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Volumn 475, Issue 7355, 2011, Pages 249-253

Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR 1; GLUTAMATE RECEPTOR 2; HETERODIMER; HOMODIMER; IFENPRODIL; ION CHANNEL; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHENYLETHANOLAMINE; PROTEIN SUBUNIT;

EID: 79960417429     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10180     Document Type: Article
Times cited : (287)

References (29)
  • 2
    • 78649301895 scopus 로고    scopus 로고
    • NovelN-methyl-D-aspartate receptor antagonists: A review of compounds patented since 2006
    • Koller, M. & Urwyler, S. NovelN-methyl-D-aspartate receptor antagonists: a review of compounds patented since 2006. Expert Opin. Ther. Pat. 20, 1683-1702 (2010).
    • (2010) Expert Opin. Ther. Pat. , vol.20 , pp. 1683-1702
    • Koller, M.1    Urwyler, S.2
  • 3
    • 77957235696 scopus 로고    scopus 로고
    • Control of assembly and function of glutamate receptors by the amino-terminal domain
    • Hansen, K. B., Furukawa, H. & Traynelis, S. F. Control of assembly and function of glutamate receptors by the amino-terminal domain. Mol. Pharmacol. 78, 535-549 (2010).
    • (2010) Mol. Pharmacol. , vol.78 , pp. 535-549
    • Hansen, K.B.1    Furukawa, H.2    Traynelis, S.F.3
  • 4
    • 70350324907 scopus 로고    scopus 로고
    • Allosteric modulators of NR2BcontainingNMDAreceptors: Molecularmechanismsandtherapeutic potential
    • Mony, L., Kew, J. N., Gunthorpe, M. J. & Paoletti, P. Allosteric modulators of NR2BcontainingNMDAreceptors: molecularmechanismsandtherapeutic potential. Br. J. Pharmacol. 157, 1301-1317 (2009).
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 1301-1317
    • Mony, L.1    Kew, J.N.2    Gunthorpe, M.J.3    Paoletti, P.4
  • 5
    • 77952363301 scopus 로고    scopus 로고
    • Glutamate receptor ion channels: Structure, regulation, and function
    • Traynelis, S. F. et al. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 62, 405-496 (2010).
    • (2010) Pharmacol. Rev. , vol.62 , pp. 405-496
    • Traynelis, S.F.1
  • 6
    • 0029871365 scopus 로고    scopus 로고
    • Interactions between ifenprodil and the NR2B subunit of the N-methyl-D-aspartate receptor
    • Gallagher, M. J., Huang, H., Pritchett, D. B. & Lynch, D. R. Interactions between ifenprodil and the NR2B subunit of the N-methyl-D-aspartate receptor. J. Biol. Chem. 271, 9603-9611 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9603-9611
    • Gallagher, M.J.1    Huang, H.2    Pritchett, D.B.3    Lynch, D.R.4
  • 7
    • 0027525324 scopus 로고
    • Ifenprodil discriminates subtypes of the N-methyl-D-aspartate receptor: Selectivity and mechanisms at recombinant heteromeric receptors
    • Williams, K. Ifenprodil discriminates subtypes of the N-methyl-D-aspartate receptor: selectivity and mechanisms at recombinant heteromeric receptors. Mol. Pharmacol. 44, 851-859 (1993). (Pubitemid 23317299)
    • (1993) Molecular Pharmacology , vol.44 , Issue.4 , pp. 851-859
    • Williams, K.1
  • 8
    • 78650818672 scopus 로고    scopus 로고
    • Cloning and phylogenetic analysis of NMDA receptor subunits NR1 NR2A and NR2B in Xenopus laevis tadpoles
    • Ewald, R. C. & Cline, H. T. Cloning and phylogenetic analysis of NMDA receptor subunits NR1, NR2A and NR2B in Xenopus laevis tadpoles. Front. Mol. Neurosci. 2, 4 (2009).
    • (2009) Front. Mol. Neurosci. , vol.2 , pp. 4
    • Ewald, R.C.1    Cline, H.T.2
  • 9
    • 68349109621 scopus 로고    scopus 로고
    • Molecular and functional characterization of Xenopus laevis N-methyl-D-aspartate receptors
    • Schmidt, C. & Hollmann, M. Molecular and functional characterization of Xenopus laevis N-methyl-D-aspartate receptors. Mol. Cell. Neurosci. 42, 116-127 (2009).
    • (2009) Mol. Cell. Neurosci. , vol.42 , pp. 116-127
    • Schmidt, C.1    Hollmann, M.2
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 70149087712 scopus 로고    scopus 로고
    • Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors
    • Clayton, A. et al. Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. J. Mol. Biol. 392, 1125-1132 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 1125-1132
    • Clayton, A.1
  • 14
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky, A. I., Rosconi, M. P. & Gouaux, E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756 (2009).
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 15
    • 66649086928 scopus 로고    scopus 로고
    • Mechanismof differential control of NMDA receptor activity by NR2 subunits
    • Gielen, M., Siegler Retchless, B., Mony, L., Johnson, J. W.&Paoletti, P.Mechanismof differential control of NMDA receptor activity by NR2 subunits. Nature 459, 703-707 (2009).
    • (2009) Nature , vol.459 , pp. 703-707
    • Gielen, M.1    Siegler Retchless, B.2    Mony, L.3    Johnson, J.W.4    Paoletti, P.5
  • 16
    • 12144257176 scopus 로고    scopus 로고
    • The micromolar zinc-binding domain on the NMDA receptor subunit NR2B
    • DOI 10.1523/JNEUROSCI.3967-04.2005
    • Rachline, J., Perin-Dureau, F., Le Goff, A., Neyton, J. & Paoletti, P. The micromolar zinc-binding domain on the NMDA receptor subunit NR2B. J. Neurosci. 25, 308-317 (2005). (Pubitemid 40105601)
    • (2005) Journal of Neuroscience , vol.25 , Issue.2 , pp. 308-317
    • Rachline, J.1    Perin-Dureau, F.2    Le Goff, A.3    Neyton, J.4    Paoletti, P.5
  • 18
    • 0033051714 scopus 로고    scopus 로고
    • A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D- aspartate receptor: Effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein
    • Masuko, T. et al. A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol. Pharmacol. 55, 957-969 (1999). (Pubitemid 29252360)
    • (1999) Molecular Pharmacology , vol.55 , Issue.6 , pp. 957-969
    • Masuko, T.1    Kashiwagi, K.2    Kuno, T.3    Nguyen, N.D.4    Pahk, A.J.5    Fukuchi, J.-I.6    Igarashi, K.7    Williams, K.8
  • 19
    • 0037101607 scopus 로고    scopus 로고
    • Mapping the binding site of the neuroprotectant ifenprodil on NMDA receptors
    • Perin-Dureau, F., Rachline, J., Neyton, J. & Paoletti, P. Mapping the binding site of the neuroprotectant ifenprodil on NMDA receptors. J. Neurosci. 22, 5955-5965 (2002). (Pubitemid 35387640)
    • (2002) Journal of Neuroscience , vol.22 , Issue.14 , pp. 5955-5965
    • Perin-Dureau, F.1    Rachline, J.2    Neyton, J.3    Paoletti, P.4
  • 20
    • 79955525364 scopus 로고    scopus 로고
    • Amino terminal domains of the NMDA receptor are organized as local heterodimers
    • Lee, C. H. & Gouaux, E. Amino terminal domains of the NMDA receptor are organized as local heterodimers. PLoS ONE 6, e19181 (2011).
    • (2011) PLoS ONE , vol.6
    • Lee, C.H.1    Gouaux, E.2
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997). (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • DOI 10.1016/S0076-6879(97)76073-7
    • de La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997). (Pubitemid 27085618)
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • 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    Coot, C.K.2
  • 28
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. Size-distribution analysis ofmacromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619 (2000). (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 29
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • DOI 10.1038/nature04089, PII N04089
    • Furukawa, H., Singh, S. K., Mancusso, R. & Gouaux, E. Subunit arrangement and function in NMDA receptors. Nature 438, 185-192 (2005). (Pubitemid 41599865)
    • (2005) Nature , vol.438 , Issue.7065 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.