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Volumn 8, Issue 8, 2012, Pages 2949-2961

Exploring residue component contributions to dynamical network models of allostery

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EID: 84865063074     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct300377a     Document Type: Article
Times cited : (146)

References (60)
  • 1
    • 79959334490 scopus 로고    scopus 로고
    • 50th anniversary of the word "allosteric"
    • Changeux, J. P. 50th anniversary of the word "allosteric" Protein Sci. 2011, 20, 1119-24
    • (2011) Protein Sci. , vol.20 , pp. 1119-1124
    • Changeux, J.P.1
  • 2
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J.; Changeux, J. P.; Jacob, F. Allosteric proteins and cellular control systems J. Mol. Biol. 1963, 6, 306-29
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 3
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J.; Wyman, J.; Changeux, J. P. On the Nature of Allosteric Transitions: A Plausible Model J. Mol. Biol. 1965, 12, 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 4
    • 0014014862 scopus 로고
    • On the nature of allosteric transitions: Implications of non-exclusive ligand binding
    • Rubin, M. M.; Changeux, J. P. On the nature of allosteric transitions: implications of non-exclusive ligand binding J. Mol. Biol. 1966, 21, 265-74
    • (1966) J. Mol. Biol. , vol.21 , pp. 265-274
    • Rubin, M.M.1    Changeux, J.P.2
  • 5
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel, G. M.; Lockless, S. W.; Wall, M. A.; Ranganathan, R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins Nat. Struct. Biol. 2003, 10, 59-69
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 6
    • 33745860948 scopus 로고    scopus 로고
    • Evolutionarily conserved allosteric network in the Cys loop family of ligand-gated ion channels revealed by statistical covariance analyses
    • Chen, Y.; Reilly, K.; Chang, Y. Evolutionarily conserved allosteric network in the Cys loop family of ligand-gated ion channels revealed by statistical covariance analyses J. Biol. Chem. 2006, 281, 18184-92
    • (2006) J. Biol. Chem. , vol.281 , pp. 18184-18192
    • Chen, Y.1    Reilly, K.2    Chang, Y.3
  • 7
    • 33745461893 scopus 로고    scopus 로고
    • Residues crucial for maintaining short paths in network communication mediate signaling in proteins
    • del Sol, A.; Fujihashi, H.; Amoros, D.; Nussinov, R. Residues crucial for maintaining short paths in network communication mediate signaling in proteins Mol. Syst. Biol. 2006, 2, 1-12
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 1-12
    • Del Sol, A.1    Fujihashi, H.2    Amoros, D.3    Nussinov, R.4
  • 8
    • 33847609615 scopus 로고    scopus 로고
    • A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase
    • Amaro, R. E.; Sethi, A.; Myers, R. S.; Davisson, V. J.; Luthey-Schulten, Z. A. A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase Biochemistry 2007, 46, 2156-73
    • (2007) Biochemistry , vol.46 , pp. 2156-2173
    • Amaro, R.E.1    Sethi, A.2    Myers, R.S.3    Davisson, V.J.4    Luthey-Schulten, Z.A.5
  • 9
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S. W.; Ranganathan, R. Evolutionarily conserved pathways of energetic connectivity in protein families Science 1999, 286, 295-9
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 10
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D. E., Jr.; Nemethy, G.; Filmer, D. Comparison of experimental binding data and theoretical models in proteins containing subunits Biochemistry 1966, 5, 365-85
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 11
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux, J. P.; Edelstein, S. J. Allosteric mechanisms of signal transduction Science 2005, 308, 1424-8
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 12
    • 41149104308 scopus 로고    scopus 로고
    • Allostery: Absence of a change in shape does not imply that allostery is not at play
    • Tsai, C. J.; del Sol, A.; Nussinov, R. Allostery: absence of a change in shape does not imply that allostery is not at play J. Mol. Biol. 2008, 378, 1-11
    • (2008) J. Mol. Biol. , vol.378 , pp. 1-11
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 13
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey, N. M.; Benkovic, S. J. Allosteric regulation and catalysis emerge via a common route Nat. Chem. Biol. 2008, 4, 474-82
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 14
    • 41049092674 scopus 로고    scopus 로고
    • Coupling between global dynamics and signal transduction pathways: A mechanism of allostery for chaperonin GroEL
    • Chennubhotla, C.; Yang, Z.; Bahar, I. Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroEL Mol. Biosyst. 2008, 4, 287-92
    • (2008) Mol. Biosyst. , vol.4 , pp. 287-292
    • Chennubhotla, C.1    Yang, Z.2    Bahar, I.3
  • 15
    • 0021658956 scopus 로고
    • Allostery without Conformational Change - A Plausible Model
    • Cooper, A.; Dryden, D. T. F. Allostery without Conformational Change-a Plausible Model Eur. Biophys. J. Biophys. Lett. 1984, 11, 103-109
    • (1984) Eur. Biophys. J. Biophys. Lett. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 16
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M. R.; Wells, J. A. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Nat. Rev. Drug Discovery 2004, 3, 301-17
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 17
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G.; Szabo, A. Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules. 1. Theory and Range of Validity J. Am. Chem. Soc. 1982, 104, 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 18
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G.; Szabo, A. Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules. 2. Analysis of Experimental Results J. Am. Chem. Soc. 1982, 104, 4559-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 19
    • 78149500243 scopus 로고    scopus 로고
    • Using NMR to study fast dynamics in proteins: Methods and applications
    • Sapienza, P. J.; Lee, A. L. Using NMR to study fast dynamics in proteins: methods and applications Curr. Opin. Pharmacol. 2010, 10, 723-30
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 723-730
    • Sapienza, P.J.1    Lee, A.L.2
  • 20
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • Yang, D.; Kay, L. E. Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding J. Mol. Biol. 1996, 263, 369-82
    • (1996) J. Mol. Biol. , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.E.2
  • 23
    • 0033515432 scopus 로고    scopus 로고
    • Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3
    • Horstink, L. M.; Abseher, R.; Nilges, M.; Hilbers, C. W. Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3 J. Mol. Biol. 1999, 287, 569-77
    • (1999) J. Mol. Biol. , vol.287 , pp. 569-577
    • Horstink, L.M.1    Abseher, R.2    Nilges, M.3    Hilbers, C.W.4
  • 24
    • 33745782784 scopus 로고    scopus 로고
    • Comparison of coupled motions in Escherichia coli and Bacillus subtilis dihydrofolate reductase
    • Watney, J. B.; Hammes-Schiffer, S. Comparison of coupled motions in Escherichia coli and Bacillus subtilis dihydrofolate reductase J. Phys. Chem. B 2006, 110, 10130-8
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10130-10138
    • Watney, J.B.1    Hammes-Schiffer, S.2
  • 25
    • 42649130377 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the Escherichia coli NikR protein: Equilibrium conformational fluctuations reveal interdomain allosteric communication pathways
    • Bradley, M. J.; Chivers, P. T.; Baker, N. A. Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways J. Mol. Biol. 2008, 378, 1155-73
    • (2008) J. Mol. Biol. , vol.378 , pp. 1155-1173
    • Bradley, M.J.1    Chivers, P.T.2    Baker, N.A.3
  • 26
    • 33644847828 scopus 로고    scopus 로고
    • Generalized correlation for biomolecular dynamics
    • Lange, O. F.; Grubmuller, H. Generalized correlation for biomolecular dynamics Proteins 2006, 62, 1053-61
    • (2006) Proteins , vol.62 , pp. 1053-1061
    • Lange, O.F.1    Grubmuller, H.2
  • 27
    • 34547227692 scopus 로고    scopus 로고
    • Extraction of configurational entropy from molecular simulations via an expansion approximation
    • Killian, B. J.; Yundenfreund Kravitz, J.; Gilson, M. K. Extraction of configurational entropy from molecular simulations via an expansion approximation J. Chem. Phys. 2007, 127, 024107
    • (2007) J. Chem. Phys. , vol.127 , pp. 024107
    • Killian, B.J.1    Yundenfreund Kravitz, J.2    Gilson, M.K.3
  • 32
    • 0025777753 scopus 로고
    • The catalytic mechanism of the amidotransferase domain of the Syrian hamster multifunctional protein CAD. Evidence for a CAD-glutamyl covalent intermediate in the formation of carbamyl phosphate
    • Chaparian, M. G.; Evans, D. R. The catalytic mechanism of the amidotransferase domain of the Syrian hamster multifunctional protein CAD. Evidence for a CAD-glutamyl covalent intermediate in the formation of carbamyl phosphate J. Biol. Chem. 1991, 266, 3387-95
    • (1991) J. Biol. Chem. , vol.266 , pp. 3387-3395
    • Chaparian, M.G.1    Evans, D.R.2
  • 33
    • 0026643934 scopus 로고
    • P-aminobenzoate synthesis in Escherichia coli: Kinetic and mechanistic characterization of the amidotransferase PabA
    • Roux, B.; Walsh, C. T. p-aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA Biochemistry 1992, 31, 6904-10
    • (1992) Biochemistry , vol.31 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 34
    • 0028821816 scopus 로고
    • The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine
    • Nakamura, J.; Straub, K.; Wu, J.; Lou, L. The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine J. Biol. Chem. 1995, 270, 23450-5
    • (1995) J. Biol. Chem. , vol.270 , pp. 23450-23455
    • Nakamura, J.1    Straub, K.2    Wu, J.3    Lou, L.4
  • 35
    • 0037715142 scopus 로고    scopus 로고
    • Thr-431 and Arg-433 are part of a conserved sequence motif of the glutamine amidotransferase domain of CTP synthases and are involved in GTP activation of the Lactococcus lactis enzyme
    • Willemoes, M. Thr-431 and Arg-433 are part of a conserved sequence motif of the glutamine amidotransferase domain of CTP synthases and are involved in GTP activation of the Lactococcus lactis enzyme J. Biol. Chem. 2003, 278, 9407-11
    • (2003) J. Biol. Chem. , vol.278 , pp. 9407-9411
    • Willemoes, M.1
  • 36
    • 0034284955 scopus 로고    scopus 로고
    • Structural evidence for evolution of the β/α barrel scaffold by gene duplication and fusion
    • Lang, D.; Thoma, R.; Henn-Sax, M.; Sterner, R.; Wilmanns, M. Structural evidence for evolution of the β/α barrel scaffold by gene duplication and fusion Science 2000, 289, 1546-50
    • (2000) Science , vol.289 , pp. 1546-1550
    • Lang, D.1    Thoma, R.2    Henn-Sax, M.3    Sterner, R.4    Wilmanns, M.5
  • 37
    • 0037938734 scopus 로고    scopus 로고
    • Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase
    • Myers, R. S.; Jensen, J. R.; Deras, I. L.; Smith, J. L.; Davisson, V. J. Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase Biochemistry 2003, 42, 7013-22
    • (2003) Biochemistry , vol.42 , pp. 7013-7022
    • Myers, R.S.1    Jensen, J.R.2    Deras, I.L.3    Smith, J.L.4    Davisson, V.J.5
  • 40
    • 0038614879 scopus 로고    scopus 로고
    • Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: Crystal structures of a ternary complex and the free enzyme
    • Chaudhuri, B. N.; Lange, S. C.; Myers, R. S.; Davisson, V. J.; Smith, J. L. Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme Biochemistry 2003, 42, 7003-12
    • (2003) Biochemistry , vol.42 , pp. 7003-7012
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Davisson, V.J.4    Smith, J.L.5
  • 41
    • 84945708259 scopus 로고
    • A theorem on boolean matrices
    • Warshall, S., A Theorem on Boolean Matrices. J. Assoc. Comput. Mach. 1962, 9, 11.
    • (1962) J. Assoc. Comput. Mach. , vol.9 , pp. 11
    • Warshall, S.1
  • 42
    • 84945709831 scopus 로고
    • Algorithm-97 - Shortest Path
    • Floyd, R. W. Algorithm-97-Shortest Path Commun. ACM 1962, 5, 345-345
    • (1962) Commun. ACM , vol.5 , pp. 345-345
    • Floyd, R.W.1
  • 43
    • 0037062448 scopus 로고    scopus 로고
    • Community structure in social and biological networks
    • Girvan, M.; Newman, M. E. Community structure in social and biological networks Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 7821-6
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7821-7826
    • Girvan, M.1    Newman, M.E.2
  • 44
    • 79251535315 scopus 로고    scopus 로고
    • Graphical analysis of pH-dependent properties of proteins predicted using PROPKA
    • not supplied
    • Michaø, R.; Mats, O. Graphical analysis of pH-dependent properties of proteins predicted using PROPKA. BMC Struct. Biol. 2011, not supplied.
    • (2011) BMC Struct. Biol.
    • Michaø, R.1    Mats, O.2
  • 45
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: Unifying sequence and structure data for evolutionary analysis
    • Roberts, E.; Eargle, J.; Wright, D.; Luthey-Schulten, Z. MultiSeq: unifying sequence and structure data for evolutionary analysis BMC Bioinf. 2006, 7, 382
    • (2006) BMC Bioinf. , vol.7 , pp. 382
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 46
    • 0026743174 scopus 로고
    • Multiple Protein-Sequence Alignment from Tertiary Structure Comparison - Assignment of Global and Residue Confidence Levels
    • Russell, R. B.; Barton, G. J. Multiple Protein-Sequence Alignment from Tertiary Structure Comparison-Assignment of Global and Residue Confidence Levels Proteins: Struct., Funct., Genet. 1992, 14, 309-323
    • (1992) Proteins: Struct., Funct., Genet. , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 47
    • 0027765576 scopus 로고
    • The limits of protein secondary structure prediction accuracy from multiple sequence alignment
    • Russell, R. B.; Barton, G. J. The Limits of Protein Secondary Structure Prediction Accuracy from Multiple Sequence Alignment J. Mol. Biol. 1993, 234, 951-957
    • (1993) J. Mol. Biol. , vol.234 , pp. 951-957
    • Russell, R.B.1    Barton, G.J.2
  • 48
    • 23244440559 scopus 로고    scopus 로고
    • Structural elements in IGP synthase exclude water to optimize ammonia transfer
    • Amaro, R. E.; Myers, R. S.; Davisson, V. J.; Luthey-Schulten, Z. A. Structural elements in IGP synthase exclude water to optimize ammonia transfer Biophys. J. 2005, 89, 475-87
    • (2005) Biophys. J. , vol.89 , pp. 475-487
    • Amaro, R.E.1    Myers, R.S.2    Davisson, V.J.3    Luthey-Schulten, Z.A.4
  • 49
    • 8644260166 scopus 로고    scopus 로고
    • Molecular dynamics simulations of substrate channeling through an α-β Barrel protein
    • Amaro, R.; Luthey-Schulten, Z. Molecular dynamics simulations of substrate channeling through an α-β barrel protein Chem. Phys. 2004, 307, 147-155
    • (2004) Chem. Phys. , vol.307 , pp. 147-155
    • Amaro, R.1    Luthey-Schulten, Z.2
  • 50
    • 0004251454 scopus 로고    scopus 로고
    • Theoretical Biophysics Group, Institute for Medical Optics, Ludwig-Maximilians University: Munich
    • Grubmuller, H. Solvate V 1.0; Theoretical Biophysics Group, Institute for Medical Optics, Ludwig-Maximilians University: Munich, 1996.
    • (1996) Solvate v 1.0
    • Grubmuller, H.1
  • 51
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar, P. r.; Larsson, P.; Cuendet, M. A.; Hess, B.; Lindahl, E. Implementation of the CHARMM Force Field in GROMACS: Analysis of Protein Stability Effects from Correction Maps, Virtual Interaction Sites, and Water Models J. Chem. Theory Comput. 2010, 6, 459-466
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 459-466
    • Bjelkmar, P.R.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 52
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An N.Log(N) Method for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald-an N.Log(N) Method for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 53
    • 33749172039 scopus 로고    scopus 로고
    • Software news and updates. Carma: A molecular dynamics analysis program
    • Glykos, N. M. Software news and updates. Carma: a molecular dynamics analysis program J. Comput. Chem. 2006, 27, 1765-8
    • (2006) J. Comput. Chem. , vol.27 , pp. 1765-1768
    • Glykos, N.M.1
  • 54
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • Andricioaei, I.; Karplus, M. On the calculation of entropy from covariance matrices of the atomic fluctuations J. Chem. Phys. 2001, 115, 6289-6292
    • (2001) J. Chem. Phys. , vol.115 , pp. 6289-6292
    • Andricioaei, I.1    Karplus, M.2
  • 55
    • 23244441019 scopus 로고    scopus 로고
    • Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase
    • Myers, R. S.; Amaro, R. E.; Luthey-Schulten, Z. A.; Davisson, V. J. Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase Biochemistry 2005, 44, 11974-85
    • (2005) Biochemistry , vol.44 , pp. 11974-11985
    • Myers, R.S.1    Amaro, R.E.2    Luthey-Schulten, Z.A.3    Davisson, V.J.4
  • 56
    • 78649766072 scopus 로고    scopus 로고
    • Nanometer propagation of millisecond motions in V-type allostery
    • Lipchock, J. M.; Loria, J. P. Nanometer Propagation of Millisecond Motions in V-Type Allostery Structure 2010, 18, 1596-1607
    • (2010) Structure , vol.18 , pp. 1596-1607
    • Lipchock, J.M.1    Loria, J.P.2
  • 57
    • 0035827583 scopus 로고    scopus 로고
    • Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex
    • Beismann-Driemeyer, S.; Sterner, R. Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex J. Biol. Chem. 2001, 276, 20387-96
    • (2001) J. Biol. Chem. , vol.276 , pp. 20387-20396
    • Beismann-Driemeyer, S.1    Sterner, R.2
  • 59
    • 0038325358 scopus 로고    scopus 로고
    • Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: Open-closed conformational change and ammonia tunneling
    • Omi, R.; Mizuguchi, H.; Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K. Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: Open-closed conformational change and ammonia tunneling J. Biochem. 2002, 132, 759-765
    • (2002) J. Biochem. , vol.132 , pp. 759-765
    • Omi, R.1    Mizuguchi, H.2    Goto, M.3    Miyahara, I.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7


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