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Volumn 56, Issue 17, 2013, Pages 7003-7014

Unbinding pathways from the glucocorticoid receptor shed light on the reduced sensitivity of glucocorticoid ligands to a naturally occurring, clinically relevant mutant receptor

Author keywords

[No Author keywords available]

Indexed keywords

DEXAMETHASONE; GLUCOCORTICOID RECEPTOR;

EID: 84884235713     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400802b     Document Type: Article
Times cited : (29)

References (37)
  • 1
    • 77951901129 scopus 로고    scopus 로고
    • Structural Overview of the Nuclear Receptor Superfamily: Insights into Physiology and Therapeutics
    • Huang, P.; Chandra, V.; Rastinejad, F. Structural Overview of the Nuclear Receptor Superfamily: Insights into Physiology and Therapeutics Annu. Rev. Physiol. 2010, 72, 247-272
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 247-272
    • Huang, P.1    Chandra, V.2    Rastinejad, F.3
  • 2
    • 0028283503 scopus 로고
    • Molecular Mechanisms of Action of Steroid/Thyroid Receptor Superfamily Members
    • Tsai, M.; O'Malley, B. W. Molecular Mechanisms of Action of Steroid/Thyroid Receptor Superfamily Members Annu. Rev. Biochem. 1994, 63, 451-486
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.1    O'Malley, B.W.2
  • 3
    • 77951762462 scopus 로고    scopus 로고
    • Structure of the Glucocorticoid Receptor, a Flexible Protein That Can Adapt to Different Ligands
    • Veleiro, A. S.; Alvarez, L. D.; Eduardo, S. L.; Burton, G. Structure of the Glucocorticoid Receptor, a Flexible Protein That Can Adapt to Different Ligands ChemMedChem 2010, 5, 649-659
    • (2010) ChemMedChem , vol.5 , pp. 649-659
    • Veleiro, A.S.1    Alvarez, L.D.2    Eduardo, S.L.3    Burton, G.4
  • 4
    • 84860877711 scopus 로고    scopus 로고
    • Deciphering Modern Glucocorticoid Cross-pharmacology Using Ancestral Corticosteroid Receptors
    • Kohn, J. A.; Deshpande, K.; Ortlund, E. A. Deciphering Modern Glucocorticoid Cross-pharmacology Using Ancestral Corticosteroid Receptors J. Biol. Chem. 2012, 287, 16267-16275
    • (2012) J. Biol. Chem. , vol.287 , pp. 16267-16275
    • Kohn, J.A.1    Deshpande, K.2    Ortlund, E.A.3
  • 5
    • 79953726304 scopus 로고    scopus 로고
    • Glucocorticosteroids: Current and future directions
    • Barnes, P. J. Glucocorticosteroids: Current and future directions Br. J. Pharmacol. 2011, 163, 29-43
    • (2011) Br. J. Pharmacol. , vol.163 , pp. 29-43
    • Barnes, P.J.1
  • 6
    • 18444405534 scopus 로고    scopus 로고
    • Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition
    • Bledsoe, R. K.; Montana, V. G.; Stanley, T. B.; Delves, C. J.; Apolito, C. J.; McKee, D. D.; Consler, T. G.; Parks, D. J.; Stewart, E. L.; Willson, T. M. Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition Cell 2002, 110, 93-105
    • (2002) Cell , vol.110 , pp. 93-105
    • Bledsoe, R.K.1    Montana, V.G.2    Stanley, T.B.3    Delves, C.J.4    Apolito, C.J.5    McKee, D.D.6    Consler, T.G.7    Parks, D.J.8    Stewart, E.L.9    Willson, T.M.10
  • 7
    • 33744477341 scopus 로고    scopus 로고
    • How corticosteroids control inflammation: Quintiles Prize Lecture 2005
    • Barnes, P. J. How corticosteroids control inflammation: Quintiles Prize Lecture 2005 Br. J. Pharmacol. 2009, 148, 245-254
    • (2009) Br. J. Pharmacol. , vol.148 , pp. 245-254
    • Barnes, P.J.1
  • 8
    • 77952951084 scopus 로고    scopus 로고
    • Mechanisms and resistance in glucocorticoid control of inflammation
    • Barnes, P. J. Mechanisms and resistance in glucocorticoid control of inflammation J. Steroid Biochem. Mol. Biol. 2010, 120, 76-85
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.120 , pp. 76-85
    • Barnes, P.J.1
  • 10
    • 34848829143 scopus 로고    scopus 로고
    • Human receptor kinetics and lung tissue retention of the enhanced-affinity glucocorticoid fluticasone furoate
    • Valotis, A.; Högger, P. Human receptor kinetics and lung tissue retention of the enhanced-affinity glucocorticoid fluticasone furoate Respir. Res. 2007, 8, 54
    • (2007) Respir. Res. , vol.8 , pp. 54
    • Valotis, A.1    Högger, P.2
  • 11
    • 45749101311 scopus 로고    scopus 로고
    • X-ray Crystal Structure of the Novel Enhanced-Affinity Glucocorticoid Agonist Fluticasone Furoate in the Glucocorticoid Receptor-Ligand Binding Domain
    • Biggadike, K.; Bledsoe, R. K.; Hassell, A. M.; Kirk, B. E.; McLay, I. M.; Shewchuk, L. M.; Stewart, E. L. X-ray Crystal Structure of the Novel Enhanced-Affinity Glucocorticoid Agonist Fluticasone Furoate in the Glucocorticoid Receptor-Ligand Binding Domain J. Med. Chem. 2008, 51, 3349-3352
    • (2008) J. Med. Chem. , vol.51 , pp. 3349-3352
    • Biggadike, K.1    Bledsoe, R.K.2    Hassell, A.M.3    Kirk, B.E.4    McLay, I.M.5    Shewchuk, L.M.6    Stewart, E.L.7
  • 12
    • 80054737671 scopus 로고    scopus 로고
    • Long-acting fluticasone furoate has a superior pharmacological profile to fluticasone propionate in human respiratory cells
    • Rossios, C.; To, Y.; To, M.; Ito, M.; Barnes, P. J.; Adcock, I. M.; Johnson, M.; Ito, K. Long-acting fluticasone furoate has a superior pharmacological profile to fluticasone propionate in human respiratory cells Eur. J. Pharmacol. 2011, 670, 244-251
    • (2011) Eur. J. Pharmacol. , vol.670 , pp. 244-251
    • Rossios, C.1    To, Y.2    To, M.3    Ito, M.4    Barnes, P.J.5    Adcock, I.M.6    Johnson, M.7    Ito, K.8
  • 13
    • 77955329488 scopus 로고    scopus 로고
    • Drug-target residence time: Critical information for lead optimization
    • Lu, H.; Tonge, P. J. Drug-target residence time: Critical information for lead optimization Curr. Opin. Chem. Biol. 2010, 14, 467-474
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 467-474
    • Lu, H.1    Tonge, P.J.2
  • 14
    • 44049103958 scopus 로고    scopus 로고
    • Residence Time of Receptor-Ligand Complexes and Its Effect on Biological Function
    • Tummino, P. J.; Copeland, R. A. Residence Time of Receptor-Ligand Complexes and Its Effect on Biological Function Biochemistry 2008, 47, 5481-5492
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 15
    • 4344645978 scopus 로고    scopus 로고
    • Opinion: Can the pharmaceutical industry reduce attrition rates?
    • Kola, I.; Landis, J. Opinion: Can the pharmaceutical industry reduce attrition rates? Nat. Rev. Drug Discovery 2004, 3, 711-716
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 711-716
    • Kola, I.1    Landis, J.2
  • 17
    • 83055179348 scopus 로고    scopus 로고
    • Shielded Hydrogen Bonds as Structural Determinants of Binding Kinetics: Application in Drug Design
    • Schmidtke, P.; Luque, F. J.; Murray, J. B.; Barril, X. Shielded Hydrogen Bonds as Structural Determinants of Binding Kinetics: Application in Drug Design J. Am. Chem. Soc. 2011, 133, 18903-18910
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18903-18910
    • Schmidtke, P.1    Luque, F.J.2    Murray, J.B.3    Barril, X.4
  • 18
    • 77952844866 scopus 로고    scopus 로고
    • Single-Molecule Pulling Simulations Can Discern Active from Inactive Enzyme Inhibitors
    • Colizzi, F.; Perozzo, R.; Scapozza, L.; Recanatini, M.; Cavalli, A. Single-Molecule Pulling Simulations Can Discern Active from Inactive Enzyme Inhibitors J. Am. Chem. Soc. 2010, 132, 7361-7371
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7361-7371
    • Colizzi, F.1    Perozzo, R.2    Scapozza, L.3    Recanatini, M.4    Cavalli, A.5
  • 19
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium Equality for Free Energy Differences
    • Jarzynski, C. Nonequilibrium Equality for Free Energy Differences Phys. Rev. Lett. 1997, 78, 2690-2693
    • (1997) Phys. Rev. Lett. , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 20
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium Information from Nonequilibrium Measurements in an Experimental Test of Jarzynski's Equality
    • Liphardt, J. Equilibrium Information from Nonequilibrium Measurements in an Experimental Test of Jarzynski's Equality Science 2002, 296, 1832-1835
    • (2002) Science , vol.296 , pp. 1832-1835
    • Liphardt, J.1
  • 21
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality
    • Park, S.; Khalili-Araghi, F.; Tajkhorshid, E.; Schulten, K. Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality J. Chem. Phys. 2003, 119, 3559
    • (2003) J. Chem. Phys. , vol.119 , pp. 3559
    • Park, S.1    Khalili-Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 22
    • 4143087050 scopus 로고    scopus 로고
    • Calculating potentials of mean force from steered molecular dynamics simulations
    • Park, S.; Schulten, K. Calculating potentials of mean force from steered molecular dynamics simulations J. Chem. Phys. 2004, 120, 5946
    • (2004) J. Chem. Phys. , vol.120 , pp. 5946
    • Park, S.1    Schulten, K.2
  • 23
    • 70450046360 scopus 로고    scopus 로고
    • Ligand unbinding from the estrogen receptor: A computational study of pathways and ligand specificity
    • Burendahl, S.; Danciulescu, C.; Nilsson, L. Ligand unbinding from the estrogen receptor: A computational study of pathways and ligand specificity Proteins 2009, 77, 842-856
    • (2009) Proteins , vol.77 , pp. 842-856
    • Burendahl, S.1    Danciulescu, C.2    Nilsson, L.3
  • 24
    • 67651202362 scopus 로고    scopus 로고
    • Computational Insights into the Mechanism of Ligand Unbinding and Selectivity of Estrogen Receptors
    • Shen, J.; Li, W.; Liu, G.; Tang, Y.; Jiang, H. Computational Insights into the Mechanism of Ligand Unbinding and Selectivity of Estrogen Receptors J. Phys. Chem. B 2009, 113, 10436-10444
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10436-10444
    • Shen, J.1    Li, W.2    Liu, G.3    Tang, Y.4    Jiang, H.5
  • 25
    • 0038241502 scopus 로고    scopus 로고
    • Variations of the human glucocorticoid receptor gene (NR3C1): Pathological and in vitro mutations and polymorphisms
    • Bray, P. J.; Cotton, R. G. H. Variations of the human glucocorticoid receptor gene (NR3C1): Pathological and in vitro mutations and polymorphisms Hum. Mutat. 2003, 21, 557-568
    • (2003) Hum. Mutat. , vol.21 , pp. 557-568
    • Bray, P.J.1    Cotton, R.G.H.2
  • 26
    • 0036075596 scopus 로고    scopus 로고
    • A Novel, C-Terminal Dominant Negative Mutation of the GR Causes Familial Glucocorticoid Resistance through Abnormal Interactions with p160 Steroid Receptor Coactivators
    • Vottero, A. A Novel, C-Terminal Dominant Negative Mutation of the GR Causes Familial Glucocorticoid Resistance through Abnormal Interactions with p160 Steroid Receptor Coactivators J. Clin. Endocrinol. Metab. 2002, 87, 2658-2667
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 2658-2667
    • Vottero, A.1
  • 27
    • 1942536210 scopus 로고    scopus 로고
    • Natural Glucocorticoid Receptor Mutants Causing Generalized Glucocorticoid Resistance: Molecular Genotype, Genetic Transmission, and Clinical Phenotype
    • Charmandari, E. Natural Glucocorticoid Receptor Mutants Causing Generalized Glucocorticoid Resistance: Molecular Genotype, Genetic Transmission, and Clinical Phenotype J. Clin. Endocrinol. Metab. 2004, 89, 1939-1949
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 1939-1949
    • Charmandari, E.1
  • 28
    • 43249102598 scopus 로고    scopus 로고
    • Generalized Glucocorticoid Resistance: Clinical Aspects, Molecular Mechanisms, and Implications of a Rare Genetic Disorder
    • Charmandari, E.; Kino, T.; Ichijo, T.; Chrousos, G. P. Generalized Glucocorticoid Resistance: Clinical Aspects, Molecular Mechanisms, and Implications of a Rare Genetic Disorder J. Clin. Endocrinol. Metab. 2008, 93, 1563-1572
    • (2008) J. Clin. Endocrinol. Metab. , vol.93 , pp. 1563-1572
    • Charmandari, E.1    Kino, T.2    Ichijo, T.3    Chrousos, G.P.4
  • 29
    • 24144439756 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations Reveal Multiple Pathways of Ligand Dissociation from Thyroid Hormone Receptors
    • Martínez, L.; Sonoda, M. T.; Webb, P.; Baxter, J. D.; Skaf, M. S.; Polikarpov, I. Molecular Dynamics Simulations Reveal Multiple Pathways of Ligand Dissociation from Thyroid Hormone Receptors Biophys. J. 2005, 89, 2011-2023
    • (2005) Biophys. J. , vol.89 , pp. 2011-2023
    • Martínez, L.1    Sonoda, M.T.2    Webb, P.3    Baxter, J.D.4    Skaf, M.S.5    Polikarpov, I.6
  • 30
    • 30444446327 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Ligand Dissociation from Thyroid Hormone Receptors: Evidence of the Likeliest Escape Pathway and Its Implications for the Design of Novel Ligands
    • Martínez, L.; Webb, P.; Polikarpov, I.; Skaf, M. S. Molecular Dynamics Simulations of Ligand Dissociation from Thyroid Hormone Receptors: Evidence of the Likeliest Escape Pathway and Its Implications for the Design of Novel Ligands J. Med. Chem. 2006, 49, 23-26
    • (2006) J. Med. Chem. , vol.49 , pp. 23-26
    • Martínez, L.1    Webb, P.2    Polikarpov, I.3    Skaf, M.S.4
  • 31
    • 41649098153 scopus 로고    scopus 로고
    • Exploring the Molecular Basis of Action of the Passive Antiglucocorticoid 21-Hydroxy-6,19-epoxyprogesterone
    • álvarez, L. D.; Martí, M. A.; Veleiro, A. S.; Presman, D. M.; Estrin, D. A.; Pecci, A.; Burton, G. Exploring the Molecular Basis of Action of the Passive Antiglucocorticoid 21-Hydroxy-6,19-epoxyprogesterone J. Med. Chem. 2008, 51, 1352-1360
    • (2008) J. Med. Chem. , vol.51 , pp. 1352-1360
    • Álvarez, L.D.1    Martí, M.A.2    Veleiro, A.S.3    Presman, D.M.4    Estrin, D.A.5    Pecci, A.6    Burton, G.7
  • 32
    • 0037006978 scopus 로고    scopus 로고
    • Mutations of Tyrosine 537 in the Human Estrogen Receptor-α Selectively Alter the Receptor's Affinity for Estradiol and the Kinetics of the Interaction
    • Zhong, L.; Skafar, D. F. Mutations of Tyrosine 537 in the Human Estrogen Receptor-α Selectively Alter the Receptor's Affinity for Estradiol and the Kinetics of the Interaction Biochemistry 2002, 41, 4209-4217
    • (2002) Biochemistry , vol.41 , pp. 4209-4217
    • Zhong, L.1    Skafar, D.F.2
  • 34
    • 84884259005 scopus 로고    scopus 로고
    • version 9.1 () Schrödinger, LLC, New York
    • Mestro, version 9.1 (2009) Schrödinger, LLC, New York.
    • (2009) Mestro


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