메뉴 건너뛰기




Volumn 8, Issue 4, 1996, Pages 484-489

Synaptic targeting of glutamate receptors

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR; NEUROTRANSMITTER RECEPTOR; POSTSYNAPTIC RECEPTOR;

EID: 0030222203     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80024-X     Document Type: Article
Times cited : (92)

References (54)
  • 2
    • 0027234701 scopus 로고
    • The TINS/TIPS Lecture. The molecular biology of glutamate receptor channels
    • 2. Seeburg PH: The TINS/TIPS Lecture. The molecular biology of glutamate receptor channels. Trends Neurosci 1993, 16:359-365.
    • (1993) Trends Neurosci , vol.16 , pp. 359-365
    • Seeburg, P.H.1
  • 3
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampes
    • 3. Bliss TVP, Collingridge GL: A synaptic model of memory: long-term potentiation in the hippocampes. Nature 1993, 361:31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.P.1    Collingridge, G.L.2
  • 4
    • 0028208421 scopus 로고
    • Long-term synaptic depression in the mammalian brain
    • 4. Linden DJ: Long-term synaptic depression in the mammalian brain. Neuron 1994, 12:457-472.
    • (1994) Neuron , vol.12 , pp. 457-472
    • Linden, D.J.1
  • 5
    • 0028799654 scopus 로고
    • Calcium: Still center stage in hypoxic-ischemic neuronal death
    • 5. Choi DW: Calcium: still center stage in hypoxic-ischemic neuronal death. Trends Neurosci 1995, 18:58-60.
    • (1995) Trends Neurosci , vol.18 , pp. 58-60
    • Choi, D.W.1
  • 6
    • 0028204874 scopus 로고
    • Excitatory transmitter neurotoxicity
    • 6. Olney JW: Excitatory transmitter neurotoxicity. Neurobiol Aging 1994, 15:259-260.
    • (1994) Neurobiol Aging , vol.15 , pp. 259-260
    • Olney, J.W.1
  • 7
    • 0027323130 scopus 로고
    • Splice variants of the N-methyl-D-aspartate receptor NR1 identify domains involved in regulation by polyamines and protein kinase C
    • 7. Durand GM, Bennet MVL, Zukin RS: Splice variants of the N-methyl-D-aspartate receptor NR1 identify domains involved in regulation by polyamines and protein kinase C. Proc Natl Acad Sci USA 1993, 90:6731-6735.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6731-6735
    • Durand, G.M.1    Bennet, M.V.L.2    Zukin, R.S.3
  • 8
    • 0029147928 scopus 로고
    • Regulated subcellular distribution of the NR1 subunit of the NMDA receptor
    • 8. Ehlers MD, Tingley WG, Huganir RL: Regulated subcellular distribution of the NR1 subunit of the NMDA receptor. Science 1995, 269:1734-1737. Here, immunofluorescent microscopy was used to examine the subcellular distribution of NR1 splice variants expressed in QT6 quail fibroblast cells. The authors found that the 37 amino acid alternatively spliced C1 exon cassette was both necessary and sufficient for the aggregation of NR1 subunits, and that phosphorylation within the C1 cassette disrupted the NR1-enriched domains. These findings suggest that atternative splicing and protein phosphorylation might regulate the neuronal distribution of NR1 subunits.
    • (1995) Science , vol.269 , pp. 1734-1737
    • Ehlers, M.D.1    Tingley, W.G.2    Huganir, R.L.3
  • 9
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • 9. Ehlers MD, Zhang S, Bernhardt JP, Huganir RL: Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 1996, 84:745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhardt, J.P.3    Huganir, R.L.4
  • 10
    • 0027487859 scopus 로고
    • The postsynaptic density
    • 10. Kennedy MB: The postsynaptic density. Curr Opin Neurobiol 1993, 3:732-737.
    • (1993) Curr Opin Neurobiol , vol.3 , pp. 732-737
    • Kennedy, M.B.1
  • 11
    • 0025935249 scopus 로고
    • Induction of long-term potentiation is associated with an increase in the number of axospinous synapses with segmented postsynaptic densities
    • 11. Geinisman Y, DeToledo-Morrell L, Morrell F: Induction of long-term potentiation is associated with an increase in the number of axospinous synapses with segmented postsynaptic densities. Brain Res 1991, 566:77-88.
    • (1991) Brain Res , vol.566 , pp. 77-88
    • Geinisman, Y.1    Detoledo-Morrell, L.2    Morrell, F.3
  • 12
    • 0028330166 scopus 로고
    • Dendritic spines: Cellular specializations imparting both stability and flexibility to synaptic function
    • 12. Harris KM, Kater SB: Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu Rev Neurosci 1994, 17:341-371.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 13
    • 0000927212 scopus 로고
    • The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-asparlate receptor subunit 2B
    • 13. Moon IS, Apperson ML, Kennedy MB: The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-asparlate receptor subunit 2B. Proc Natl Acad Sci USA 1994, 91:3954-3958.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3954-3958
    • Moon, I.S.1    Apperson, M.L.2    Kennedy, M.B.3
  • 14
    • 0026005920 scopus 로고
    • Both NMDA and non-NMDA subtypes of glutamate receptors are concentrated at synapses on cerebral cortical neurons in culture
    • 14. Jones KA, Baughman RW: Both NMDA and non-NMDA subtypes of glutamate receptors are concentrated at synapses on cerebral cortical neurons in culture. Neuron 1991, 7:593-603.
    • (1991) Neuron , vol.7 , pp. 593-603
    • Jones, K.A.1    Baughman, R.W.2
  • 15
    • 0026560573 scopus 로고
    • Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain
    • 15. Petralia, Wenthold RJ: Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain, J Comp Neurol 1992, 318:329-354.
    • (1992) J Comp Neurol , vol.318 , pp. 329-354
    • Petralia1    Wenthold, R.J.2
  • 16
    • 0027273473 scopus 로고
    • The distribution of glutamate receptors in cultured rat hippocampal neurons: Postsynaptic clustering of AMPA-selective subunits
    • 16. Craig AM, Blackstone CD, Huganir RL, Banker G: The distribution of glutamate receptors in cultured rat hippocampal neurons: postsynaptic clustering of AMPA-selective subunits. Neuron 1993, 10:1055-1068.
    • (1993) Neuron , vol.10 , pp. 1055-1068
    • Craig, A.M.1    Blackstone, C.D.2    Huganir, R.L.3    Banker, G.4
  • 17
    • 0028285956 scopus 로고
    • Distribution and synaptic localization of immunocytochemically identified NMDA receptor subunit proteins in sensory-motor and visual cortices of monkey and human
    • 17. Huntley GW, Vickers JC, Janssen W, Brose N, Heinemann SF, Morrison JH: Distribution and synaptic localization of immunocytochemically identified NMDA receptor subunit proteins in sensory-motor and visual cortices of monkey and human. J Neurosci 1994, 14:3603-3619.
    • (1994) J Neurosci , vol.14 , pp. 3603-3619
    • Huntley, G.W.1    Vickers, J.C.2    Janssen, W.3    Brose, N.4    Heinemann, S.F.5    Morrison, J.H.6
  • 19
    • 0028053828 scopus 로고
    • Histological and ultrastructural localization of the kainate receptor subunits, KA2 and GluR6/7, in the rat nervous system using selective antipeptide antibodies
    • 19. Petralia RS, Wang Y-X, Wenthold RJ: Histological and ultrastructural localization of the kainate receptor subunits, KA2 and GluR6/7, in the rat nervous system using selective antipeptide antibodies. J Comp Neurol 1994, 349:85-110.
    • (1994) J Comp Neurol , vol.349 , pp. 85-110
    • Petralia, R.S.1    Wang, Y.-X.2    Wenthold, R.J.3
  • 20
    • 0028157362 scopus 로고
    • Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective -antipeptide antibody
    • 20. Petralia RS, Yokotani N, Wenthold RJ: Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective -antipeptide antibody. J Neurosci 1994, 14:667-696.
    • (1994) J Neurosci , vol.14 , pp. 667-696
    • Petralia, R.S.1    Yokotani, N.2    Wenthold, R.J.3
  • 21
    • 0028087773 scopus 로고
    • The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1
    • 21. Petralia RS, Wang T-X, Wenthold RJ: The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1. J Neurosci 1994, 14:6102-6120.
    • (1994) J Neurosci , vol.14 , pp. 6102-6120
    • Petralia, R.S.1    Wang, T.-X.2    Wenthold, R.J.3
  • 22
    • 0028338804 scopus 로고
    • Light and electron microscopic immunocytochemical localization of AMPA-selective glutamate receptors in the rat spinal cord
    • 22. Tachibana M, Wenthold R, Morioka RJ, Petralia RS: Light and electron microscopic immunocytochemical localization of AMPA-selective glutamate receptors in the rat spinal cord. J Comp Neurol 1994, 344:431-454.
    • (1994) J Comp Neurol , vol.344 , pp. 431-454
    • Tachibana, M.1    Wenthold, R.2    Morioka, R.J.3    Petralia, R.S.4
  • 23
    • 0029093990 scopus 로고
    • Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits
    • 23. Lau LF, Huganir RL: Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits. J Biol Chem 1995, 270:20036-20041.
    • (1995) J Biol Chem , vol.270 , pp. 20036-20041
    • Lau, L.F.1    Huganir, R.L.2
  • 24
    • 0028787876 scopus 로고
    • Synaptic expression of the high-affinity kainate receptor subunit KA2 in hippocampal cultures
    • 24. Roche KW, Huganir RL: Synaptic expression of the high-affinity kainate receptor subunit KA2 in hippocampal cultures. Neuroscience 1995, 69:383-393.
    • (1995) Neuroscience , vol.69 , pp. 383-393
    • Roche, K.W.1    Huganir, R.L.2
  • 25
    • 0028574167 scopus 로고
    • Selective clustering of glutamate and gamma-aminobutyric acid receptors opposite terminals releasing the corresponding neurotransmitters
    • 25. Craig AM, Blackstone CD, Huganir RL, Banker G: Selective clustering of glutamate and gamma-aminobutyric acid receptors opposite terminals releasing the corresponding neurotransmitters. Proc Natl Acad Sci USA 1994, 91:12373-12377.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12373-12377
    • Craig, A.M.1    Blackstone, C.D.2    Huganir, R.L.3    Banker, G.4
  • 26
    • 0027937531 scopus 로고
    • Subsynaptic segregation of metabotropic and ionotropic glutamate receptors as revealed by immunogold localization
    • 26. Nusser Z, Mulvihill E, Streit P, Somogyi P: Subsynaptic segregation of metabotropic and ionotropic glutamate receptors as revealed by immunogold localization. Neuroscience 1994, 61:421-427.
    • (1994) Neuroscience , vol.61 , pp. 421-427
    • Nusser, Z.1    Mulvihill, E.2    Streit, P.3    Somogyi, P.4
  • 27
    • 0027723681 scopus 로고
    • Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons
    • 27. Kirsch J, Wolters I, Triller A, Betz H: Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons. Nature 1993, 266:745-748.
    • (1993) Nature , vol.266 , pp. 745-748
    • Kirsch, J.1    Wolters, I.2    Triller, A.3    Betz, H.4
  • 29
    • 0028998303 scopus 로고
    • The postsynaptic localization of the glycine receptor-associated protein gephryin is regulated by the cytoskeleton
    • 29. Kirsch J, Betz H: The postsynaptic localization of the glycine receptor-associated protein gephryin is regulated by the cytoskeleton. J Neurosci 1995, 15:4148-4156.
    • (1995) J Neurosci , vol.15 , pp. 4148-4156
    • Kirsch, J.1    Betz, H.2
  • 30
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • 30. Rosenmund C, Westbrook GL: Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 1993, 10:805-814.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 31
    • 0027992341 scopus 로고
    • Mechanosensitivity of NMDA receptors in cultured mouse central neurons
    • 31. Paoletti P, Ascher P: Mechanosensitivity of NMDA receptors in cultured mouse central neurons. Neuron 1994, 13:645-655.
    • (1994) Neuron , vol.13 , pp. 645-655
    • Paoletti, P.1    Ascher, P.2
  • 32
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • 32. Kornau H-C, Schenker LJ, Kennedy MB, Seeburg PH: Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 1995, 269:1737-1740. Several NMDA receptor subunits containing carboxy-terminal T/SXV (single-letter code for amino acids) motifs were shown to interact via this motif with the second PDZ domain of SAP90/PSD-95 in both yeast two-hybrid and biochemical experiments. SAP90YPSD-95 was also shown to colocalize with the NR2B subunit at dendritic spines in cultured hippocampal neurons. This study provided the first evidence of direct interaction of postsynaptic neurotransmilter receptors with SAP90/PSD-95.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.-C.1    Schenker, L.J.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 33
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • 33. Cho K-O, Hunt CA, Kennedy MB: The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 1992, 9:929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.-O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 35
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • 35. Niethammer M, Kim E, Sheng M: Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J Neurosci 1996, 16:2157-2163. Using the yeast two-hybrid system, these authors show that the NMDA receptor subunits NR2A and NR2B can interact with both the first and the second PDZ domains of SAP90/PSD-95, and with the related protein SAP97. These findings are significant in that they demonstrate that NMDA receptor subunits are capable of interacting with multiple members of the SAP90/PSD-95 family.
    • (1996) J Neurosci , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 36
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • 36. Kennedy MB: Origin of PDZ (DHR, GLGF) domains. Trends Biochem Sci 1995, 20:350.
    • (1995) Trends Biochem Sci , vol.20 , pp. 350
    • Kennedy, M.B.1
  • 37
    • 0029143156 scopus 로고
    • Tight junctions, membrane-associated guanylate kinases and cell signalling
    • 37. Kim S: Tight junctions, membrane-associated guanylate kinases and cell signalling. Curr Opin Cell Biol 1995, 7:641-649.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 641-649
    • Kim, S.1
  • 38
    • 0029978023 scopus 로고    scopus 로고
    • Clustering membrane proteins: It's all coming together with the PSD-95/5AP90 protein family
    • 38. Gomperts SN: Clustering membrane proteins: it's all coming together with the PSD-95/5AP90 protein family. Cell 1996, 84:659-662.
    • (1996) Cell , vol.84 , pp. 659-662
    • Gomperts, S.N.1
  • 39
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • 39. Woods DF, Bryant PJ: The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell 1991, 66:451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 40
    • 0027300689 scopus 로고
    • The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: CDNA cloning and immunoelectron microscopy
    • 40. Itoh M, Nagafuchi A, Yonemura S, Kitani-Yasuda T, Tsukita S, Tsukita S: The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J Cell Biol 1993, 121:491-502.
    • (1993) J Cell Biol , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, S.5    Tsukita, S.6
  • 41
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • 41. Hoskins R, Hajnal AF, Harp SA, Kim SK: The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development 1996, 122:97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 42
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • 42. Simske JS, Kaech SM, Harp SA, Kim SK: LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 1996, 85:195-204. This study utilizes the powerful genetics of C. elegans to clone and functionally characterize the product of the lin-7 gene. The authors show that LIN-7 is a PDZ domain containing protein which binds to the LET-23 receptor tyrosine kinase both in the yeast two-hybrid system and in in vitro biochemical assays. LIN-7 is shown to localize at epithelial and vulval precursor cell junctions, at the latter of which it colocalizes with LET-23. Mutations in lin-7 result in LET-23 mislocalization. These experiments provide convincing evidence of a clear role for a PDZ domain containing protein in localizing a cell surface receptor.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 43
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • 43. Ponting CP, Phillips C: DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem Sci 1995, 20:102-103.
    • (1995) Trends Biochem Sci , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 44
    • 0028882810 scopus 로고
    • + channels by direct interaction with the PSD-95/SAP90 family of membrane-associated guanylate kinases
    • + channels when coexpressed in COS7 cells. These findings provided the first demonstration of a functional effect of SAP90/PSD-95 on the distribution of a membrane protein.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 45
    • 0028906288 scopus 로고
    • SAP97, a novel member of the superfamily of brain-related guanylate kinases
    • 45. Muller BM, Kistner U, Veh RW, Cases-Langhoff C, Becker B, Gundelfinger ED, Garner CG: SAP97, a novel member of the superfamily of brain-related guanylate kinases. J Neurosci 1995, 15:2354-2366. Here, the authors identify the second neuronal member of the S AP90/PSD-95 family, SAP97. Immunocytochemical staining indicated the presence of SAP97 in the presynaptic nerve terminals of asymmetric type 1 synapses, along unmyelinated axons, and at cell junctions of non-neuronal epithelial cells.
    • (1995) J Neurosci , vol.15 , pp. 2354-2366
    • Muller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.G.7
  • 46
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha-1-syntrophin mediated by PDZ domains
    • 46 Brenman JE, Chao DS, Gee SH, Mcgee AW, Craven SE, Santillano DR, Wu ZQ, Huang F, Xia HH, Peters MF et al.: Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha-1-syntrophin mediated by PDZ domains. Cell 1996, 84:757-767. Using both yeast two-hybrid and biochemical assays, these authors provide the first demonstration of a novel PDZ-PDZ interaction between nNOS and both SAP90/PSD-95 and alpha-1-syntrophin. Also, a novel clone was isolated from a rat brain cDNA library that encodes a SAP90/PSD-95 homolog (PSD-93) which also binds nNOS. The interaction of nNOS with SAP90/PSD-95 and/or PSD-93 might localize this important second messenger, producing enzyme to postsynaptic NMDA receptors or downstream mediators of nitric oxide signaling.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    Mcgee, A.W.4    Craven, S.E.5    Santillano, D.R.6    Wu, Z.Q.7    Huang, F.8    Xia, H.H.9    Peters, M.F.10
  • 47
    • 0028091586 scopus 로고
    • The Drosophila tumor suppressor gene dlg is required for normal synaptic bouton structure
    • 47. Lahey T, Gorczyca M, Jia XX, Budnik V: The Drosophila tumor suppressor gene dlg is required for normal synaptic bouton structure. Neuron 1994, 13:823-835.
    • (1994) Neuron , vol.13 , pp. 823-835
    • Lahey, T.1    Gorczyca, M.2    Jia, X.X.3    Budnik, V.4
  • 48
    • 0028897142 scopus 로고
    • Nucleotide binding by the synaptic associated protein SAP90
    • 48. Kistner U, Garner CC, Linial M: Nucleotide binding by the synaptic associated protein SAP90. FEBS Lett 1995, 359:159-163.
    • (1995) FEBS Lett , vol.359 , pp. 159-163
    • Kistner, U.1    Garner, C.C.2    Linial, M.3
  • 49
    • 0029962955 scopus 로고    scopus 로고
    • PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses
    • 49. Hunt CA, Schenker LJ, Kennedy MB: PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses. J Neurosci 1996, 16:1380-1388.
    • (1996) J Neurosci , vol.16 , pp. 1380-1388
    • Hunt, C.A.1    Schenker, L.J.2    Kennedy, M.B.3
  • 50
    • 0027291592 scopus 로고
    • Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C
    • 50. Alloisio N, Dalla-Venezia N, Rapa A, Andrabi K, Texier D, Gilsanz F, Cartron IP, Delaunay J, Chishti AH: Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C. Blood 1993, 82:1323-1327.
    • (1993) Blood , vol.82 , pp. 1323-1327
    • Alloisio, N.1    Dalla-Venezia, N.2    Rapa, A.3    Andrabi, K.4    Texier, D.5    Gilsanz, F.6    Cartron, I.P.7    Delaunay, J.8    Chishti, A.H.9
  • 51
    • 0028096801 scopus 로고
    • Cloning and characterization of hdlg: The human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1
    • 51. Lue RA, Marfatia SM, Branton D, Chishti AH: Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. Proc Natl Acad Sci USA 1994, 91:9818-9822.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9818-9822
    • Lue, R.A.1    Marfatia, S.M.2    Branton, D.3    Chishti, A.H.4
  • 53
    • 0025829369 scopus 로고
    • ACh receptor-rich domains organized in fibroblasts by recombinant 43-kilodalton protein
    • 53. Phillips WD, Kopta C, Blount P, Garnder PD, Steinbach JH, Merlie JP: ACh receptor-rich domains organized in fibroblasts by recombinant 43-kilodalton protein. Science 1991, 251:568-570.
    • (1991) Science , vol.251 , pp. 568-570
    • Phillips, W.D.1    Kopta, C.2    Blount, P.3    Garnder, P.D.4    Steinbach, J.H.5    Merlie, J.P.6
  • 54
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • 54. Aderem A: The MARCKS brothers: a family of protein kinase C substrates. Cell 1992, 71:713-716.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.