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Volumn 51, Issue 9, 2011, Pages 2352-2360

Accurate prediction of the bound form of the akt pleckstrin homology domain using normal mode analysis to explore structural flexibility

Author keywords

[No Author keywords available]

Indexed keywords

LIGANDS; MOLECULAR MODELING;

EID: 80053318639     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci2001742     Document Type: Article
Times cited : (8)

References (56)
  • 1
  • 3
    • 54049116732 scopus 로고    scopus 로고
    • Discovery of a novel class of AKT pleckstrin homology domain inhibitors
    • Mahadevan, D. Discovery of a novel class of AKT pleckstrin homology domain inhibitors Mol. Cancer Ther. 2008, 7, 2621-2632
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2621-2632
    • Mahadevan, D.1
  • 5
    • 27844553839 scopus 로고    scopus 로고
    • AKT crystal structure and AKT-specific inhibitors
    • DOI 10.1038/sj.onc.1209087, PII 1209087
    • Kumar, C. C.; Madison, V. AKT crystal structure and AKT-specific inhibitors Oncogene 2005, 24, 7493-7501 (Pubitemid 41637989)
    • (2005) Oncogene , vol.24 , Issue.50 , pp. 7493-7501
    • Kumar, C.C.1    Madison, V.2
  • 7
    • 0032538316 scopus 로고    scopus 로고
    • Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein
    • DOI 10.1016/S0092-8674(00)81756-0
    • Soisson, S. M.; Nimnual, A. S.; Uy, M.; Bar-Sagi, D.; Kuriyan, J. Crystal Structure of the Dbl and Pleckstrin Homology Domains from the Human Son of Sevenless Protein Cell 1998, 95, 259-268 (Pubitemid 28473786)
    • (1998) Cell , vol.95 , Issue.2 , pp. 259-268
    • Soisson, S.M.1    Nimnual, A.S.2    Uy, M.3    Bar-Sagi, D.4    Kuriyan, J.5
  • 8
    • 0242468741 scopus 로고    scopus 로고
    • Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change
    • DOI 10.1042/BJ20031229
    • Milburn, C. C.; Deak, M.; Kelly, S. M.; Price, N. C.; Alessi, D. R.; Van Aalten, D. M. F. Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change Biochem. J. 2003, 375, 531-538 (Pubitemid 37433501)
    • (2003) Biochemical Journal , vol.375 , Issue.3 , pp. 531-538
    • Milburn, C.C.1    Deak, M.2    Kelly, S.M.3    Price, N.C.4    Alessi, D.R.5    Van Aalten, D.M.F.6
  • 9
    • 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
  • 10
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • DOI 10.1126/science.1108595
    • Changeux, J. P.; Edelstein, S. J. Allosteric mechanisms of signal transduction Science 2005, 308, 1424-1428 (Pubitemid 40791288)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1424-1428
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 11
    • 0014248410 scopus 로고
    • Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux
    • Changeux, J. P.; Rubin, M. M. Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux Biochemistry 1968, 7, 553-561
    • (1968) Biochemistry , vol.7 , pp. 553-561
    • Changeux, J.P.1    Rubin, M.M.2
  • 12
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • Jackson, M. B. Kinetics of unliganded acetylcholine receptor channel gating Biophys. J. 1986, 49, 663-672 (Pubitemid 16166911)
    • (1986) Biophysical Journal , vol.49 , Issue.3 , pp. 663-672
    • Jackson, M.B.1
  • 13
    • 0038503976 scopus 로고    scopus 로고
    • Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1
    • DOI 10.1016/S1097-2765(03)00236-3
    • Sablin, E. P.; Krylova, I. N.; Fletterick, R. J.; Ingraham, H. A. Structural basis for ligandindependent activation of the orphan nuclear receptor LRH-1 Mol. Cell 2003, 11, 1575-1585 (Pubitemid 36776543)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1575-1585
    • Sablin, E.P.1    Krylova, I.N.2    Fletterick, R.J.3    Ingraham, H.A.4
  • 14
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R. J.; Cotecchia, S.; Samama, P.; Costa, T. Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins Trends Pharmacol. Sci. 1993, 14, 303-307 (Pubitemid 23242583)
    • (1993) Trends in Pharmacological Sciences , vol.14 , Issue.8 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 15
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • Bahar, I.; Lezon, T. R.; Bakan, A.; Shrivastava, I. H. Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins Chem. Rev. 2010, 110, 1463-1497
    • (2010) Chem. Rev. , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 16
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • DOI 10.1038/nature06407, PII NATURE06407
    • Henzler-Wildman, K. A.; Lei, M.; Thai, V.; Kerns, S. J.; Karplus, M.; Kern, D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis Nature 2007, 450, 913-916 (Pubitemid 350231333)
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 17
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • DOI 10.1016/j.sbi.2006.01.003, PII S0959440X06000042
    • Swain, J. F.; Gierasch, L. M. The changing landscape of protein allostery Curr. Opin. Struct. Biol. 2006, 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
  • 19
    • 0037157153 scopus 로고    scopus 로고
    • Computational drug design accommodating receptor flexibility: The relaxed complex scheme
    • DOI 10.1021/ja0260162
    • Lin, J. H.; Perryman, A. L.; Schames, J. R.; McCammon, J. A. Computational drug design accommodating receptor flexibility: the relaxed complex scheme J. Am. Chem. Soc. 2002, 124, 5632-5633 (Pubitemid 34533490)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.20 , pp. 5632-5633
    • Lin, J.-H.1    Perryman, A.L.2    Schames, J.R.3    McCammon, J.A.4
  • 21
    • 77951992987 scopus 로고    scopus 로고
    • Ensemble docking into multiple crystallographically derived protein structures: An evaluation based on the statistical analysis of enrichments
    • Craig, I. R.; Essex, J. W.; Spiegel, K. Ensemble docking into multiple crystallographically derived protein structures: an evaluation based on the statistical analysis of enrichments J. Chem. Inf. Model. 2010, 50, 511-524
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 511-524
    • Craig, I.R.1    Essex, J.W.2    Spiegel, K.3
  • 22
    • 33746924045 scopus 로고    scopus 로고
    • Ensemble docking into flexible active sites. Critical evaluation of FlexE against JNK-3 and β-secretase
    • DOI 10.1021/ci050412x
    • Polgar, T.; Keseru, G. M. Ensemble docking into flexible active sites. Critical evaluation of FlexE against JNK-3 and beta-secretase J. Chem. Inf. Model. 2006, 46, 1795-1805 (Pubitemid 44185704)
    • (2006) Journal of Chemical Information and Modeling , vol.46 , Issue.4 , pp. 1795-1805
    • Polgar, T.1    Keseru, G.M.2
  • 23
    • 77956013448 scopus 로고    scopus 로고
    • HIV-1 TAR RNA spontaneously undergoes relevant apo-to-holo conformational transitions in molecular dynamics and constrained geometrical simulations
    • Fulle, S.; Christ, N. A.; Kestner, E.; Gohlke, H. HIV-1 TAR RNA spontaneously undergoes relevant apo-to-holo conformational transitions in molecular dynamics and constrained geometrical simulations J. Chem. Inf. Model. 2010, 50, 1489-1501
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 1489-1501
    • Fulle, S.1    Christ, N.A.2    Kestner, E.3    Gohlke, H.4
  • 25
    • 0032533790 scopus 로고    scopus 로고
    • Analysis of domain motions by approximate normal mode calculations
    • DOI 10.1002/(SICI)1097-0134(19981115)33:3<417::AID-PROT10>3.0.CO;2- 8
    • Hinsen, K. Analysis of domain motions by approximate normal mode calculations Proteins 1998, 33, 417-429 (Pubitemid 28516346)
    • (1998) Proteins: Structure, Function and Genetics , vol.33 , Issue.3 , pp. 417-429
    • Hinsen, K.1
  • 26
    • 1642365068 scopus 로고    scopus 로고
    • New advances in normal mode analysis of supermolecular complexes and applications to structural refinement
    • DOI 10.2174/1389203043486892
    • Ma, J. New advances in normal mode analysis of supermolecular complexes and applications to structural refinement Curr. Protein Pept. Sci. 2004, 5, 119-123 (Pubitemid 38380058)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.2 , pp. 119-123
    • Ma, J.1
  • 27
    • 0000885331 scopus 로고
    • Harmonic analysis of large systems. I. Methodology
    • Brooks, B. R.; Janezic, D.; Karplus, M. Harmonic analysis of large systems. I. Methodology J. Comput. Chem. 1995, 16, 1522-1542
    • (1995) J. Comput. Chem. , vol.16 , pp. 1522-1542
    • Brooks, B.R.1    Janezic, D.2    Karplus, M.3
  • 28
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme
    • Levitt, M.; Sander, C.; Stern, P. S. Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme J. Mol. Biol. 1985, 181, 423-447
    • (1985) J. Mol. Biol. , vol.181 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 29
    • 0028331255 scopus 로고
    • Normal mode analysis of protein dynamics
    • Case, D. A. Normal mode analysis of protein dynamics Curr. Opin. Struct. Biol. 1994, 4, 285-290 (Pubitemid 24116915)
    • (1994) Current Opinion in Structural Biology , vol.4 , Issue.2 , pp. 285-290
    • Case, D.A.1
  • 30
    • 33646145523 scopus 로고    scopus 로고
    • Can conformational change be described by only a few normal modes?
    • Petrone, P.; Pande, V. S. Can conformational change be described by only a few normal modes? Biophys. J. 2006, 90, 1583-1593
    • (2006) Biophys. J. , vol.90 , pp. 1583-1593
    • Petrone, P.1    Pande, V.S.2
  • 31
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama, F.; Sanejouand, Y. H. Conformational change of proteins arising from normal mode calculations Protein Eng. 2001, 14, 1-6 (Pubitemid 32318932)
    • (2001) Protein Engineering , vol.14 , Issue.1 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.-H.2
  • 32
    • 38549097715 scopus 로고    scopus 로고
    • Energy minimization in low-frequency normal modes to efficiently allow for global flexibility during systematic protein-protein docking
    • DOI 10.1002/prot.21579
    • May, A.; Zacharias, M. Energy minimization in low-frequency normal modes to efficiently allow for global flexibility during systematic protein-protein docking Proteins 2008, 70, 794-809 (Pubitemid 351161939)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.3 , pp. 794-809
    • May, A.1    Zacharias, M.2
  • 33
    • 23344454719 scopus 로고    scopus 로고
    • Refinement of docked protein-ligand and protein-DNA structures using low frequency normal mode amplitude optimization
    • DOI 10.1093/nar/gki730
    • Lindahl, E.; Delarue, M. Refinement of docked protein-ligand and protein-DNA structures using low frequency normal mode amplitude optimization Nucleic Acids Res. 2005, 33, 4496-4506 (Pubitemid 41222564)
    • (2005) Nucleic Acids Research , vol.33 , Issue.14 , pp. 4496-4506
    • Lindahl, E.1    Delarue, M.2
  • 34
    • 21644473891 scopus 로고    scopus 로고
    • Representing receptor flexibility in ligand docking through relevant normal modes
    • DOI 10.1021/ja042260c
    • Cavasotto, C. N.; Kovacs, J. A.; Abagyan, R. A. Representing receptor flexibility in ligand docking through relevant normal modes J. Am. Chem. Soc. 2005, 127, 9632-9640 (Pubitemid 40934775)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.26 , pp. 9632-9640
    • Cavasotto, C.N.1    Kovacs, J.A.2    Abagyan, R.A.3
  • 35
    • 77951232176 scopus 로고    scopus 로고
    • FiberDock: Flexible induced-fit backbone refinement in molecular docking
    • Mashiach, E.; Nussinov, R.; Wolfson, H. J. FiberDock: Flexible induced-fit backbone refinement in molecular docking Proteins: Struct., Funct., Bioinf. 2010, 78, 1503-1519
    • (2010) Proteins: Struct., Funct., Bioinf. , vol.78 , pp. 1503-1519
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3
  • 36
    • 30044434744 scopus 로고    scopus 로고
    • Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state
    • DOI 10.1073/pnas.0507603102
    • Tobi, D.; Bahar, I. Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 18908-18913 (Pubitemid 43049540)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.52 , pp. 18908-18913
    • Tobi, D.1    Bahar, I.2
  • 37
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser, A.; Do, R. K.; Sali, A. Modeling of loops in protein structures Protein Sci. 2000, 9, 1753-1773
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 38
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion, M. M. Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis Phys. Rev. Lett. 1996, 77, 1905-1908 (Pubitemid 126625816)
    • (1996) Physical Review Letters , vol.77 , Issue.9 , pp. 1905-1908
    • Tirion, M.M.1
  • 39
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi, H.; Ueda, Y.; Go, N. Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions Int. J. Pept. Protein Res. 1975, 7, 445-459
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 40
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a g-like model
    • DOI 10.1006/jmbi.2001.5037
    • Koga, N.; Takada, S. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model J. Mol. Biol. 2001, 313, 171-180 (Pubitemid 33001173)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.1 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 42
    • 0030549642 scopus 로고    scopus 로고
    • Efficient computation of potential energy first and second derivatives for molecular dynamics, normal coordinate analysis, and molecular mechanics calculations
    • Tuzun, R. E.; Noid, D. W.; Sumpter, B. G. Efficient computation of potential energy first and second derivatives for molecular dynamics, normal coordinate analysis, and molecular mechanics calculations Macromol. Theory Simul. 1996, 5, 771-788
    • (1996) Macromol. Theory Simul. , vol.5 , pp. 771-788
    • Tuzun, R.E.1    Noid, D.W.2    Sumpter, B.G.3
  • 43
    • 80053317671 scopus 로고    scopus 로고
    • Scientific Computing Tools for Python-Numpy. (accessed 17-November-2010)
    • Scientific Computing Tools for Python-Numpy. 2010. http://numpy.scipy. org/ (accessed 17-November-2010).
    • (2010)
  • 44
    • 46249092554 scopus 로고    scopus 로고
    • Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 47
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 1997, 267, 727-748 (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 48
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • DOI 10.1016/j.sbi.2005.08.007, PII S0959440X05001557, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Bahar, I.; Rader, A. J. Coarse-grained normal mode analysis in structural biology Curr. Opin. Struct. Biol. 2005, 15, 586-592 (Pubitemid 41393491)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 49
    • 0004203940 scopus 로고    scopus 로고
    • 3 rd ed. Wellesley-Cambridge Press: Wellesley, MA
    • Strang, G. Introduction to Linear Algebra, 3 rd ed.; Wellesley-Cambridge Press: Wellesley, MA, 2003.
    • (2003) Introduction to Linear Algebra
    • Strang, G.1
  • 50
    • 67649225348 scopus 로고    scopus 로고
    • Efficient drug lead discovery and optimization
    • Jorgensen, W. L. Efficient drug lead discovery and optimization Acc. Chem. Res. 2009, 42, 724-733
    • (2009) Acc. Chem. Res. , vol.42 , pp. 724-733
    • Jorgensen, W.L.1
  • 51
    • 33749242759 scopus 로고    scopus 로고
    • Contribution of conformer focusing to the uncertainty in predicting free energies for protein-ligand binding
    • DOI 10.1021/jm060763i
    • Tirado-Rives, J.; Jorgensen, W. L. Contribution of conformer focusing to the uncertainty in predicting free energies for protein-ligand binding J. Med. Chem. 2006, 49, 5880-5884 (Pubitemid 44484934)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.20 , pp. 5880-5884
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 52
    • 41149134297 scopus 로고    scopus 로고
    • Probing ligand binding modes of human cytochrome P450 2J2 by homology modeling, molecular dynamics simulation, and flexible molecular docking
    • DOI 10.1002/prot.21778
    • Li, W.; Tang, Y.; Liu, H.; Cheng, J.; Zhu, W.; Jiang, H. Probing ligand binding modes of human cytochrome P450 2J2 by homology modeling, molecular dynamics simulation, and flexible molecular docking Proteins: Struct., Funct., Bioinf. 2008, 71, 938-949 (Pubitemid 351436336)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.2 , pp. 938-949
    • Li, W.1    Tang, Y.2    Liu, H.3    Cheng, J.4    Zhu, W.5    Jiang, H.6
  • 53
    • 77955096900 scopus 로고    scopus 로고
    • Computational approaches for protein function prediction: A combined strategy from multiple sequence alignment to molecular docking-based virtual screening
    • Pierri, C. L.; Parisi, G.; Porcelli, V. Computational approaches for protein function prediction: A combined strategy from multiple sequence alignment to molecular docking-based virtual screening Biochim. Biophys. Acta, Proteins Proteomics 2010, 1804, 1695-1712
    • (2010) Biochim. Biophys. Acta, Proteins Proteomics , vol.1804 , pp. 1695-1712
    • Pierri, C.L.1    Parisi, G.2    Porcelli, V.3
  • 54
    • 33646002994 scopus 로고    scopus 로고
    • Comparative modeling for protein structure prediction
    • Ginalski, K. Comparative modeling for protein structure prediction Curr. Opin. Struct. Biol. 2006, 16, 172-177
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 172-177
    • Ginalski, K.1
  • 55
    • 67650150099 scopus 로고    scopus 로고
    • Improving structure-based function prediction using molecular dynamics
    • Glazer, D. S.; Radmer, R. J.; Altman, R. B. Improving structure-based function prediction using molecular dynamics Structure 2009, 17, 919-929
    • (2009) Structure , vol.17 , pp. 919-929
    • Glazer, D.S.1    Radmer, R.J.2    Altman, R.B.3
  • 56
    • 33847114057 scopus 로고    scopus 로고
    • Conformational dynamics of the estrogen receptor α: Molecular dynamics simulations of the influence of binding site structure on protein dynamics
    • DOI 10.1021/bi061656t
    • Celik, L.; Lund, J. D. D.; Schiott, B. Conformational Dynamics of the Estrogen Receptor alpha: Molecular Dynamics Simulations of the Influence of Binding Site Structure on Protein Dynamics. Biochemistry 2007, 46, 1743-1758. (Pubitemid 46290551)
    • (2007) Biochemistry , vol.46 , Issue.7 , pp. 1743-1758
    • Celik, L.1    Lund, J.D.D.2    Schiott, B.3


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