메뉴 건너뛰기




Volumn 354, Issue 1, 2007, Pages 102-108

Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function

Author keywords

Agonist binding; Glutamate receptor; Glycine binding site; Ligand gated ion channel; NMDA receptor

Indexed keywords

CATION CHANNEL; GLUTAMIC ACID; GLYCINE; GLYCINE RECEPTOR; MUTANT PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; PROTEIN NR3; UNCLASSIFIED DRUG;

EID: 33846313907     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.153     Document Type: Article
Times cited : (60)

References (17)
  • 1
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • re16
    • Cull-Candy S.G., and Leszkiewicz D.N. Role of distinct NMDA receptor subtypes at central synapses. Sci. STKE 19 (2004) 255 re16
    • (2004) Sci. STKE , vol.19 , pp. 255
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 2
    • 0023091647 scopus 로고
    • Glycine potentiates the NMDA response in cultured mouse brain neurons
    • Johnson J.W., and Ascher P. Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature 325 (1987) 529-531
    • (1987) Nature , vol.325 , pp. 529-531
    • Johnson, J.W.1    Ascher, P.2
  • 3
    • 0028284469 scopus 로고
    • Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins
    • Kuryatov A., Laube B., Betz H., and Kuhse J. Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. Neuron 12 (1994) 1291-1300
    • (1994) Neuron , vol.12 , pp. 1291-1300
    • Kuryatov, A.1    Laube, B.2    Betz, H.3    Kuhse, J.4
  • 4
    • 0030991790 scopus 로고    scopus 로고
    • Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit
    • Laube B., Hirai H., Sturgess M., Betz H., and Kuhse J. Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit. Neuron 18 (1997) 450-493
    • (1997) Neuron , vol.18 , pp. 450-493
    • Laube, B.1    Hirai, H.2    Sturgess, M.3    Betz, H.4    Kuhse, J.5
  • 5
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa H., and Gouaux E. Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22 (2003) 2873-2885
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 8
    • 0035650937 scopus 로고    scopus 로고
    • Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate receptor subunit that works in a dominant-negative manner
    • Nishi M., Hinds H., Lu H.P., Kawata M., and Hayashi Y. Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate receptor subunit that works in a dominant-negative manner. J. Neurosci. 21 (2001) RC185
    • (2001) J. Neurosci. , vol.21
    • Nishi, M.1    Hinds, H.2    Lu, H.P.3    Kawata, M.4    Hayashi, Y.5
  • 9
    • 0037074985 scopus 로고    scopus 로고
    • Excitatory glycine receptors containing the NR3 familiy of NMDA receptor subunits
    • Chatterton J.E., et al. Excitatory glycine receptors containing the NR3 familiy of NMDA receptor subunits. Nature 415 (2002) 793-797
    • (2002) Nature , vol.415 , pp. 793-797
    • Chatterton, J.E.1
  • 10
    • 33646849232 scopus 로고    scopus 로고
    • Characterization of a soluble ligand binding domain of the NMDA receptor regulatory subunit NR3A
    • Yao Y., and Mayer M.L. Characterization of a soluble ligand binding domain of the NMDA receptor regulatory subunit NR3A. J. Neurosci. 26 (2006) 4559-4566
    • (2006) J. Neurosci. , vol.26 , pp. 4559-4566
    • Yao, Y.1    Mayer, M.L.2
  • 11
    • 0037931744 scopus 로고    scopus 로고
    • A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor alpha1 subunit
    • Sadtler S., Laube B., Lashub A., Nicke A., Betz H., and Schmalzing G. A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor alpha1 subunit. J. Biol. Chem. 278 (2003) 16782-16790
    • (2003) J. Biol. Chem. , vol.278 , pp. 16782-16790
    • Sadtler, S.1    Laube, B.2    Lashub, A.3    Nicke, A.4    Betz, H.5    Schmalzing, G.6
  • 12
    • 0032493660 scopus 로고    scopus 로고
    • Expression and initial characterization of a soluble glycine binding domain of the N-methyl-d-aspartate receptor NR1 subunit
    • Ivanovic A., Reilander H., Laube B., and Kuhse J. Expression and initial characterization of a soluble glycine binding domain of the N-methyl-d-aspartate receptor NR1 subunit. J. Biol. Chem. 273 (1998) 19933-19937
    • (1998) J. Biol. Chem. , vol.273 , pp. 19933-19937
    • Ivanovic, A.1    Reilander, H.2    Laube, B.3    Kuhse, J.4
  • 13
    • 0029893942 scopus 로고    scopus 로고
    • The glycine binding site of the N-methyl-d-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region
    • Hirai H., Kirsch J., Laube B., Betz H., and Kuhse J. The glycine binding site of the N-methyl-d-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Proc. Natl. Acad. Sci. USA 93 (1996) 6031-6036
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6031-6036
    • Hirai, H.1    Kirsch, J.2    Laube, B.3    Betz, H.4    Kuhse, J.5
  • 14
    • 33645321641 scopus 로고    scopus 로고
    • Glutamate receptors at atomic resolution
    • Mayer M.L. Glutamate receptors at atomic resolution. Nature 440 (2006) 456-462
    • (2006) Nature , vol.440 , pp. 456-462
    • Mayer, M.L.1
  • 15
    • 33749059766 scopus 로고    scopus 로고
    • Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor
    • Armstrong N., Jasti J., Beich-Frandsen M., and Gouaux E. Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127 (2006) 85-97
    • (2006) Cell , vol.127 , pp. 85-97
    • Armstrong, N.1    Jasti, J.2    Beich-Frandsen, M.3    Gouaux, E.4
  • 16
    • 0032575065 scopus 로고    scopus 로고
    • Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A
    • Das S., et al. Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A. Nature 393 (1998) 377-381
    • (1998) Nature , vol.393 , pp. 377-381
    • Das, S.1
  • 17
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa H., Singh S.K., Mancusso R., and Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 438 (2005) 185-192
    • (2005) Nature , vol.438 , 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.