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Volumn 31, Issue 10, 2011, Pages 3565-3579

Separation of domain contacts is required for heterotetrameric assembly of functional NMDA receptors

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMPA RECEPTOR; CYSTEINE; HOMODIMER; IONOTROPIC RECEPTOR; KAINIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; THREONINE; TYROSINE;

EID: 79952399129     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.6041-10.2011     Document Type: Article
Times cited : (62)

References (57)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F-1 ATPase
    • Abrahams JP, Leslie AG (1996) Methods used in the structure determination of bovine mitochondrial F-1 ATPase. Acta Crystallogr D 52:30-42.
    • (1996) Acta Crystallogr D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 2
    • 0035885866 scopus 로고    scopus 로고
    • Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B
    • DOI 10.1006/geno.2001.6666
    • Andersson O, Stenqvist A, Attersand A, von Euler G (2001) Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics 78:178-184. (Pubitemid 34001421)
    • (2001) Genomics , vol.78 , Issue.3 , pp. 178-184
    • Andersson, O.1    Stenqvist, A.2    Attersand, A.3    Von Euler, G.4
  • 3
    • 34548500800 scopus 로고    scopus 로고
    • N-methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor
    • DOI 10.1074/jbc.M702778200
    • Atlason PT, Garside ML, Meddows E, Whiting P, McIlhinney RA (2007) N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor. J Biol Chem 282:25299-25307. (Pubitemid 47372789)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25299-25307
    • Atlason, P.T.1    Garside, M.L.2    Meddows, E.3    Whiting, P.4    McIlhinney, R.A.J.5
  • 4
    • 0034884750 scopus 로고    scopus 로고
    • Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
    • DOI 10.1016/S0896-6273(01)00333-6
    • Ayalon G, Stern-Bach Y (2001) Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron 31:103-113. (Pubitemid 32757092)
    • (2001) Neuron , vol.31 , Issue.1 , pp. 103-113
    • Ayalon, G.1    Stern-Bach, Y.2
  • 5
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745-2752.
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 6
    • 0033136273 scopus 로고    scopus 로고
    • 2+ inhibition of the NMDA receptor
    • 2+ inhibition of the NMDA receptor. Neuron 23:171-180.
    • (1999) Neuron , vol.23 , pp. 171-180
    • Choi, Y.B.1    Lipton, S.A.2
  • 7
    • 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, Siebold C, Gilbert RJ, Sutton GC, Harlos K, McIlhinney RA, Jones EY, Aricescu AR (2009) 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) J Mol Biol , vol.392 , pp. 1125-1132
    • Clayton, A.1    Siebold, C.2    Gilbert, R.J.3    Sutton, G.C.4    Harlos, K.5    McIlhinney, R.A.6    Jones, E.Y.7    Aricescu, A.R.8
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 9
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • Cull-Candy SG, Leszkiewicz DN (2004) Role of distinct NMDA receptor subtypes at central synapses. Sci STKE 2004:re16.
    • (2004) Sci STKE , vol.2004
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 10
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multi-wavelength anomalous diffraction methods
    • Chap 7 (Carter CW, Sweet RM, eds), New York: Academic
    • de La Fortelle E, Bricogne G (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multi-wavelength anomalous diffraction methods. In: Methods in enzymology, Vol 276, Chap 7 (Carter CW, Sweet RM, eds), pp 472-494. New York: Academic.
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 14
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, Ladjadj M, Leith A (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116:190-199. (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 15
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • DOI 10.1038/nature04089, PII N04089
    • Furukawa H, Singh SK, Mancusso R, Gouaux E (2005) Subunit arrangement and function in NMDA receptors. Nature 438:185-192. (Pubitemid 41599865)
    • (2005) Nature , vol.438 , Issue.7065 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 16
    • 37549045649 scopus 로고    scopus 로고
    • Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition
    • Gielen M, Le Goff A, Stroebel D, Johnson JW, Neyton J, Paoletti P (2008) Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition. Neuron 57:80-93.
    • (2008) Neuron , vol.57 , pp. 80-93
    • Gielen, M.1    Le Goff, A.2    Stroebel, D.3    Johnson, J.W.4    Neyton, J.5    Paoletti, P.6
  • 17
    • 66649086928 scopus 로고    scopus 로고
    • Mechanism of differential control of NMDA receptor activity by NR2 subunits
    • Gielen M, Siegler Retchless B, Mony L, Johnson JW, Paoletti P (2009) Mechanism of differential control of NMDA receptor activity by NR2 subunits. Nature 459:703-707.
    • (2009) Nature , vol.459 , pp. 703-707
    • Gielen, M.1    Siegler Retchless, B.2    Mony, L.3    Johnson, J.W.4    Paoletti, P.5
  • 18
    • 34447648920 scopus 로고    scopus 로고
    • Molecular determinants of AMPA receptor subunit assembly
    • DOI 10.1016/j.tins.2007.06.005, PII S016622360700152X
    • Greger IH, Ziff EB, Penn AC (2007) Molecular determinants of AMPA receptor subunit assembly. Trends Neurosci 30:407-416. (Pubitemid 47088718)
    • (2007) Trends in Neurosciences , vol.30 , Issue.8 , pp. 407-416
    • Greger, I.H.1    Ziff, E.B.2    Penn, A.C.3
  • 19
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • Ho BK, Gruswitz F (2008) HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct Biol 8:49.
    • (2008) BMC Struct Biol , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 20
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M, Maron C, Heinemann S (1994) N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13:1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 21
    • 20444408992 scopus 로고    scopus 로고
    • Mechanism of partial agonist action at the NR1 subunit of NMDA receptors
    • DOI 10.1016/j.neuron.2005.05.022, PII S0896627305004691
    • Inanobe A, Furukawa H, Gouaux E (2005) Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron 47:71-84. (Pubitemid 40922851)
    • (2005) Neuron , vol.47 , Issue.1 , pp. 71-84
    • Inanobe, A.1    Furukawa, H.2    Gouaux, E.3
  • 22
    • 33746223009 scopus 로고    scopus 로고
    • Zinc modulates bidirectional hippocampal plasticity by effects on NMDA receptors
    • Izumi Y, Auberson YP, Zorumski CF (2006) Zinc modulates bidirectional hippocampal plasticity by effects on NMDA receptors. J Neurosci 26:7181-7188.
    • (2006) J Neurosci , vol.26 , pp. 7181-7188
    • Izumi, Y.1    Auberson, Y.P.2    Zorumski, C.F.3
  • 24
    • 72449151659 scopus 로고    scopus 로고
    • Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit
    • Karakas E, Simorowski N, Furukawa H (2009) Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. EMBO J 28:3910-3920.
    • (2009) EMBO J , vol.28 , pp. 3910-3920
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 25
    • 0036830627 scopus 로고    scopus 로고
    • NMDA receptor pathways as drug targets
    • Kemp JA, McKernan RM (2002) NMDA receptor pathways as drug targets. Nat Neurosci [Suppl] 5:1039-1042.
    • (2002) Nat Neurosci , vol.5 , Issue.SUPPL. , pp. 1039-1042
    • Kemp, J.A.1    McKernan, R.M.2
  • 26
    • 78549248799 scopus 로고    scopus 로고
    • Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains
    • Kumar J, Mayer ML (2010) Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains. J Mol Biol 404:680-696.
    • (2010) J Mol Biol , vol.404 , pp. 680-696
    • Kumar, J.1    Mayer, M.L.2
  • 27
    • 67349285101 scopus 로고    scopus 로고
    • The N-terminal domain of GluR6-subtype glutamate receptor ion channels
    • Kumar J, Schuck P, Jin R, Mayer ML (2009) The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nat Struct Mol Biol 16:631-638.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 631-638
    • Kumar, J.1    Schuck, P.2    Jin, R.3    Mayer, M.L.4
  • 29
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3- hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD
    • Kuusinen A, Abele R, Madden DR, Keinänen K (1999) Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3- hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD. J Biol Chem 274:28937-28943.
    • (1999) J Biol Chem , vol.274 , pp. 28937-28943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinänen, K.4
  • 31
    • 0033546277 scopus 로고    scopus 로고
    • Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their N-terminal domains
    • Leuschner WD, Hoch W (1999) Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their N-terminal domains. J Biol Chem 274:16907-16916.
    • (1999) J Biol Chem , vol.274 , pp. 16907-16916
    • Leuschner, W.D.1    Hoch, W.2
  • 32
    • 0034718494 scopus 로고    scopus 로고
    • Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors
    • Low CM, Zheng F, Lyuboslavsky P, Traynelis SF (2000) Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors. Proc Natl Acad Sci U S A 97:11062-11067.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11062-11067
    • Low, C.M.1    Zheng, F.2    Lyuboslavsky, P.3    Traynelis, S.F.4
  • 33
    • 0032192555 scopus 로고    scopus 로고
    • Assembly intracellular targeting and cell surface expression of the human N-methyl-D-aspartate receptor subunits NR1a and NR2A in transfected cells
    • McIlhinney RA, Le Bourdellès B, Molnár E, Tricaud N, Streit P, Whiting PJ (1998) Assembly intracellular targeting and cell surface expression of the human N-methyl-D-aspartate receptor subunits NR1a and NR2A in transfected cells. Neuropharmacology 37:1355-1367.
    • (1998) Neuropharmacology , vol.37 , pp. 1355-1367
    • McIlhinney, R.A.1    Le Bourdellès, B.2    Molnár, E.3    Tricaud, N.4    Streit, P.5    Whiting, P.J.6
  • 34
    • 0035377311 scopus 로고    scopus 로고
    • Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors
    • Meddows E, Le Bourdelles B, Grimwood S, Wafford K, Sandhu S, Whiting P, McIlhinney RA (2001) Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors. J Biol Chem 276:18795-18803.
    • (2001) J Biol Chem , vol.276 , pp. 18795-18803
    • Meddows, E.1    Le Bourdelles, B.2    Grimwood, S.3    Wafford, K.4    Sandhu, S.5    Whiting, P.6    McIlhinney, R.A.7
  • 36
    • 0026419327 scopus 로고
    • Molecular cloning and characterization of the rat NMDA receptor
    • Moriyoshi K, Masu M, Ishii T, Shigemoto R, Mizuno N, Nakanishi S (1991) Molecular cloning and characterization of the rat NMDA receptor. Nature 354:31-37. (Pubitemid 21896774)
    • (1991) Nature , vol.354 , Issue.6348 , pp. 31-37
    • Moriyoshi, K.1    Masu, M.2    Ishii, T.3    Shigemoto, R.4    Mizuno, N.5    Nakanishi, S.6
  • 38
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • DOI 10.1038/nature03328
    • Nakagawa T, Cheng Y, Ramm E, Sheng M, Walz T (2005) Structure and different conformational states of native AMPA receptor complexes. Nature 433:545-549. (Pubitemid 40204314)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 39
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - Powerful tools in modern electron microscopy
    • DOI 10.1251/bpo70
    • Ohi M, Li Y, Cheng Y, Walz T (2004) Negative staining and image classification -powerful tools in modern electron microscopy. Biol Proced Online 6:23-34. (Pubitemid 38597695)
    • (2004) Biological Procedures Online , vol.6 , Issue.1 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 40
    • 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 (1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0034517709 scopus 로고    scopus 로고
    • Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit
    • DOI 10.1016/S0896-6273(00)00163-X
    • Paoletti P, Perin-Dureau F, Fayyazuddin A, Le Goff A, Callebaut I, Neyton J (2000) Molecular organization of a zinc binding N-terminal modulatory domain in a NMDA receptor subunit. Neuron 28:911-925. (Pubitemid 32038081)
    • (2000) Neuron , vol.28 , Issue.3 , pp. 911-925
    • Paoletti, P.1    Perin-Dureau, F.2    Fayyazuddin, A.3    Le, G.A.4    Callebaut, I.5    Neyton, J.6
  • 43
    • 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 (2002) Mapping the binding site of the neuroprotectant ifenprodil on NMDA receptors. J Neurosci 22:5955-5965. (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
  • 45
    • 21644449030 scopus 로고    scopus 로고
    • Subunit assembly of N-methyl-D-aspartate receptors analyzed by fluorescence resonance energy transfer
    • Qiu S, Hua YL, Yang F, Chen YZ, Luo JH (2005) Subunit assembly of N-methyl-D-aspartate receptors analyzed by fluorescence resonance energy transfer. J Biol Chem 280:24923-24930.
    • (2005) J Biol Chem , vol.280 , pp. 24923-24930
    • Qiu, S.1    Hua, Y.L.2    Yang, F.3    Chen, Y.Z.4    Luo, J.H.5
  • 46
    • 67749122463 scopus 로고    scopus 로고
    • An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-methyl-D-aspartate receptors
    • Qiu S, Zhang XM, Cao JY, Yang W, Yan YG, Shan L, Zheng J, Luo JH (2009) An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-methyl-D-aspartate receptors. J Biol Chem 284:20285-20298.
    • (2009) J Biol Chem , vol.284 , pp. 20285-20298
    • Qiu, S.1    Zhang, X.M.2    Cao, J.Y.3    Yang, W.4    Yan, Y.G.5    Shan, L.6    Zheng, J.7    Luo, J.H.8
  • 47
    • 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 (2005) The micromolar zinc-binding domain on the NMDA receptor subunit NR2B. J Neurosci 25:308-317. (Pubitemid 40105601)
    • (2005) Journal of Neuroscience , vol.25 , Issue.2 , pp. 308-317
    • Rachline, J.1    Perin-Dureau, F.2    Le, G.A.3    Neyton, J.4    Paoletti, P.5
  • 48
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci U S A 99:13419-13424.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 49
    • 0034330386 scopus 로고    scopus 로고
    • Postsynaptic organization and regulation of excitatory synapses
    • Scannevin RH, Huganir RL (2000) Postsynaptic organization and regulation of excitatory synapses. Nat Rev Neurosci 1:133-141.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 133-141
    • Scannevin, R.H.1    Huganir, R.L.2
  • 51
    • 38049134598 scopus 로고    scopus 로고
    • Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly
    • Schüler T, Mesic I, Madry C, Bartholomäus I, Laube B (2008) Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly. J Biol Chem 283:37-46.
    • (2008) J Biol Chem , vol.283 , pp. 37-46
    • Schüler, T.1    Mesic, I.2    Madry, C.3    Bartholomäus, I.4    Laube, B.5
  • 52
    • 77249102565 scopus 로고    scopus 로고
    • Contribution of the global subunit structure and stargazin on the maturation of AMPA receptors
    • Shanks NF, Maruo T, Farina AN, Ellisman MH, Nakagawa T (2010) Contribution of the global subunit structure and stargazin on the maturation of AMPA receptors. J Neurosci 30:2728-2740.
    • (2010) J Neurosci , vol.30 , pp. 2728-2740
    • Shanks, N.F.1    Maruo, T.2    Farina, A.N.3    Ellisman, M.H.4    Nakagawa, T.5
  • 53
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky AI, Rosconi MP, Gouaux E (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462:745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 54
    • 78149495223 scopus 로고    scopus 로고
    • Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain
    • Stroebel D, Carvalho S, Paoletti P (2011) Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain. Neuropharmacology 60:151-158.
    • (2011) Neuropharmacology , vol.60 , pp. 151-158
    • Stroebel, D.1    Carvalho, S.2    Paoletti, P.3
  • 55
    • 0026766877 scopus 로고
    • Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing
    • Sugihara H, Moriyoshi K, Ishii T, Masu M, Nakanishi S (1992) Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing. Biochem Biophys Res Commun 185:826-832.
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 826-832
    • Sugihara, H.1    Moriyoshi, K.2    Ishii, T.3    Masu, M.4    Nakanishi, S.5
  • 57
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein C, Blanc E, Roversi P, Bricogne G (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364:215-230. (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4


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