메뉴 건너뛰기




Volumn 56, Issue 9, 2016, Pages 1808-1822

Molecular mechanism of biased ligand conformational changes in CC chemokine receptor 7

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; HYDROGEN BONDS; PROTEINS;

EID: 84989299167     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/acs.jcim.6b00367     Document Type: Article
Times cited : (14)

References (85)
  • 1
    • 84862776738 scopus 로고    scopus 로고
    • Biased Signaling Pathways in β2-Adrenergic Receptor Characterized by 19F-NMR
    • Liu, J. J.; Horst, R.; Katritch, V.; Stevens, R. C.; Wüthrich, K. Biased Signaling Pathways in β2-Adrenergic Receptor Characterized by 19F-NMR Science 2012, 335, 1106-1110 10.1126/science.1215802
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wüthrich, K.5
  • 2
    • 84855901533 scopus 로고    scopus 로고
    • Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors
    • Reiter, E.; Ahn, S.; Shukla, A. K.; Lefkowitz, R. J. Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors Annu. Rev. Pharmacol. Toxicol. 2012, 52, 179-197 10.1146/annurev.pharmtox.010909.105800
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 4
    • 67649856866 scopus 로고    scopus 로고
    • Selective Engagement of G Protein Coupled Receptor Kinases (GRKs) Encodes Distinct Functions of Biased Ligands
    • Zidar, D. A.; Violin, J. D.; Whalen, E. J.; Lefkowitz, R. J. Selective Engagement of G Protein Coupled Receptor Kinases (GRKs) Encodes Distinct Functions of Biased Ligands Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 9649-9654 10.1073/pnas.0904361106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9649-9654
    • Zidar, D.A.1    Violin, J.D.2    Whalen, E.J.3    Lefkowitz, R.J.4
  • 5
    • 77957778459 scopus 로고    scopus 로고
    • Molecular Basis for Activation of G Protein-coupled Receptor Kinases
    • Boguth, C. A.; Singh, P.; Huang, C.; Tesmer, J. J. G. Molecular Basis for Activation of G Protein-coupled Receptor Kinases EMBO J. 2010, 29, 3249-3259 10.1038/emboj.2010.206
    • (2010) EMBO J. , vol.29 , pp. 3249-3259
    • Boguth, C.A.1    Singh, P.2    Huang, C.3    Tesmer, J.J.G.4
  • 6
    • 84872221774 scopus 로고    scopus 로고
    • Structure-Function of the G-Protein-Coupled Receptor Superfamily
    • Katritch, V.; Cherezov, V.; Stevens, R. C. Structure-Function of the G-Protein-Coupled Receptor Superfamily Annu. Rev. Pharmacol. Toxicol. 2013, 53, 531-556 10.1146/annurev-pharmtox-032112-135923
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 8
    • 42649086026 scopus 로고    scopus 로고
    • CCR7 and Its Ligands: Balancing Immunity and Tolerance
    • Förster, R.; Davalos-Misslitz, A. C.; Rot, A. CCR7 and Its Ligands: Balancing Immunity and Tolerance Nat. Rev. Immunol. 2008, 8, 362-371 10.1038/nri2297
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 362-371
    • Förster, R.1    Davalos-Misslitz, A.C.2    Rot, A.3
  • 9
    • 79955010407 scopus 로고    scopus 로고
    • Dendritic Cell Chemotaxis in 3D under Defined Chemokine Gradients Reveals Differential Response to Ligands CCL21 and CCL19
    • Haessler, U.; Pisano, M.; Wu, M.; Swartz, M. A. Dendritic Cell Chemotaxis in 3D under Defined Chemokine Gradients Reveals Differential Response to Ligands CCL21 and CCL19 Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 5614-5619 10.1073/pnas.1014920108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 5614-5619
    • Haessler, U.1    Pisano, M.2    Wu, M.3    Swartz, M.A.4
  • 11
    • 2542423686 scopus 로고    scopus 로고
    • Differential Desensitization, Receptor Phosphorylation, -Arrestin Recruitment, and ERK1/2 Activation by the Two Endogenous Ligands for the CC Chemokine Receptor 7
    • Kohout, T. A.; Nicholas, S. L.; Perry, S. J.; Reinhart, G.; Junger, S.; Struthers, R. S. Differential Desensitization, Receptor Phosphorylation, -Arrestin Recruitment, and ERK1/2 Activation by the Two Endogenous Ligands for the CC Chemokine Receptor 7 J. Biol. Chem. 2004, 279, 23214-23222 10.1074/jbc.M402125200
    • (2004) J. Biol. Chem. , vol.279 , pp. 23214-23222
    • Kohout, T.A.1    Nicholas, S.L.2    Perry, S.J.3    Reinhart, G.4    Junger, S.5    Struthers, R.S.6
  • 19
    • 84882654052 scopus 로고    scopus 로고
    • Simulations of Biased Agonists in the β2 Adrenergic Receptor with Accelerated Molecular Dynamics
    • Tikhonova, I. G.; Selvam, B.; Ivetac, A.; Wereszczynski, J.; McCammon, J. A. Simulations of Biased Agonists in the β2 Adrenergic Receptor with Accelerated Molecular Dynamics Biochemistry 2013, 52, 5593-5603 10.1021/bi400499n
    • (2013) Biochemistry , vol.52 , pp. 5593-5603
    • Tikhonova, I.G.1    Selvam, B.2    Ivetac, A.3    Wereszczynski, J.4    McCammon, J.A.5
  • 21
    • 3142716857 scopus 로고    scopus 로고
    • Accelerated Molecular Dynamics: A Promising and Efficient Simulation Method for Biomolecules
    • Hamelberg, D.; Mongan, J.; McCammon, J. A. Accelerated Molecular Dynamics: A Promising and Efficient Simulation Method for Biomolecules J. Chem. Phys. 2004, 120, 11919-11929 10.1063/1.1755656
    • (2004) J. Chem. Phys. , vol.120 , pp. 11919-11929
    • Hamelberg, D.1    Mongan, J.2    McCammon, J.A.3
  • 22
    • 80051695986 scopus 로고    scopus 로고
    • Implementation of Accelerated Molecular Dynamics in NAMD
    • Wang, Y.; Harrison, C. B.; Schulten, K.; McCammon, J. A. Implementation of Accelerated Molecular Dynamics in NAMD Comput. Sci. Discovery 2011, 4, 015002 10.1088/1749-4699/4/1/015002
    • (2011) Comput. Sci. Discovery , vol.4 , pp. 015002
    • Wang, Y.1    Harrison, C.B.2    Schulten, K.3    McCammon, J.A.4
  • 23
    • 77957055780 scopus 로고
    • Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relations in G Protein-Coupled Receptors
    • In; Sealfon, S. C. Receptor Molecular Biology; Academic Press, Vol
    • Ballesteros, J. A.; Weinstein, H. Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relations in G Protein-Coupled Receptors. In Methods in Neurosciences; Sealfon, S. C., Ed.; Receptor Molecular Biology; Academic Press, 1995; Vol. 25, pp 366-428.
    • (1995) Methods in Neurosciences , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 29
    • 0027136282 scopus 로고
    • Comparative Protein Modelling by Satisfaction of Spatial Restraints
    • Šali, A.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Restraints J. Mol. Biol. 1993, 234, 779-815 10.1006/jmbi.1993.1626
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 35
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A Unified Platform for Automated Protein Structure and Function Prediction
    • Roy, A.; Kucukural, A.; Zhang, Y. I-TASSER: A Unified Platform for Automated Protein Structure and Function Prediction Nat. Protoc. 2010, 5, 725-738 10.1038/nprot.2010.5
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 36
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER Server for Protein 3D Structure Prediction
    • Zhang, Y. I-TASSER Server for Protein 3D Structure Prediction BMC Bioinf. 2008, 9, 40 10.1186/1471-2105-9-40
    • (2008) BMC Bioinf. , vol.9 , pp. 40
    • Zhang, Y.1
  • 37
    • 77955779227 scopus 로고    scopus 로고
    • Conserved Binding Mode of Human β2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-Ray Crystallography
    • Wacker, D.; Fenalti, G.; Brown, M. A.; Katritch, V.; Abagyan, R.; Cherezov, V.; Stevens, R. C. Conserved Binding Mode of Human β2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-Ray Crystallography J. Am. Chem. Soc. 2010, 132, 11443-11445 10.1021/ja105108q
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11443-11445
    • Wacker, D.1    Fenalti, G.2    Brown, M.A.3    Katritch, V.4    Abagyan, R.5    Cherezov, V.6    Stevens, R.C.7
  • 39
    • 84903776217 scopus 로고    scopus 로고
    • Modelling Three-Dimensional Protein Structures for Applications in Drug Design
    • Schmidt, T.; Bergner, A.; Schwede, T. Modelling Three-Dimensional Protein Structures for Applications in Drug Design Drug Discovery Today 2014, 19, 890-897 10.1016/j.drudis.2013.10.027
    • (2014) Drug Discovery Today , vol.19 , pp. 890-897
    • Schmidt, T.1    Bergner, A.2    Schwede, T.3
  • 40
    • 0033081379 scopus 로고    scopus 로고
    • Structure of a CXC Chemokine-Receptor Fragment in Complex with Interleukin-8
    • Skelton, N. J.; Quan, C.; Reilly, D.; Lowman, H. Structure of a CXC Chemokine-Receptor Fragment in Complex with Interleukin-8 Structure 1999, 7, 157-168 10.1016/S0969-2126(99)80022-7
    • (1999) Structure , vol.7 , pp. 157-168
    • Skelton, N.J.1    Quan, C.2    Reilly, D.3    Lowman, H.4
  • 41
    • 84908548257 scopus 로고    scopus 로고
    • Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: The N-Terminal Region of CCR3 Bound to CCL11/Eotaxin-1
    • Millard, C. J.; Ludeman, J. P.; Canals, M.; Bridgford, J. L.; Hinds, M. G.; Clayton, D. J.; Christopoulos, A.; Payne, R. J.; Stone, M. J. Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: The N-Terminal Region of CCR3 Bound to CCL11/Eotaxin-1 Structure 2014, 22, 1571-1581 10.1016/j.str.2014.08.023
    • (2014) Structure , vol.22 , pp. 1571-1581
    • Millard, C.J.1    Ludeman, J.P.2    Canals, M.3    Bridgford, J.L.4    Hinds, M.G.5    Clayton, D.J.6    Christopoulos, A.7    Payne, R.J.8    Stone, M.J.9
  • 45
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual Molecular Dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD: Visual Molecular Dynamics J. Mol. Graphics 1996, 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 47
    • 3142714765 scopus 로고    scopus 로고
    • Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations
    • Mackerell, A. D.; Feig, M.; Brooks, C. L. Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations J. Comput. Chem. 2004, 25, 1400-1415 10.1002/jcc.20065
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 48
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ψ, ψ and Side-Chain π1 and π2 Dihedral Angles
    • Best, R. B.; Zhu, X.; Shim, J.; Lopes, P. E. M.; Mittal, J.; Feig, M.; MacKerell, A. D. Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ψ, ψ and Side-Chain π1 and π2 Dihedral Angles J. Chem. Theory Comput. 2012, 8, 3257-3273 10.1021/ct300400x
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 3257-3273
    • Best, R.B.1    Zhu, X.2    Shim, J.3    Lopes, P.E.M.4    Mittal, J.5    Feig, M.6    MacKerell, A.D.7
  • 50
    • 84861060898 scopus 로고    scopus 로고
    • OPM Database and PPM Web Server: Resources for Positioning of Proteins in Membranes
    • Lomize, M. A.; Pogozheva, I. D.; Joo, H.; Mosberg, H. I.; Lomize, A. L. OPM Database and PPM Web Server: Resources for Positioning of Proteins in Membranes Nucleic Acids Res. 2012, 40, D370-D376 10.1093/nar/gkr703
    • (2012) Nucleic Acids Res. , vol.40 , pp. D370-D376
    • Lomize, M.A.1    Pogozheva, I.D.2    Joo, H.3    Mosberg, H.I.4    Lomize, A.L.5
  • 51
    • 84887279441 scopus 로고    scopus 로고
    • Accurate and Efficient Integration for Molecular Dynamics Simulations at Constant Temperature and Pressure
    • Lippert, R. A.; Predescu, C.; Ierardi, D. J.; Mackenzie, K. M.; Eastwood, M. P.; Dror, R. O.; Shaw, D. E. Accurate and Efficient Integration for Molecular Dynamics Simulations at Constant Temperature and Pressure J. Chem. Phys. 2013, 139, 164106 10.1063/1.4825247
    • (2013) J. Chem. Phys. , vol.139 , pp. 164106
    • Lippert, R.A.1    Predescu, C.2    Ierardi, D.J.3    MacKenzie, K.M.4    Eastwood, M.P.5    Dror, R.O.6    Shaw, D.E.7
  • 52
    • 78650649545 scopus 로고    scopus 로고
    • R. Core Team. R Foundation for Statistical Computing: Vienna, Austria
    • R. Core Team. A Language and Environment for Statistical Computing; R Foundation for Statistical Computing: Vienna, Austria, 2014.
    • (2014) A Language and Environment for Statistical Computing
  • 54
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: An R Package for the Comparative Analysis of Protein Structures
    • Grant, B. J.; Rodrigues, A. P. C.; ElSawy, K. M.; McCammon, J. A.; Caves, L. S. D. Bio3d: An R Package for the Comparative Analysis of Protein Structures Bioinformatics 2006, 22, 2695-2696 10.1093/bioinformatics/btl461
    • (2006) Bioinformatics , vol.22 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.C.2    ElSawy, K.M.3    McCammon, J.A.4    Caves, L.S.D.5
  • 55
    • 84923915053 scopus 로고    scopus 로고
    • Integrating Protein Structural Dynamics and Evolutionary Analysis with Bio3D
    • Skjærven, L.; Yao, X.-Q.; Scarabelli, G.; Grant, B. J. Integrating Protein Structural Dynamics and Evolutionary Analysis with Bio3D BMC Bioinf. 2014, 15, 399 10.1186/s12859-014-0399-6
    • (2014) BMC Bioinf. , vol.15 , pp. 399
    • Skjærven, L.1    Yao, X.-Q.2    Scarabelli, G.3    Grant, B.J.4
  • 57
    • 0030333470 scopus 로고    scopus 로고
    • Three-Dimensional Hydrogen-Bond Geometry and Probability Information from a Crystal Survey
    • Mills, J. E. J.; Dean, P. M. Three-Dimensional Hydrogen-Bond Geometry and Probability Information from a Crystal Survey J. Comput.-Aided Mol. Des. 1996, 10, 607-622 10.1007/BF00134183
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , pp. 607-622
    • Mills, J.E.J.1    Dean, P.M.2
  • 59
    • 0032546782 scopus 로고    scopus 로고
    • π-Stacking Interactions ALIVE and WELL in PROTEINS
    • McGaughey, G. B.; Gagné, M.; Rappé, A. K. π-Stacking Interactions ALIVE AND WELL IN PROTEINS J. Biol. Chem. 1998, 273, 15458-15463 10.1074/jbc.273.25.15458
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagné, M.2    Rappé, A.K.3
  • 62
    • 0025008168 scopus 로고
    • Sequence Logos: A New Way to Display Consensus Sequences
    • Schneider, T. D.; Stephens, R. M. Sequence Logos: A New Way to Display Consensus Sequences Nucleic Acids Res. 1990, 18, 6097-6100 10.1093/nar/18.20.6097
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 63
    • 84861210523 scopus 로고    scopus 로고
    • Nucleotide-Dependent Mechanism of Get3 as Elucidated from Free Energy Calculations
    • Wereszczynski, J.; McCammon, J. A. Nucleotide-Dependent Mechanism of Get3 as Elucidated from Free Energy Calculations Proc. Natl. Acad. Sci. U. S. A. 2012, 109, 7759-7764 10.1073/pnas.1117441109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 7759-7764
    • Wereszczynski, J.1    McCammon, J.A.2
  • 66
    • 5644273863 scopus 로고    scopus 로고
    • Identification of CC Chemokine Receptor 7 Residues Important for Receptor Activation
    • Ott, T. R.; Pahuja, A.; Nickolls, S. A.; Alleva, D. G.; Struthers, R. S. Identification of CC Chemokine Receptor 7 Residues Important for Receptor Activation J. Biol. Chem. 2004, 279, 42383-42392 10.1074/jbc.M401097200
    • (2004) J. Biol. Chem. , vol.279 , pp. 42383-42392
    • Ott, T.R.1    Pahuja, A.2    Nickolls, S.A.3    Alleva, D.G.4    Struthers, R.S.5
  • 67
    • 1642393757 scopus 로고    scopus 로고
    • Determinants of High-Affinity Binding and Receptor Activation in the N-Terminus of CCL-19 (MIP-3β)
    • Ott, T. R.; Lio, F. M.; Olshefski, D.; Liu, X.-J.; Struthers, R. S.; Ling, N. Determinants of High-Affinity Binding and Receptor Activation in the N-Terminus of CCL-19 (MIP-3β) Biochemistry 2004, 43, 3670-3678 10.1021/bi035895h
    • (2004) Biochemistry , vol.43 , pp. 3670-3678
    • Ott, T.R.1    Lio, F.M.2    Olshefski, D.3    Liu, X.-J.4    Struthers, R.S.5    Ling, N.6
  • 70
    • 70149112575 scopus 로고    scopus 로고
    • Structural Waters Define a Functional Channel Mediating Activation of the GPCR, Rhodopsin
    • Angel, T. E.; Gupta, S.; Jastrzebska, B.; Palczewski, K.; Chance, M. R. Structural Waters Define a Functional Channel Mediating Activation of the GPCR, Rhodopsin Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 14367-14372 10.1073/pnas.0901074106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14367-14372
    • Angel, T.E.1    Gupta, S.2    Jastrzebska, B.3    Palczewski, K.4    Chance, M.R.5
  • 71
    • 66649096395 scopus 로고    scopus 로고
    • Conserved Waters Mediate Structural and Functional Activation of Family A (rhodopsin-Like) G Protein-Coupled Receptors
    • Angel, T. E.; Chance, M. R.; Palczewski, K. Conserved Waters Mediate Structural and Functional Activation of Family A (rhodopsin-Like) G Protein-Coupled Receptors Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 8555-8560 10.1073/pnas.0903545106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8555-8560
    • Angel, T.E.1    Chance, M.R.2    Palczewski, K.3
  • 72
    • 84921026921 scopus 로고    scopus 로고
    • Activation of G-Protein-Coupled Receptors Correlates with the Formation of a Continuous Internal Water Pathway
    • Yuan, S.; Filipek, S.; Palczewski, K.; Vogel, H. Activation of G-Protein-Coupled Receptors Correlates with the Formation of a Continuous Internal Water Pathway Nat. Commun. 2014, 5, 4733 10.1038/ncomms5733
    • (2014) Nat. Commun. , vol.5 , pp. 4733
    • Yuan, S.1    Filipek, S.2    Palczewski, K.3    Vogel, H.4
  • 73
    • 84943329391 scopus 로고    scopus 로고
    • Biased Gs versus Gq and β-Arrestin Signaling in the NK1 Receptor Determined by Interactions in the Water Hydrogen-Bond Network
    • Valentin-Hansen, L.; Frimurer, T. M.; Mokrosinski, J.; Holliday, N. D.; Schwartz, T. W. Biased Gs versus Gq and β-Arrestin Signaling in the NK1 Receptor Determined by Interactions in the Water Hydrogen-Bond Network J. Biol. Chem. 2015, 290, 24495-24508 10.1074/jbc.M115.641944
    • (2015) J. Biol. Chem. , vol.290 , pp. 24495-24508
    • Valentin-Hansen, L.1    Frimurer, T.M.2    Mokrosinski, J.3    Holliday, N.D.4    Schwartz, T.W.5
  • 74
    • 44949236117 scopus 로고    scopus 로고
    • High-Resolution Distance Mapping in Rhodopsin Reveals the Pattern of Helix Movement due to Activation
    • Altenbach, C.; Kusnetzow, A. K.; Ernst, O. P.; Hofmann, K. P.; Hubbell, W. L. High-Resolution Distance Mapping in Rhodopsin Reveals the Pattern of Helix Movement due to Activation Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 7439-7444 10.1073/pnas.0802515105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 78
    • 80052082999 scopus 로고    scopus 로고
    • Structural Insights into Agonist-Induced Activation of G-Protein-Coupled Receptors
    • Deupi, X.; Standfuss, J. Structural Insights into Agonist-Induced Activation of G-Protein-Coupled Receptors Curr. Opin. Struct. Biol. 2011, 21, 541-551 10.1016/j.sbi.2011.06.002
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 79
    • 41149137801 scopus 로고    scopus 로고
    • Activation of G Protein-Coupled Receptors: Beyond Two-State Models and Tertiary Conformational Changes
    • Park, P. S.-H.; Lodowski, D. T.; Palczewski, K. Activation of G Protein-Coupled Receptors: Beyond Two-State Models and Tertiary Conformational Changes Annu. Rev. Pharmacol. Toxicol. 2008, 48, 107-141 10.1146/annurev.pharmtox.48.113006.094630
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 107-141
    • Park, P.S.-H.1    Lodowski, D.T.2    Palczewski, K.3
  • 80
    • 77952906089 scopus 로고    scopus 로고
    • Structure and Activation of the Visual Pigment Rhodopsin
    • Smith, S. O. Structure and Activation of the Visual Pigment Rhodopsin Annu. Rev. Biophys. 2010, 39, 309-328 10.1146/annurev-biophys-101209-104901
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 82
    • 84905040907 scopus 로고    scopus 로고
    • CCR7: Roles in Cancer Cell Dissemination, Migration and Metastasis Formation
    • Legler, D. F.; Uetz-von Allmen, E.; Hauser, M. A. CCR7: Roles in Cancer Cell Dissemination, Migration and Metastasis Formation Int. J. Biochem. Cell Biol. 2014, 54, 78-82 10.1016/j.biocel.2014.07.002
    • (2014) Int. J. Biochem. Cell Biol. , vol.54 , pp. 78-82
    • Legler, D.F.1    Uetz-Von Allmen, E.2    Hauser, M.A.3
  • 83
    • 77952231121 scopus 로고    scopus 로고
    • Induction of Lymphoidlike Stroma and Immune Escape by Tumors That Express the Chemokine CCL21
    • Shields, J. D.; Kourtis, I. C.; Tomei, A. A.; Roberts, J. M.; Swartz, M. A. Induction of Lymphoidlike Stroma and Immune Escape by Tumors That Express the Chemokine CCL21 Science 2010, 328, 749-752 10.1126/science.1185837
    • (2010) Science , vol.328 , pp. 749-752
    • Shields, J.D.1    Kourtis, I.C.2    Tomei, A.A.3    Roberts, J.M.4    Swartz, M.A.5
  • 85
    • 84924255532 scopus 로고    scopus 로고
    • The Role of CCL21/CCR7 Chemokine Axis in Breast Cancer-Induced Lymphangiogenesis
    • Tutunea-Fatan, E.; Majumder, M.; Xin, X.; Lala, P. K. The Role of CCL21/CCR7 Chemokine Axis in Breast Cancer-Induced Lymphangiogenesis Mol. Cancer 2015, 14, 35 10.1186/s12943-015-0306-4
    • (2015) Mol. Cancer , vol.14 , pp. 35
    • Tutunea-Fatan, E.1    Majumder, M.2    Xin, X.3    Lala, P.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.