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Volumn 504, Issue 7479, 2013, Pages 254-259

Structural mechanism of ligand activation in human GABA B receptor

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; 4 AMINOBUTYRIC ACID B RECEPTOR 1; 4 AMINOBUTYRIC ACID B RECEPTOR 2; UNCLASSIFIED DRUG;

EID: 84890434896     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12725     Document Type: Article
Times cited : (164)

References (62)
  • 1
    • 3042546515 scopus 로고    scopus 로고
    • Molecular structure and physiological functions of GABA(B) receptors
    • Bettler, B., Kaupmann, K., Mosbacher, J. & Gassmann, M. Molecular structure and physiological functions of GABA(B) receptors. Physiol. Rev. 84, 835-867 (2004)
    • (2004) Physiol. Rev. , vol.84 , pp. 835-867
    • Bettler, B.1    Kaupmann, K.2    Mosbacher, J.3    Gassmann, M.4
  • 2
    • 0036259020 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXXIII. Mammalian gamma-aminobutyric acid(B) receptors: Structure and function
    • Bowery, N. G. et al. International Union of Pharmacology. XXXIII. Mammalian gamma-aminobutyric acid(B) receptors: structure and function. Pharmacol. Rev. 54, 247-264 (2002)
    • (2002) Pharmacol. Rev. , vol.54 , pp. 247-264
    • Bowery, N.G.1
  • 3
    • 77955068362 scopus 로고    scopus 로고
    • Chemistry and pharmacology of GABAB receptor ligands
    • Froestl, W. Chemistry and pharmacology of GABAB receptor ligands. Adv. Pharmacol. 58, 19-62 (2010)
    • (2010) Adv. Pharmacol. , vol.58 , pp. 19-62
    • Froestl, W.1
  • 4
    • 3042628452 scopus 로고    scopus 로고
    • The activation mechanism of class-C G-protein coupled receptors
    • Pin, J. P. et al. The activation mechanism of class-C G-protein coupled receptors. Biol. Cell 96, 335-342 (2004)
    • (2004) Biol. Cell , vol.96 , pp. 335-342
    • Pin, J.P.1
  • 5
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • Romano, C., Yang, W. L. & O'Malley, K. L. Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J. Biol. Chem. 271, 28612-28616 (1996)
    • (1996) J. Biol. Chem. , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.L.2    O'malley, K.L.3
  • 6
    • 0032557433 scopus 로고    scopus 로고
    • Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1
    • Okamoto, T. et al. Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1. J. Biol. Chem. 273, 13089-13096 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 13089-13096
    • Okamoto, T.1
  • 7
    • 0034623081 scopus 로고    scopus 로고
    • Cryptic dimer interface and domain organization of the extracellular region of metabotropic glutamate receptor subtype 1
    • Tsuji, Y. et al. Cryptic dimer interface and domain organization of the extracellular region of metabotropic glutamate receptor subtype 1. J. Biol. Chem. 275, 28144-28151 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 28144-28151
    • Tsuji, Y.1
  • 8
    • 0032483541 scopus 로고    scopus 로고
    • Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells
    • Bai, M., Trivedi, S. & Brown, E. M. Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells. J. Biol. Chem. 273, 23605-23610 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 23605-23610
    • Bai, M.1    Trivedi, S.2    Brown, E.M.3
  • 9
    • 0005169503 scopus 로고    scopus 로고
    • GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2
    • Jones, K. A. et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature 396, 674-679 (1998)
    • (1998) Nature , vol.396 , pp. 674-679
    • Jones, K.A.1
  • 10
    • 0032542382 scopus 로고    scopus 로고
    • GABA(B)-receptor subtypes assemble into functional heteromeric complexes
    • Kaupmann, K. et al. GABA(B)-receptor subtypes assemble into functional heteromeric complexes. Nature 396, 683-687 (1998)
    • (1998) Nature , vol.396 , pp. 683-687
    • Kaupmann, K.1
  • 11
    • 17444380779 scopus 로고    scopus 로고
    • Heterodimerization is required for the formation of a functional GABA(B) receptor
    • White, J. H. et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature 396, 679-682 (1998)
    • (1998) Nature , vol.396 , pp. 679-682
    • White, J.H.1
  • 12
    • 0032929331 scopus 로고    scopus 로고
    • Role of heteromer formation in GABAB receptor function
    • Kuner, R. et al. Role of heteromer formation in GABAB receptor function. Science 283, 74-77 (1999)
    • (1999) Science , vol.283 , pp. 74-77
    • Kuner, R.1
  • 13
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerization: Contribution to pharmacology and function
    • 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
  • 14
    • 0033582820 scopus 로고    scopus 로고
    • Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity
    • Ng, G. Y. et al. Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity. J. Biol. Chem. 274, 7607-7610 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 7607-7610
    • Ng, G.Y.1
  • 15
    • 0035839040 scopus 로고    scopus 로고
    • Mammalian sweet taste receptors
    • Nelson, G. et al. Mammalian sweet taste receptors. Cell 106, 381-390 (2001)
    • (2001) Cell , vol.106 , pp. 381-390
    • Nelson, G.1
  • 16
    • 0037075555 scopus 로고    scopus 로고
    • An amino-acid taste receptor
    • Nelson, G. et al. An amino-acid taste receptor. Nature 416, 199-202 (2002)
    • (2002) Nature , vol.416 , pp. 199-202
    • Nelson, G.1
  • 17
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic, M., Jan, Y. N. & Jan, L. Y. A trafficking checkpoint controls GABA(B) receptor heterodimerization. Neuron 27, 97-106 (2000)
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 18
    • 0035866088 scopus 로고    scopus 로고
    • C-terminal interaction is essential for surface trafficking but not for heteromeric assembly of GABA(b) receptors
    • Pagano, A. et al. C-terminal interaction is essential for surface trafficking but not for heteromeric assembly of GABA(b) receptors. J. Neurosci. 21, 1189-1202 (2001)
    • (2001) J. Neurosci. , vol.21 , pp. 1189-1202
    • Pagano, A.1
  • 19
    • 0030894681 scopus 로고    scopus 로고
    • Expression cloning ofGABA(B) receptorsuncovers similarity to metabotropic glutamate receptors
    • Kaupmann, K. et al. Expression cloning ofGABA(B) receptorsuncovers similarity to metabotropic glutamate receptors. Nature 386, 239-246 (1997)
    • (1997) Nature , vol.386 , pp. 239-246
    • Kaupmann, K.1
  • 20
    • 0032771147 scopus 로고    scopus 로고
    • The N-terminal domain of gamma-aminobutyric Acid(B) receptors is sufficient to specify agonist and antagonist binding
    • Malitschek, B. et al. The N-terminal domain of gamma-aminobutyric Acid(B) receptors is sufficient to specify agonist and antagonist binding. Mol. Pharmacol. 56, 448-454 (1999)
    • (1999) Mol. Pharmacol. , vol.56 , pp. 448-454
    • Malitschek, B.1
  • 21
    • 0036759170 scopus 로고    scopus 로고
    • No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits
    • Kniazeff, J., Galvez, T., Labesse, G. & Pin, J. P. No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits. J. Neurosci. 22, 7352-7361 (2002)
    • (2002) J. Neurosci. , vol.22 , pp. 7352-7361
    • Kniazeff, J.1    Galvez, T.2    Labesse, G.3    Pin, J.P.4
  • 22
    • 0035341213 scopus 로고    scopus 로고
    • Allosteric interactions between GB1 andGB2 subunits are required for optimal GABA(B) receptor function
    • Galvez, T. et al. Allosteric interactions between GB1 andGB2 subunits are required for optimal GABA(B) receptor function. EMBO J. 20, 2152-2159 (2001)
    • (2001) EMBO J. , vol.20 , pp. 2152-2159
    • Galvez, T.1
  • 23
    • 1942469528 scopus 로고    scopus 로고
    • Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit
    • Liu, J. et al. Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit. J. Biol. Chem. 279, 15824-15830 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 15824-15830
    • Liu, J.1
  • 24
    • 41949131778 scopus 로고    scopus 로고
    • Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor
    • Nomura, R., Suzuki, Y., Kakizuka, A. &Jingami, H. Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor. J. Biol. Chem. 283, 4665-4673 (2008)
    • (2008) J. Biol. Chem. , vol.283 , pp. 4665-4673
    • Nomura, R.1    Suzuki, Y.2    Kakizuka, A.3    Jingami, H.4
  • 25
    • 78650920787 scopus 로고    scopus 로고
    • Trans-activation between 7TM domains: Implication in heterodimeric GABA(B) receptor activation
    • Monnier, C. et al. Trans-activation between 7TM domains: implication in heterodimeric GABA(B) receptor activation. EMBO J. 30, 32-42 (2011)
    • (2011) EMBO J. , vol.30 , pp. 32-42
    • Monnier, C.1
  • 26
    • 84862842176 scopus 로고    scopus 로고
    • Structure and functional interaction of the extracellular domain of human GABAB receptor GBR2
    • Geng, Y. et al. Structure and functional interaction of the extracellular domain of human GABAB receptor GBR2. Nature Neurosci. 15, 970-978 (2012)
    • (2012) Nature Neurosci. , vol.15 , pp. 970-978
    • Geng, Y.1
  • 27
    • 0035807889 scopus 로고    scopus 로고
    • Ligand-induced signal transduction within heterodimeric GABA(B) receptor
    • Margeta-Mitrovic, M., Jan, Y. N. & Jan, L. Y. Ligand-induced signal transduction within heterodimeric GABA(B) receptor. Proc. Natl Acad. Sci. USA 98, 14643-14648 (2001)
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14643-14648
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 28
    • 0035807875 scopus 로고    scopus 로고
    • Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors
    • Margeta-Mitrovic, M., Jan, Y. N. & Jan, L. Y. Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors. Proc. Natl Acad. Sci. USA 98, 14649-14654 (2001)
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14649-14654
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 29
    • 0035887699 scopus 로고    scopus 로고
    • GABA(B2) is essential for g-protein coupling of the GABA(B) receptor heterodimer
    • Robbins, M. J. et al. GABA(B2) is essential for g-protein coupling of the GABA(B) receptor heterodimer. J. Neurosci. 21, 8043-8052 (2001)
    • (2001) J. Neurosci. , vol.21 , pp. 8043-8052
    • Robbins, M.J.1
  • 30
    • 0036479250 scopus 로고    scopus 로고
    • A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor
    • Duthey, B. et al. A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor. J. Biol. Chem. 277, 3236-3241 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 3236-3241
    • Duthey, B.1
  • 31
    • 0036073523 scopus 로고    scopus 로고
    • The intracellular loops of the GB2 subunit are crucial for G-protein coupling of the heteromeric gamma-aminobutyrate B receptor
    • Havlickova, M. et al. The intracellular loops of the GB2 subunit are crucial for G-protein coupling of the heteromeric gamma-aminobutyrate B receptor. Mol. Pharmacol. 62, 343-350 (2002)
    • (2002) Mol. Pharmacol. , vol.62 , pp. 343-350
    • Havlickova, M.1
  • 32
    • 4644296105 scopus 로고    scopus 로고
    • Activation mechanism of the heterodimeric GABA(B) receptor
    • Pin, J. P. et al. Activation mechanism of the heterodimeric GABA(B) receptor. Biochem. Pharmacol. 68, 1565-1572 (2004)
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1565-1572
    • Pin, J.P.1
  • 33
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • 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
  • 34
    • 0037022586 scopus 로고    scopus 로고
    • Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd31
    • Tsuchiya, D., Kunishima, N., Kamiya, N., Jingami, H. &Morikawa, K. Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd31. Proc. Natl Acad. Sci. USA 99, 2660-2665 (2002)
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 35
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • 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
  • 36
    • 0034612573 scopus 로고    scopus 로고
    • Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor
    • van den Akker, F. et al. Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor. Nature 406, 101-104 (2000)
    • (2000) Nature , vol.406 , pp. 101-104
    • Van Den Akker, F.1
  • 37
    • 0035979721 scopus 로고    scopus 로고
    • Allosteric activationof a spring-loaded natriuretic peptide receptor dimer by hormone
    • He, X.,Chow, D.,Martick, M. M. &Garcia, K. C. Allosteric activationof a spring-loaded natriuretic peptide receptor dimer by hormone. Science 293, 1657-1662 (2001)
    • (2001) Science , vol.293 , pp. 1657-1662
    • He, X.1    Chow, D.2    Martick, M.M.3    Garcia, K.C.4
  • 38
    • 67649565613 scopus 로고    scopus 로고
    • Crystal structure and association behaviour of the GluR2 aminoterminal domain
    • Jin, R. et al. Crystal structure and association behaviour of the GluR2 aminoterminal domain. EMBO J. 28, 1812-1823 (2009)
    • (2009) EMBO J. , vol.28 , pp. 1812-1823
    • Jin, R.1
  • 39
    • 72449151659 scopus 로고    scopus 로고
    • Structure of the zinc-bound aminoterminal domain of the NMDA receptor NR2B subunit
    • Karakas, E., Simorowski, N. & Furukawa, H. Structure of the zinc-bound aminoterminal domain of the NMDA receptor NR2B subunit. EMBO J. 28, 3910-3920 (2009)
    • (2009) EMBO J. , vol.28 , pp. 3910-3920
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 40
    • 67349285101 scopus 로고    scopus 로고
    • The N-terminal domain of GluR6-subtype glutamate receptor ion channels
    • Kumar, J., Schuck, P., Jin, R. & Mayer, M. L. The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nature Struct. Mol. Biol. 16, 631-638 (2009)
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 631-638
    • Kumar, J.1    Schuck, P.2    Jin, R.3    Mayer, M.L.4
  • 41
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack, J. S., Saper, M. A. & Quiocho, F. A. Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 206, 171-191 (1989)
    • (1989) J. Mol. Biol. , vol.206 , pp. 171-191
    • Sack, J.S.1    Saper, M.A.2    Quiocho, F.A.3
  • 42
    • 1642499173 scopus 로고    scopus 로고
    • Locking the dimeric GABA(B) G-protein-coupled receptor in its active state
    • Kniazeff, J. et al. Locking the dimeric GABA(B) G-protein-coupled receptor in its active state. J. Neurosci. 24, 370-377 (2004)
    • (2004) J. Neurosci. , vol.24 , pp. 370-377
    • Kniazeff, J.1
  • 43
    • 43249098905 scopus 로고    scopus 로고
    • Functioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning
    • Rondard, P. et al. Functioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning. EMBO J. 27, 1321-1332 (2008)
    • (2008) EMBO J. , vol.27 , pp. 1321-1332
    • Rondard, P.1
  • 44
    • 0033531793 scopus 로고    scopus 로고
    • Mutagenesis and modeling of the GABAB receptor extracellular domain support a venus flytrap mechanismfor ligand binding
    • Galvez, T. et al. Mutagenesis and modeling of the GABAB receptor extracellular domain support a venus flytrap mechanismfor ligand binding. J. Biol. Chem. 274, 13362-13369 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 13362-13369
    • Galvez, T.1
  • 45
    • 0034731374 scopus 로고    scopus 로고
    • Mapping the agonist-binding site of GABAB type 1 subunit sheds light on the activation process of GABAB receptors
    • Galvez, T. et al. Mapping the agonist-binding site of GABAB type 1 subunit sheds light on the activation process of GABAB receptors. J. Biol. Chem. 275, 41166-41174 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 41166-41174
    • Galvez, T.1
  • 46
    • 18144452059 scopus 로고    scopus 로고
    • Ca(21) requirement for high-affinity gamma-aminobutyric acid (GABA) binding at GABA(B) receptors: Involvement of serine 269 of the GABA(B)R1 subunit
    • Galvez, T. et al. Ca(21) requirement for high-affinity gamma-aminobutyric acid (GABA) binding at GABA(B) receptors: involvement of serine 269 of the GABA(B)R1 subunit. Mol. Pharmacol. 57, 419-426 (2000)
    • (2000) Mol. Pharmacol. , vol.57 , pp. 419-426
    • Galvez, T.1
  • 47
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • Kniazeff, J. et al. Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Nature Struct. Mol. Biol. 11, 706-713 (2004)
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1
  • 48
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa, H., Singh, S. K., Mancusso, R. & Gouaux, E. Subunit arrangement and function in NMDA receptors. Nature 438, 185-192 (2005)
    • (2005) Nature , vol.438 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 49
    • 0032589511 scopus 로고    scopus 로고
    • Heterodimerization of a functional GABAB receptor is mediated by parallel coiled-coil alpha-helices
    • Kammerer, R. A. et al. Heterodimerization of a functional GABAB receptor is mediated by parallel coiled-coil alpha-helices. Biochemistry 38, 13263-13269 (1999)
    • (1999) Biochemistry , vol.38 , pp. 13263-13269
    • Kammerer, R.A.1
  • 50
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger, I., Fitzgerald, D. J. & Richmond, T. J. Baculovirus expression system for heterologous multiprotein complexes. Nature Biotechnol. 22, 1583-1587 (2004)
    • (2004) Nature Biotechnol. , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 52
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • 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
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997)
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 0028802657 scopus 로고
    • The (S)-enantiomer of 2-hydroxysaclofen is the active GABAB receptor antagonist in central and peripheral preparations
    • Kerr, D. I., Ong, J., Doolette, D. J., Schafer, K. & Prager, R. H. The (S)-enantiomer of 2-hydroxysaclofen is the active GABAB receptor antagonist in central and peripheral preparations. Eur. J. Pharmacol. 287, 185-189 (1995)
    • (1995) Eur. J. Pharmacol. , vol.287 , pp. 185-189
    • Kerr, D.I.1    Ong, J.2    Doolette, D.J.3    Schafer, K.4    Prager, R.H.5
  • 55
    • 0028171204 scopus 로고
    • GABAB antagonists: Resolution, absolute stereochemistry, and pharmacology of (R)-and (S)-phaclofen
    • Frydenvang, K. et al. GABAB antagonists: resolution, absolute stereochemistry, and pharmacology of (R)-and (S)-phaclofen. Chirality 6, 583-589 (1994)
    • (1994) Chirality , vol.6 , pp. 583-589
    • Frydenvang, K.1
  • 56
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007)
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 57
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • 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
  • 58
    • 0033776369 scopus 로고    scopus 로고
    • Modelling prior distributions of atoms for macromolecular refinement and completion
    • Roversi, P., Blanc, E., Vonrhein, C., Evans, G. & Bricogne, G. Modelling prior distributions of atoms for macromolecular refinement and completion. Acta Crystallogr. D 56, 1316-1323 (2000)
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1316-1323
    • Roversi, P.1    Blanc, E.2    Vonrhein, C.3    Evans, G.4    Bricogne, G.5
  • 59
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010)
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 60
    • 0347719528 scopus 로고    scopus 로고
    • Evaluation of protein fold comparison servers
    • Novotny, M., Madsen, D. & Kleywegt, G. J. Evaluation of protein fold comparison servers. Proteins 54, 260-270 (2004)
    • (2004) Proteins , vol.54 , pp. 260-270
    • Novotny, M.1    Madsen, D.2    Kleywegt, G.J.3
  • 61
    • 84884682632 scopus 로고    scopus 로고
    • Collaboration gets the most out of software
    • Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013)
    • (2013) ELife , vol.2
    • Morin, A.1
  • 62
    • 0141506109 scopus 로고    scopus 로고
    • Disulfide by Design: A computational method for the rational design of disulfide bonds in proteins
    • Dombkowski, A. A. Disulfide by Design: a computational method for the rational design of disulfide bonds in proteins. Bioinformatics 19, 1852-1853 (2003)
    • (2003) Bioinformatics , vol.19 , pp. 1852-1853
    • Dombkowski, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.