1
Chen, M.2
Yang, W.3
-
35
-
-
67649114369
-
Simultaneous escaping of explicit and hidden free energy barriers: Application of the orthogonal space random walk strategy in generalized ensemble based conformational sampling
-
Zheng, L., Chen, M., and Yang, W. (2009) Simultaneous escaping of explicit and hidden free energy barriers: application of the orthogonal space random walk strategy in generalized ensemble based conformational sampling J. Chem. Phys. 130, 234105
-
(2009)
J. Chem. Phys.
, vol.130
, pp. 234105
-
-
Zheng, L.1
Chen, M.2
Yang, W.3
-
37
-
-
24344510514
-
Is Arg418 the catalytic base required for the hydrolysis step of the IMP dehydrogenase reaction?
-
DOI 10.1021/bi048342v
-
Guillén Schlippe, Y. V. and Hedstrom, L. (2005) Is Arg418 the Catalytic Base Required for the Hydrolysis Step of the IMP Dehydrogenase Reaction? Biochemistry 44, 11700-11707 (Pubitemid 41262703)
-
(2005)
Biochemistry
, vol.44
, Issue.35
, pp. 11700-11707
-
-
Guillen Schlippe, Y.V.1
Hedstrom, L.2
-
38
-
-
15744377146
-
The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase
-
DOI 10.1074/jbc.M409847200
-
Kohler, G. A., Gong, X., Bentink, S., Theiss, S., Pagani, G. M., Agabian, N., and Hedstrom, L. (2005) The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase J. Biol. Chem. 280, 11295-11302 (Pubitemid 40418436)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.12
, pp. 11295-11302
-
-
Kohler, G.A.1
Gong, X.2
Bentink, S.3
Theiss, S.4
Pagani, G.M.5
Agabian, N.6
Hedstrom, L.7
-
39
-
-
0029902679
-
Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
-
DOI 10.1006/abio.1996.0238
-
Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 237, 260-273 (Pubitemid 26177089)
-
(1996)
Analytical Biochemistry
, vol.237
, Issue.2
, pp. 260-273
-
-
Kuzmic, P.1
-
40
-
-
0041784950
-
All-atom empirical potential for molecular modeling and dynamics studies of proteins
-
MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, W. E., III, Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins J. Phys. Chem. B 102, 3586-3616 (Pubitemid 128576688)
-
(1998)
Journal of Physical Chemistry B
, vol.102
, Issue.18
, pp. 3586-3616
-
-
MacKerell Jr., A.D.1
Bashford, D.2
Bellott, M.3
Dunbrack Jr., R.L.4
Evanseck, J.D.5
Field, M.J.6
Fischer, S.7
Gao, J.8
Guo, H.9
Ha, S.10
Joseph-McCarthy, D.11
Kuchnir, L.12
Kuczera, K.13
Lau, F.T.K.14
Mattos, C.15
Michnick, S.16
Ngo, T.17
Nguyen, D.T.18
Prodhom, B.19
Reiher III, W.E.20
Roux, B.21
Schlenkrich, M.22
Smith, J.C.23
Stote, R.24
Straub, J.25
Watanabe, M.26
Wiorkiewicz-Kuczera, J.27
Yin, D.28
Karplus, M.29
more..
-
41
-
-
38049034590
-
Comparative Protein Structure Modeling with MODELLER
-
(Baxevanis, A. D. Ed.) John Wiley & Sons, Inc. New York.
-
Eswar, N., Marti-Renom, M. A., Webb, B., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., and Sali, A. (2006) Comparative Protein Structure Modeling With MODELLER, in Current Protocols in Bioinformatics (Baxevanis, A. D., Ed.) pp 5.6.1-5.6.30, John Wiley & Sons, Inc., New York.
-
(2006)
Current Protocols in Bioinformatics
, pp. 561-5630
-
-
Eswar, N.1
Marti-Renom, M.A.2
Webb, B.3
Madhusudhan, M.S.4
Eramian, D.5
Shen, M.6
Pieper, U.7
Sali, A.8
-
42
-
-
77950132714
-
Simulating Monovalent and Divalent Ions in Aqueous Solution Using a Drude Polarizable Force Field
-
Yu, H. B., Whitfield, T. W., Harder, E., Lamoureux, G., Vorobyov, I., Anisimov, V. M., MacKerell, A. D., and Roux, B. (2010) Simulating Monovalent and Divalent Ions in Aqueous Solution Using a Drude Polarizable Force Field J. Chem. Theory Comput. 6, 774-786
-
(2010)
J. Chem. Theory Comput.
, vol.6
, pp. 774-786
-
-
Yu, H.B.1
Whitfield, T.W.2
Harder, E.3
Lamoureux, G.4
Vorobyov, I.5
Anisimov, V.M.6
MacKerell, A.D.7
Roux, B.8
-
43
-
-
0034681940
-
Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: Evidence of a substrate-induced hinged-lid motion by loop 6
-
DOI 10.1021/bi992645l
-
McMillan, F. M., Cahoon, M., White, A., Hedstrom, L., Petsko, G. A., and Ringe, D. (2000) Crystal structure at 2.4 Å resolution of Borrelia burgdorferi Inosine 5′-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6 Biochemistry 39, 4533-4542 (Pubitemid 30212670)
-
(2000)
Biochemistry
, vol.39
, Issue.15
, pp. 4533-4542
-
-
McMillan, F.M.1
Cahoon, M.2
White, A.3
Hedstrom, L.4
Petsko, G.A.5
Ringe, D.6
-
44
-
-
0035799367
-
Dynamics of protein ligand binding on multiple time scales: NADH binding to lactate dehydrogenase
-
DOI 10.1021/bi0026268
-
Deng, H., Zhadin, N., and Callender, R. (2001) Dynamics of protein ligand binding on multiple time scales: NADH binding to lactate dehydrogenase Biochemistry 40, 3767-3773 (Pubitemid 32280413)
-
(2001)
Biochemistry
, vol.40
, Issue.13
, pp. 3767-3773
-
-
Deng, H.1
Zhadin, N.2
Callender, R.3
-
45
-
-
23244457509
-
The approach to the Michaelis complex in lactate dehydrogenase: The substrate binding pathway
-
DOI 10.1529/biophysj.105.062604
-
McClendon, S., Zhadin, N., and Callender, R. (2005) The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway Biophys. J. 89, 2024-2032 (Pubitemid 41233557)
-
(2005)
Biophysical Journal
, vol.89
, Issue.3
, pp. 2024-2032
-
-
McClendon, S.1
Zhadin, N.2
Callender, R.3
-
46
-
-
0024358426
-
Mapping the transition state and pathway of protein folding by protein engineering
-
DOI 10.1038/340122a0
-
Matouschek, A., Kellis, J. T., Jr., Serrano, L., and Fersht, A. R. (1989) Mapping the transition state and pathway of protein folding by protein engineering Nature 340, 122-126 (Pubitemid 19175363)
-
(1989)
Nature
, vol.340
, Issue.6229
, pp. 122-126
-
-
Matouschek, A.1
Kellis Jr., J.T.2
Serrano, L.3
Fersht, A.R.4
-
47
-
-
14844320178
-
The protein folding transition state: What are φ-values really telling us?
-
DOI 10.2174/0929866053005809
-
Raleigh, D. P. and Plaxco, K. W. (2005) The protein folding transition state: what are Phi-values really telling us? Protein Pept Lett 12, 117-122 (Pubitemid 40335663)
-
(2005)
Protein and Peptide Letters
, vol.12
, Issue.2
, pp. 117-122
-
-
Raleigh, D.P.1
Plaxco, K.W.2
-
48
-
-
3343013823
-
The analysis of protein folding kinetic data produced in protein engineering experiments
-
DOI 10.1016/j.ymeth.2004.03.013, PII S1046202304000507
-
Zarrine-Afsar, A. and Davidson, A. R. (2004) The analysis of protein folding kinetic data produced in protein engineering experiments Methods 34, 41-50 (Pubitemid 38993207)
-
(2004)
Methods
, vol.34
, Issue.1
, pp. 41-50
-
-
Zarrine-Afsar, A.1
Davidson, A.R.2
-
49
-
-
0034872511
-
Transition states and the meaning of Φ-values in protein folding kinetics
-
DOI 10.1038/nsb0901-765
-
Ozkan, S. B., Bahar, I., and Dill, K. A. (2001) Transition states and the meaning of Phi-values in protein folding kinetics Nat. Struct. Biol. 8, 765-769 (Pubitemid 32803593)
-
(2001)
Nature Structural Biology
, vol.8
, Issue.9
, pp. 765-769
-
-
Ozkan, S.B.1
Bahar, I.2
Dill, K.A.3
-
50
-
-
33645809946
-
Water dynamics and salt-activation of enzymes in organic media: Mechanistic implications revealed by NMR spectroscopy
-
Eppler, R. K., Komor, R. S., Huynh, J., Dordick, J. S., Reimer, J. A., and Clark, D. S. (2006) Water dynamics and salt-activation of enzymes in organic media: mechanistic implications revealed by NMR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 103, 5706-5710
-
(2006)
Proc. Natl. Acad. Sci. U. S. A.
, vol.103
, pp. 5706-5710
-
-
Eppler, R.K.1
Komor, R.S.2
Huynh, J.3
Dordick, J.S.4
Reimer, J.A.5
Clark, D.S.6
-
51
-
-
33748628543
-
Trapped water molecules are essential to structural dynamics and function of a ribozyme
-
DOI 10.1073/pnas.0605090103
-
Rhodes, M. M., Reblova, K., Sponer, J., and Walter, N. G. (2006) Trapped water molecules are essential to structural dynamics and function of a ribozyme Proc. Natl. Acad. Sci. U. S. A. 103, 13380-13385 (Pubitemid 44380116)
-
(2006)
Proceedings of the National Academy of Sciences of the United States of America
, vol.103
, Issue.36
, pp. 13380-13385
-
-
Rhodes, M.M.1
Reblova, K.2
Sponer, J.3
Walter, N.G.4
-
52
-
-
33845252049
-
Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam
-
DOI 10.1021/bi0617355
-
OuYang, B., Pochapsky, S. S., Pagani, G. M., and Pochapsky, T. C. (2006) Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam Biochemistry 45, 14379-14388 (Pubitemid 44865194)
-
(2006)
Biochemistry
, vol.45
, Issue.48
, pp. 14379-14388
-
-
OuYang, B.1
Pochapsky, S.S.2
Pagani, G.M.3
Pochapsky, T.C.4
-
53
-
-
4444221565
-
UCSF Chimera- A visualization system for exploratory research and analysis
-
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., and Ferrin, T. E. (2004) UCSF Chimera- a visualization system for exploratory research and analysis J. Comput. Chem. 25, 1605-1612
-
(2004)
J. Comput. Chem.
, vol.25
, pp. 1605-1612
-
-
Pettersen, E.F.1
Goddard, T.D.2
Huang, C.C.3
Couch, G.S.4
Greenblatt, D.M.5
Meng, E.C.6
Ferrin, T.E.7
|