메뉴 건너뛰기




Volumn 566, Issue 7742, 2019, Pages 79-84

Author Correction: Structural insights into the activation of metabotropic glutamate receptors (Nature, (2019), 566, 7742, (79-84), 10.1038/s41586-019-0881-4);Structural insights into the activation of metabotropic glutamate receptors

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; METABOTROPIC RECEPTOR; METABOTROPIC RECEPTOR 5; GRM5 PROTEIN, HUMAN; LIGAND;

EID: 85061007455     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/s41586-019-0983-z     Document Type: Erratum
Times cited : (233)

References (59)
  • 1
    • 77949516412 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: physiology, pharmacology, and disease
    • COI: 1:CAS:528:DC%2BC3cXisVelurg%3D, PID: 20055706
    • Niswender, C. M. & Conn, P. J. Metabotropic glutamate receptors: physiology, pharmacology, and disease. Annu. Rev. Pharmacol. Toxicol. 50, 295–322 (2010)
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 295-322
    • Niswender, C.M.1    Conn, P.J.2
  • 2
    • 85000366245 scopus 로고    scopus 로고
    • B receptor complexes
    • COI: 1:CAS:528:DC%2BC28XhvFylsLfM, PID: 27905440
    • B receptor complexes. Nature 540, 60–68 (2016)
    • (2016) Nature , vol.540 , pp. 60-68
    • Pin, J.-P.1    Bettler, B.2
  • 3
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • COI: 1:CAS:528:DC%2BD3cXnvVWqs74%3D, PID: 11069170
    • Kunishima, N. et al. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407, 971–977 (2000)
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 4
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • COI: 1:CAS:528:DC%2BD2cXmtVamtr8%3D, PID: 15235591
    • Kniazeff, J. et al. Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Nat. Struct. Mol. Biol. 11, 706–713 (2004)
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1
  • 5
    • 84865180885 scopus 로고    scopus 로고
    • Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1
    • PID: 22894836
    • Hlavackova, V. et al. Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1. Sci. Signal. 5, ra59 (2012)
    • (2012) Sci. Signal. , vol.5 , pp. ra59
    • Hlavackova, V.1
  • 6
    • 84897580006 scopus 로고    scopus 로고
    • Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator
    • COI: 1:CAS:528:DC%2BC2cXlt1eht78%3D, PID: 24603153
    • Wu, H. et al. Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator. Science 344, 58–64 (2014)
    • (2014) Science , vol.344 , pp. 58-64
    • Wu, H.1
  • 7
    • 84904994581 scopus 로고    scopus 로고
    • Structure of class C GPCR metabotropic glutamate receptor 5 transmembrane domain
    • PID: 25042998
    • Doré, A. S. et al. Structure of class C GPCR metabotropic glutamate receptor 5 transmembrane domain. Nature 511, 557–562 (2014)
    • (2014) Nature , vol.511 , pp. 557-562
    • Doré, A.S.1
  • 8
    • 84940544977 scopus 로고    scopus 로고
    • 5 negative allosteric modulator HTL14242 (3-chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile)
    • COI: 1:CAS:528:DC%2BC2MXht1Gms7%2FP, PID: 26225459
    • 5 negative allosteric modulator HTL14242 (3-chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile). J. Med. Chem. 58, 6653–6664 (2015)
    • (2015) J. Med. Chem. , vol.58 , pp. 6653-6664
    • Christopher, J.A.1
  • 9
    • 85059808266 scopus 로고    scopus 로고
    • Structure-based optimization strategies for G protein-coupled receptor (GPCR) allosteric modulators: A case study from analyses of new metabotropic glutamate receptor 5 (mGlu 5) X-ray structures
    • 5) X-ray structures. J. Med. Chem. 10.1021/acs.jmedchem.7b01722 (2018)
    • (2018) J. Med. Chem.
    • Christopher, J.A.1
  • 10
    • 85049650721 scopus 로고    scopus 로고
    • Structural insights into G-protein-coupled receptor allostery
    • COI: 1:CAS:528:DC%2BC1cXht1Ojt7rF, PID: 29973731
    • Thal, D. M., Glukhova, A., Sexton, P. M. & Christopoulos, A. Structural insights into G-protein-coupled receptor allostery. Nature 559, 45–53 (2018)
    • (2018) Nature , vol.559 , pp. 45-53
    • Thal, D.M.1    Glukhova, A.2    Sexton, P.M.3    Christopoulos, A.4
  • 11
    • 0346458626 scopus 로고    scopus 로고
    • Heptahelical domain of metabotropic glutamate receptor 5 behaves like rhodopsin-like receptors
    • COI: 1:CAS:528:DC%2BD2cXjvFaksg%3D%3D, PID: 14691258
    • Goudet, C. et al. Heptahelical domain of metabotropic glutamate receptor 5 behaves like rhodopsin-like receptors. Proc. Natl Acad. Sci. USA 101, 378–383 (2004)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 378-383
    • Goudet, C.1
  • 12
    • 84867045173 scopus 로고    scopus 로고
    • Distinct roles of metabotropic glutamate receptor dimerization in agonist activation and G-protein coupling
    • COI: 1:CAS:528:DC%2BC38XhsFGktLzL, PID: 22988116
    • El Moustaine, D. et al. Distinct roles of metabotropic glutamate receptor dimerization in agonist activation and G-protein coupling. Proc. Natl Acad. Sci. 109, 16342–16347 (2012)
    • (2012) Proc. Natl Acad. Sci. , vol.109 , pp. 16342-16347
    • El Moustaine, D.1
  • 13
    • 85009073084 scopus 로고    scopus 로고
    • Nanobodies to study G protein-coupled receptor structure and function
    • COI: 1:CAS:528:DC%2BC28XitVyis73N, PID: 27959623
    • Manglik, A., Kobilka, B. K. & Steyaert, J. Nanobodies to study G protein-coupled receptor structure and function. Annu. Rev. Pharmacol. Toxicol. 57, 19–37 (2017)
    • (2017) Annu. Rev. Pharmacol. Toxicol. , vol.57 , pp. 19-37
    • Manglik, A.1    Kobilka, B.K.2    Steyaert, J.3
  • 14
    • 20144381462 scopus 로고    scopus 로고
    • A novel selective positive allosteric modulator of metabotropic glutamate receptor subtype 5 has in vivo activity and antipsychotic-like effects in rat behavioral models
    • COI: 1:CAS:528:DC%2BD2MXjtlSnsLg%3D, PID: 15608073
    • Kinney, G. G. et al. A novel selective positive allosteric modulator of metabotropic glutamate receptor subtype 5 has in vivo activity and antipsychotic-like effects in rat behavioral models. J. Pharmacol. Exp. Ther. 313, 199–206 (2005)
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , pp. 199-206
    • Kinney, G.G.1
  • 15
    • 84867831749 scopus 로고    scopus 로고
    • Investigating metabotropic glutamate receptor 5 allosteric modulator cooperativity, affinity, and agonism: enriching structure-function studies and structure-activity relationships
    • COI: 1:CAS:528:DC%2BC38XhsFKktLvF, PID: 22863693
    • Gregory, K. J. et al. Investigating metabotropic glutamate receptor 5 allosteric modulator cooperativity, affinity, and agonism: enriching structure-function studies and structure-activity relationships. Mol. Pharmacol. 82, 860–875 (2012)
    • (2012) Mol. Pharmacol. , vol.82 , pp. 860-875
    • Gregory, K.J.1
  • 16
    • 79954988501 scopus 로고    scopus 로고
    • Quantitative analysis reveals multiple mechanisms of allosteric modulation of the mGlu5 receptor in rat astroglia
    • COI: 1:CAS:528:DC%2BC3MXls1OltL0%3D, PID: 21321061
    • Bradley, S. J., Langmead, C. J., Watson, J. M. & Challiss, R. A. J. Quantitative analysis reveals multiple mechanisms of allosteric modulation of the mGlu5 receptor in rat astroglia. Mol. Pharmacol. 79, 874–885 (2011)
    • (2011) Mol. Pharmacol. , vol.79 , pp. 874-885
    • Bradley, S.J.1    Langmead, C.J.2    Watson, J.M.3    Challiss, R.A.J.4
  • 17
    • 84862964996 scopus 로고    scopus 로고
    • Functional impact of allosteric agonist activity of selective positive allosteric modulators of metabotropic glutamate receptor subtype 5 in regulating central nervous system function
    • COI: 1:CAS:528:DC%2BC38XjtVSkt7s%3D, PID: 22021324
    • Noetzel, M. J. et al. Functional impact of allosteric agonist activity of selective positive allosteric modulators of metabotropic glutamate receptor subtype 5 in regulating central nervous system function. Mol. Pharmacol. 81, 120–133 (2012)
    • (2012) Mol. Pharmacol. , vol.81 , pp. 120-133
    • Noetzel, M.J.1
  • 18
    • 73149087939 scopus 로고    scopus 로고
    • 2+ signaling initiated by the type 5 metabotropic glutamate receptor
    • COI: 1:CAS:528:DC%2BD1MXhsFajtbzJ, PID: 19737913
    • 2+ signaling initiated by the type 5 metabotropic glutamate receptor. Mol. Pharmacol. 76, 1302–1313 (2009)
    • (2009) Mol. Pharmacol. , vol.76 , pp. 1302-1313
    • Bradley, S.J.1    Watson, J.M.2    Challiss, R.A.J.3
  • 19
    • 84876065856 scopus 로고    scopus 로고
    • Illuminating the activation mechanisms and allosteric properties of metabotropic glutamate receptors
    • COI: 1:CAS:528:DC%2BC3sXnsFCmsL8%3D, PID: 23487753
    • Doumazane, E. et al. Illuminating the activation mechanisms and allosteric properties of metabotropic glutamate receptors. Proc. Natl Acad. Sci. USA 110, E1416–E1425 (2013)
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E1416-E1425
    • Doumazane, E.1
  • 20
    • 85007099137 scopus 로고    scopus 로고
    • Discovery of (1S,2R,3S,4S,5R,6R)-2-amino-3-[(3,4-difluorophenyl)sulfanylmethyl]-4-hydroxy-bicyclo[3.1.0]hexane-2,6-dicarboxylic acid hydrochloride (LY3020371·HCl): A potent, metabotropic glutamate 2/3 receptor antagonist with antidepressant-like activity
    • COI: 1:CAS:528:DC%2BC28XhvVCjsL%2FJ, PID: 28002967
    • Chappell, M. D. et al. Discovery of (1S,2R,3S,4S,5R,6R)-2-amino-3-[(3,4-difluorophenyl)sulfanylmethyl]-4-hydroxy-bicyclo[3.1.0]hexane-2,6-dicarboxylic acid hydrochloride (LY3020371·HCl): A potent, metabotropic glutamate 2/3 receptor antagonist with antidepressant-like activity. J. Med. Chem. 59, 10974–10993 (2016)
    • (2016) J. Med. Chem. , vol.59 , pp. 10974-10993
    • Chappell, M.D.1
  • 21
    • 80053057994 scopus 로고    scopus 로고
    • Interdomain movements in metabotropic glutamate receptor activation
    • COI: 1:CAS:528:DC%2BC3MXht1KisLjO, PID: 21896740
    • Huang, S. et al. Interdomain movements in metabotropic glutamate receptor activation. Proc. Natl Acad. Sci. USA 108, 15480–15485 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15480-15485
    • Huang, S.1
  • 22
    • 34447520294 scopus 로고    scopus 로고
    • 18F-labeling of 3-fluoro-5-(2-(2-(fluoromethyl)thiazol-4-yl)ethynyl)benzonitrile as a high affinity radioligand for imaging monkey brain metabotropic glutamate subtype-5 receptors with positron emission tomography
    • PID: 17571866
    • 18F-labeling of 3-fluoro-5-(2-(2-(fluoromethyl)thiazol-4-yl)ethynyl)benzonitrile as a high affinity radioligand for imaging monkey brain metabotropic glutamate subtype-5 receptors with positron emission tomography. J. Med. Chem. 50, 3256–3266 (2007)
    • (2007) J. Med. Chem. , vol.50 , pp. 3256-3266
    • Siméon, F.G.1
  • 23
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • COI: 1:CAS:528:DC%2BD2sXjt1ymsrs%3D, PID: 17360426
    • Muto, T., Tsuchiya, D., Morikawa, K. & Jingami, H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc. Natl Acad. Sci. USA 104, 3759–3764 (2007)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 24
    • 0034602293 scopus 로고    scopus 로고
    • Cys-140 is critical for metabotropic glutamate receptor-1 dimerization
    • COI: 1:CAS:528:DC%2BD3cXotFWls74%3D, PID: 10945991
    • Ray, K. & Hauschild, B. C. Cys-140 is critical for metabotropic glutamate receptor-1 dimerization. J. Biol. Chem. 275, 34245–34251 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 34245-34251
    • Ray, K.1    Hauschild, B.C.2
  • 25
    • 84930226866 scopus 로고    scopus 로고
    • 2-adrenergic receptor signaling
    • COI: 1:CAS:528:DC%2BC2MXosVaqsLw%3D, PID: 25981665
    • 2-adrenergic receptor signaling. Cell 161, 1101–1111 (2015)
    • (2015) Cell , vol.161 , pp. 1101-1111
    • Manglik, A.1
  • 26
    • 78651399683 scopus 로고    scopus 로고
    • 2 adrenoceptor complex
    • COI: 1:CAS:528:DC%2BC3MXkvFehsQ%3D%3D, PID: 21228876
    • 2 adrenoceptor complex. Nature 469, 236–240 (2011)
    • (2011) Nature , vol.469 , pp. 236-240
    • Rosenbaum, D.M.1
  • 27
    • 84992700373 scopus 로고    scopus 로고
    • Mechanism of assembly and cooperativity of homomeric and heteromeric metabotropic glutamate receptors
    • COI: 1:CAS:528:DC%2BC28XhsFajsLjP, PID: 27641494
    • Levitz, J. et al. Mechanism of assembly and cooperativity of homomeric and heteromeric metabotropic glutamate receptors. Neuron 92, 143–159 (2016)
    • (2016) Neuron , vol.92 , pp. 143-159
    • Levitz, J.1
  • 28
    • 85049448496 scopus 로고    scopus 로고
    • Identifying G protein-coupled receptor dimers from crystal packings
    • COI: 1:CAS:528:DC%2BC1cXht1KlsLjE
    • Stenkamp, R. E. Identifying G protein-coupled receptor dimers from crystal packings. Acta Crystallogr. D 74, 655–670 (2018)
    • (2018) Acta Crystallogr. D , vol.74 , pp. 655-670
    • Stenkamp, R.E.1
  • 29
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerization: contribution to pharmacology and function
    • COI: 1:CAS:528:DC%2BD1MXhsVKmu7nO, PID: 19309353
    • Milligan, G. G protein-coupled receptor hetero-dimerization: contribution to pharmacology and function. Br. J. Pharmacol. 158, 5–14 (2009)
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 5-14
    • Milligan, G.1
  • 30
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • COI: 1:CAS:528:DC%2BD28Xht1Wqu77P, PID: 17086179
    • James, J. R., Oliveira, M. I., Carmo, A. M., Iaboni, A. & Davis, S. J. A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nat. Methods 3, 1001–1006 (2006)
    • (2006) Nat. Methods , vol.3 , pp. 1001-1006
    • James, J.R.1    Oliveira, M.I.2    Carmo, A.M.3    Iaboni, A.4    Davis, S.J.5
  • 31
    • 84919704267 scopus 로고    scopus 로고
    • Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer
    • COI: 1:CAS:528:DC%2BC2cXitFKltL%2FI, PID: 25503927
    • Xue, L. et al. Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer. Nat. Chem. Biol. 11, 134–140 (2015)
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 134-140
    • Xue, L.1
  • 32
    • 84920166693 scopus 로고    scopus 로고
    • Generic GPCR residue numbers – aligning topology maps while minding the gaps
    • COI: 1:CAS:528:DC%2BC2cXitVSgu7rK, PID: 25541108
    • Isberg, V. et al. Generic GPCR residue numbers – aligning topology maps while minding the gaps. Trends Pharmacol. Sci. 36, 22–31 (2015)
    • (2015) Trends Pharmacol. Sci. , vol.36 , pp. 22-31
    • Isberg, V.1
  • 35
    • 84983057081 scopus 로고    scopus 로고
    • Structural mechanism of ligand activation in human calcium-sensing receptor
    • PID: 27434672
    • Geng, Y. et al. Structural mechanism of ligand activation in human calcium-sensing receptor. eLife 5, e13662 (2016)
    • (2016) eLife , vol.5
    • Geng, Y.1
  • 36
    • 0027396317 scopus 로고
    • Characterization of metabotropic glutamate receptors coupled to a pertussis toxin sensitive G-protein in bovine brain coated vesicles
    • PID: 8420805
    • Martín, M., Sanz, J. M. & Cubero, A. Characterization of metabotropic glutamate receptors coupled to a pertussis toxin sensitive G-protein in bovine brain coated vesicles. FEBS Lett. 316, 191–196 (1993)
    • (1993) FEBS Lett. , vol.316 , pp. 191-196
    • Martín, M.1    Sanz, J.M.2    Cubero, A.3
  • 37
    • 84956726555 scopus 로고    scopus 로고
    • Molecular mechanism of positive allosteric modulation of the metabotropic glutamate receptor 2 by JNJ-46281222
    • COI: 1:CAS:528:DC%2BC28XnvVOlsw%3D%3D, PID: 26589404
    • Doornbos, M. L. J. et al. Molecular mechanism of positive allosteric modulation of the metabotropic glutamate receptor 2 by JNJ-46281222. Br. J. Pharmacol. 173, 588–600 (2016)
    • (2016) Br. J. Pharmacol. , vol.173 , pp. 588-600
    • Doornbos, M.L.J.1
  • 38
    • 76449099287 scopus 로고    scopus 로고
    • XDS
    • COI: 1:CAS:528:DC%2BC3cXhs1SisLc%3D, PID: 20124692
    • Kabsch, W. XDS. Acta Crystallogr. D 66, 125–132 (2010)
    • (2010) Acta Crystallogr. D , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 39
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • PID: 16369096
    • Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D 62, 72–82 (2006)
    • (2006) Acta Crystallogr. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 40
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • COI: 1:CAS:528:DC%2BC3MXktFWqt70%3D, PID: 21460441
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235–242 (2011)
    • (2011) Acta Crystallogr. D , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 41
    • 85050235281 scopus 로고    scopus 로고
    • SWISS-MODEL: homology modelling of protein structures and complexes
    • PID: 29788355
    • Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 46, W296–W303 (2018)
    • (2018) Nucleic Acids Res. , vol.46 , pp. W296-W303
    • Waterhouse, A.1
  • 42
    • 80053642374 scopus 로고    scopus 로고
    • The Phenix software for automated determination of macromolecular structures
    • COI: 1:CAS:528:DC%2BC3MXhtlaqt73F, PID: 21821126
    • Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94–106 (2011)
    • (2011) Methods , vol.55 , pp. 94-106
    • Adams, P.D.1
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • PID: 15572765
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 85049454428 scopus 로고    scopus 로고
    • Global Phasing, Cambridge
    • Bricogne, G. et al. BUSTER v.2.10.3 (Global Phasing, Cambridge, 2017)
    • (2017) BUSTER v.2.10.3
    • Bricogne, G.1
  • 45
    • 84860287260 scopus 로고    scopus 로고
    • Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER
    • COI: 1:CAS:528:DC%2BC38Xlt1Gns78%3D, PID: 22505257
    • Smart, O. S. et al. Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER. Acta Crystallogr. D 68, 368–380 (2012)
    • (2012) Acta Crystallogr. D , vol.68 , pp. 368-380
    • Smart, O.S.1
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • COI: 1:STN:280:DC%2BD2czpsFegsw%3D%3D, PID: 15299926
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240–255 (1997)
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
    • 85035199313 scopus 로고    scopus 로고
    • MolProbity: More and better reference data for improved all-atom structure validation
    • COI: 1:CAS:528:DC%2BC2sXhvVKgsrnO, PID: 29067766
    • Williams, C. J. et al. MolProbity: More and better reference data for improved all-atom structure validation. Protein Sci. 27, 293–315 (2018)
    • (2018) Protein Sci. , vol.27 , pp. 293-315
    • Williams, C.J.1
  • 48
    • 84894623293 scopus 로고    scopus 로고
    • A general protocol for the generation of nanobodies for structural biology
    • COI: 1:CAS:528:DC%2BC2cXmtVegsr8%3D, PID: 24577359
    • Pardon, E. et al. A general protocol for the generation of nanobodies for structural biology. Nat. Protoc. 9, 674–693 (2014)
    • (2014) Nat. Protoc. , vol.9 , pp. 674-693
    • Pardon, E.1
  • 49
    • 0037448394 scopus 로고    scopus 로고
    • 3-[(2-Methyl-1,3-thiazol-4-yl)ethynyl]-pyridine: a potent and highly selective metabotropic glutamate subtype 5 receptor antagonist with anxiolytic activity
    • COI: 1:CAS:528:DC%2BD38XpsVensLk%3D, PID: 12519057
    • Cosford, N. D. P. et al. 3-[(2-Methyl-1,3-thiazol-4-yl)ethynyl]-pyridine: a potent and highly selective metabotropic glutamate subtype 5 receptor antagonist with anxiolytic activity. J. Med. Chem. 46, 204–206 (2003)
    • (2003) J. Med. Chem. , vol.46 , pp. 204-206
    • Cosford, N.D.P.1
  • 50
    • 80054750375 scopus 로고    scopus 로고
    • Reconstitution of G protein-coupled receptors into a model bilayer system: reconstituted high-density lipoprotein particles
    • PID: 21870225
    • Vélez-Ruiz, G. A. & Sunahara, R. K. Reconstitution of G protein-coupled receptors into a model bilayer system: reconstituted high-density lipoprotein particles. Methods Mol. Biol. 756, 167–182 (2011)
    • (2011) Methods Mol. Biol. , vol.756 , pp. 167-182
    • Vélez-Ruiz, G.A.1    Sunahara, R.K.2
  • 51
    • 8644252687 scopus 로고    scopus 로고
    • Discovery of positive allosteric modulators for the metabotropic glutamate receptor subtype 5 from a series of N-(1,3-diphenyl-1H- pyrazol-5-yl)benzamides that potentiate receptor function in vivo
    • COI: 1:CAS:528:DC%2BD2cXovVKgtLc%3D, PID: 15537338
    • Lindsley, C. W. et al. Discovery of positive allosteric modulators for the metabotropic glutamate receptor subtype 5 from a series of N-(1,3-diphenyl-1H- pyrazol-5-yl)benzamides that potentiate receptor function in vivo. J. Med. Chem. 47, 5825–5828 (2004)
    • (2004) J. Med. Chem. , vol.47 , pp. 5825-5828
    • Lindsley, C.W.1
  • 52
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • COI: 1:CAS:528:DC%2BC2sXjt1ags7g%3D, PID: 5494038
    • Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y. & Agard, D. A. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017)
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1    Palovcak, E.2    Armache, J.-P.3    Verba, K.A.4    Cheng, Y.5    Agard, D.A.6
  • 53
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • COI: 1:CAS:528:DC%2BC2MXhvVOqsbzF, PID: 4711343
    • Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016)
    • (2016) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 54
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • COI: 1:CAS:528:DC%2BC38Xhs12jsLvO, PID: 3690530
    • Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012)
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 55
    • 85011645437 scopus 로고    scopus 로고
    • cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
    • COI: 1:CAS:528:DC%2BC2sXitlGisbs%3D, PID: 28165473
    • Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017)
    • (2017) Nat. Methods , vol.14 , pp. 290-296
    • Punjani, A.1    Rubinstein, J.L.2    Fleet, D.J.3    Brubaker, M.A.4
  • 56
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • COI: 1:CAS:528:DC%2BD28XhtlaltrfF, PID: 17011211
    • Heymann, J. B. & Belnap, D. M. Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157, 3–18 (2007)
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 57
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • COI: 1:CAS:528:DyaK28Xis12nsrg%3D, PID: 8744570, 27–28
    • Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 33–38, 27–28 (1996)
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 58
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • COI: 1:CAS:528:DC%2BD2MXht1SlsbbJ, PID: 2486339
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781–1802 (2005)
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 59
    • 84943528301 scopus 로고    scopus 로고
    • Improved peptide and protein torsional energetics with the OPLSAA force field
    • COI: 1:CAS:528:DC%2BC2MXpsFOlsbc%3D, PID: 26190950
    • Robertson, M. J., Tirado-Rives, J. & Jorgensen, W. L. Improved peptide and protein torsional energetics with the OPLSAA force field. J. Chem. Theory Comput. 11, 3499–3509 (2015)
    • (2015) J. Chem. Theory Comput. , vol.11 , pp. 3499-3509
    • Robertson, M.J.1    Tirado-Rives, J.2    Jorgensen, W.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.