메뉴 건너뛰기




Volumn 31, Issue 1, 2011, Pages 3-14

Heat shock cognate protein 70 regulates gephyrin clustering

Author keywords

[No Author keywords available]

Indexed keywords

GEPHYRIN; HEAT SHOCK COGNATE PROTEIN 70;

EID: 78650890791     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.2533-10.2011     Document Type: Article
Times cited : (31)

References (78)
  • 1
    • 27944470138 scopus 로고    scopus 로고
    • Heat-shock cognate 70 is required for the activation of heat-shock factor 1 in mammalian cells
    • Ahn SG, Kim SA, Yoon JH, Vacratsis P (2005) Heat-shock cognate 70 is required for the activation of heat-shock factor 1 in mammalian cells. Biochem J 392:145-152.
    • (2005) Biochem J , vol.392 , pp. 145-152
    • Ahn, S.G.1    Kim, S.A.2    Yoon, J.H.3    Vacratsis, P.4
  • 2
    • 0025062963 scopus 로고
    • Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family
    • Alvares K, Carrillo A, Yuan PM, Kawano H, Morimoto RI, Reddy JK (1990) Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family. Proc Natl Acad Sci U S A 87:5293-5297.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5293-5297
    • Alvares, K.1    Carrillo, A.2    Yuan, P.M.3    Kawano, H.4    Morimoto, R.I.5    Reddy, J.K.6
  • 3
    • 0027420758 scopus 로고
    • The 70-kDa heat shock cognate protein (HSC70) is a major constituent of the CNS and is up-regulated only at the mRNA level in acute experimental autoimmune encephalomyelitis
    • Aquino DA, Klipfel AA, Brosnan CF, Norton WT (1993) The 70-kDa heat shock cognate protein (HSC70) is a major constituent of the CNS and is up-regulated only at the mRNA level in acute experimental autoimmune encephalomyelitis. J Neurochem 61:1340-1348.
    • (1993) J Neurochem , vol.61 , pp. 1340-1348
    • Aquino, D.A.1    Klipfel, A.A.2    Brosnan, C.F.3    Norton, W.T.4
  • 4
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
    • Arndt V, Daniel C, Nastainczyk W, Alberti S, Höhfeld J (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol Biol Cell 16:5891-5900.
    • (2005) Mol Biol Cell , vol.16 , pp. 5891-5900
    • Arndt, V.1    Daniel, C.2    Nastainczyk, W.3    Alberti, S.4    Höhfeld, J.5
  • 5
    • 0033963212 scopus 로고    scopus 로고
    • Localization of the heat-shock protein Hsp70 to the synapse following hyperthermic stress in the brain
    • Bechtold DA, Rush SJ, Brown IR (2000) Localization of the heat-shock protein Hsp70 to the synapse following hyperthermic stress in the brain. J Neurochem 74:641-646.
    • (2000) J Neurochem , vol.74 , pp. 641-646
    • Bechtold, D.A.1    Rush, S.J.2    Brown, I.R.3
  • 7
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 8
    • 0036733668 scopus 로고    scopus 로고
    • HSP70 constitutive expression in rat central nervous system from postnatal development to maturity
    • Bodega G, Hernández C, Suárez I, Martín M, Fernández B (2002) HSP70 constitutive expression in rat central nervous system from postnatal development to maturity. J Histochem Cytochem 50:1161-1168.
    • (2002) J Histochem Cytochem , vol.50 , pp. 1161-1168
    • Bodega, G.1    Hernández, C.2    Suárez, I.3    Martín, M.4    Fernández, B.5
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 12
    • 33751421771 scopus 로고    scopus 로고
    • Protein profiling of rat ventral prostate following chronic finasteride administration: Identification and localization of a novel putative androgen-regulated protein
    • Cayatte C, Pons C, Guigonis JM, Pizzol J, Elies L, Kennel P, Rouquié D, Bars R, Rossi B, Samson M (2006) Protein profiling of rat ventral prostate following chronic finasteride administration: identification and localization of a novel putative androgen-regulated protein. Mol Cell Proteomics 5:2031-2043.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2031-2043
    • Cayatte, C.1    Pons, C.2    Guigonis, J.M.3    Pizzol, J.4    Elies, L.5    Kennel, P.6    Rouquié, D.7    Bars, R.8    Rossi, B.9    Samson, M.10
  • 14
    • 33748185659 scopus 로고    scopus 로고
    • Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane
    • Charrier C, Ehrensperger MV, Dahan M, Lévi S, Triller A (2006) Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane. J Neurosci 26:8502-8511.
    • (2006) J Neurosci , vol.26 , pp. 8502-8511
    • Charrier, C.1    Ehrensperger, M.V.2    Dahan, M.3    Lévi, S.4    Triller, A.5
  • 16
    • 0037088917 scopus 로고    scopus 로고
    • Endosomal compartments serve multiple hippocampal dendritic spines from a widespread rather than a local store of recycling membrane
    • Cooney JR, Hurlburt JL, Selig DK, Harris KM, Fiala JC (2002) Endosomal compartments serve multiple hippocampal dendritic spines from a widespread rather than a local store of recycling membrane. J Neurosci 22:2215-2224.
    • (2002) J Neurosci , vol.22 , pp. 2215-2224
    • Cooney, J.R.1    Hurlburt, J.L.2    Selig, D.K.3    Harris, K.M.4    Fiala, J.C.5
  • 17
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M, Lévi S, Luccardini C, Rostaing P, Riveau B, Triller A (2003) Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302:442-445.
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Lévi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 18
    • 0032924485 scopus 로고    scopus 로고
    • Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons
    • Dumoulin A, Rostaing P, Bedet C, Lévi S, Isambert MF, Henry JP, Triller A, Gasnier B (1999) Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons. J Cell Sci 112:811-823.
    • (1999) J Cell Sci , vol.112 , pp. 811-823
    • Dumoulin, A.1    Rostaing, P.2    Bedet, C.3    Lévi, S.4    Isambert, M.F.5    Henry, J.P.6    Triller, A.7    Gasnier, B.8
  • 19
    • 0033769370 scopus 로고    scopus 로고
    • Formation of mixed glycine and GABAergic synapses in cultured spinal cord neurons
    • Dumoulin A, Lévi S, Riveau B, Gasnier B, Triller A (2000) Formation of mixed glycine and GABAergic synapses in cultured spinal cord neurons. Eur J Neurosci 12:3883-3892.
    • (2000) Eur J Neurosci , vol.12 , pp. 3883-3892
    • Dumoulin, A.1    Lévi, S.2    Riveau, B.3    Gasnier, B.4    Triller, A.5
  • 20
    • 34247857560 scopus 로고    scopus 로고
    • Multiple association states between glycine receptors and gephyrin identified by SPT analysis
    • Ehrensperger MV, Hanus C, Vannier C, Triller A, Dahan M (2007) Multiple association states between glycine receptors and gephyrin identified by SPT analysis. Biophys J 92:3706-3718.
    • (2007) Biophys J , vol.92 , pp. 3706-3718
    • Ehrensperger, M.V.1    Hanus, C.2    Vannier, C.3    Triller, A.4    Dahan, M.5
  • 21
    • 4344616571 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by Hsp70 chaperones
    • Erbse A, Mayer MP, Bukau B (2004) Mechanism of substrate recognition by Hsp70 chaperones. Biochem Soc Trans 32:617-621.
    • (2004) Biochem Soc Trans , vol.32 , pp. 617-621
    • Erbse, A.1    Mayer, M.P.2    Bukau, B.3
  • 24
    • 0032963006 scopus 로고    scopus 로고
    • Dendritic and postsynaptic protein synthetic machinery
    • Gardiol A, Racca C, Triller A (1999) Dendritic and postsynaptic protein synthetic machinery. J Neurosci 19:168-179.
    • (1999) J Neurosci , vol.19 , pp. 168-179
    • Gardiol, A.1    Racca, C.2    Triller, A.3
  • 25
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 27
    • 0842347344 scopus 로고    scopus 로고
    • Intracellular association of glycine receptor with gephyrin increases its plasma membrane accumulation rate
    • Hanus C, Vannier C, Triller A (2004) Intracellular association of glycine receptor with gephyrin increases its plasma membrane accumulation rate. J Neurosci 24:1119-1128.
    • (2004) J Neurosci , vol.24 , pp. 1119-1128
    • Hanus, C.1    Vannier, C.2    Triller, A.3
  • 28
    • 33646850883 scopus 로고    scopus 로고
    • Activity-dependent movements of postsynaptic scaffolds at inhibitory synapses
    • Hanus C, Ehrensperger MV, Triller A (2006) Activity-dependent movements of postsynaptic scaffolds at inhibitory synapses. J Neurosci 26:4586-4595.
    • (2006) J Neurosci , vol.26 , pp. 4586-4595
    • Hanus, C.1    Ehrensperger, M.V.2    Triller, A.3
  • 29
    • 0024433249 scopus 로고
    • Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia: A candidate intermediate in the vesicle uncoating reaction
    • Heuser J, Steer CJ (1989) Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia: a candidate intermediate in the vesicle uncoating reaction. J Cell Biol 109:1457-1466.
    • (1989) J Cell Biol , vol.109 , pp. 1457-1466
    • Heuser, J.1    Steer, C.J.2
  • 30
    • 0028309738 scopus 로고
    • Association of peroxisome proliferator-activated receptor and Hsp72
    • Huang Q, Alvares K, Chu R, Bradfield CA, Reddy JK (1994) Association of peroxisome proliferator-activated receptor and Hsp72. J Biol Chem 269:8493-8497.
    • (1994) J Biol Chem , vol.269 , pp. 8493-8497
    • Huang, Q.1    Alvares, K.2    Chu, R.3    Bradfield, C.A.4    Reddy, J.K.5
  • 32
    • 0032970689 scopus 로고    scopus 로고
    • Incorporation of a gephyrin-binding motif targets NMDA receptors to gephyrin-rich domains in HEK 293 cells
    • Kins S, Kuhse J, Laube B, Betz H, Kirsch J (1999) Incorporation of a gephyrin-binding motif targets NMDA receptors to gephyrin-rich domains in HEK 293 cells. Eur J Neurosci 11:740-744.
    • (1999) Eur J Neurosci , vol.11 , pp. 740-744
    • Kins, S.1    Kuhse, J.2    Laube, B.3    Betz, H.4    Kirsch, J.5
  • 33
    • 0033994755 scopus 로고    scopus 로고
    • Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin
    • Kins S, Betz H, Kirsch J (2000) Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin. Nat Neurosci 3:22-29.
    • (2000) Nat Neurosci , vol.3 , pp. 22-29
    • Kins, S.1    Betz, H.2    Kirsch, J.3
  • 35
    • 0034919997 scopus 로고    scopus 로고
    • The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors
    • Kittler JT, Rostaing P, Schiavo G, Fritschy JM, Olsen R, Triller A, Moss SJ (2001) The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors. Mol Cell Neurosci 18:13-25.
    • (2001) Mol Cell Neurosci , vol.18 , pp. 13-25
    • Kittler, J.T.1    Rostaing, P.2    Schiavo, G.3    Fritschy, J.M.4    Olsen, R.5    Triller, A.6    Moss, S.J.7
  • 37
    • 0035965126 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9
    • Lavoie SB, Albert AL, Handa H, Vincent M, Bensaude O (2001) The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9. J Mol Biol 312:675-685.
    • (2001) J Mol Biol , vol.312 , pp. 675-685
    • Lavoie, S.B.1    Albert, A.L.2    Handa, H.3    Vincent, M.4    Bensaude, O.5
  • 38
    • 47749151041 scopus 로고    scopus 로고
    • Homeostatic regulation of synaptic GlyR numbers driven by lateral diffusion
    • Lévi S, Schweizer C, Bannai H, Pascual O, Charrier C, Triller A (2008) Homeostatic regulation of synaptic GlyR numbers driven by lateral diffusion. Neuron 59:261-273.
    • (2008) Neuron , vol.59 , pp. 261-273
    • Lévi, S.1    Schweizer, C.2    Bannai, H.3    Pascual, O.4    Charrier, C.5    Triller, A.6
  • 40
    • 0034695475 scopus 로고    scopus 로고
    • Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli
    • Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H (2000) Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli. J Biol Chem 275:1814-1822.
    • (2000) J Biol Chem , vol.275 , pp. 1814-1822
    • Liu, M.T.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 44
    • 0030601990 scopus 로고    scopus 로고
    • The neuronal stress response: Nuclear translocation of heat shock proteins as an indicator of hyperthermic stress
    • Manzerra P, Brown IR (1996) The neuronal stress response: nuclear translocation of heat shock proteins as an indicator of hyperthermic stress. Exp Cell Res 229:35-47.
    • (1996) Exp Cell Res , vol.229 , pp. 35-47
    • Manzerra, P.1    Brown, I.R.2
  • 45
    • 0027490256 scopus 로고
    • Temporal and spatial distribution of heat shock mRNA and protein (hsp70) in the rabbit cerebellum in response to hyperthermia
    • Manzerra P, Rush SJ, Brown IR (1993) Temporal and spatial distribution of heat shock mRNA and protein (hsp70) in the rabbit cerebellum in response to hyperthermia. J Neurosci Res 36:480-490.
    • (1993) J Neurosci Res , vol.36 , pp. 480-490
    • Manzerra, P.1    Rush, S.J.2    Brown, I.R.3
  • 46
    • 0031039134 scopus 로고    scopus 로고
    • Tissue-specific differences in heat shock protein hsc70 and hsp70 in the control and hyperthermic rabbit
    • Manzerra P, Rush SJ, Brown IR (1997) Tissue-specific differences in heat shock protein hsc70 and hsp70 in the control and hyperthermic rabbit. J Cell Physiol 170:130-137.
    • (1997) J Cell Physiol , vol.170 , pp. 130-137
    • Manzerra, P.1    Rush, S.J.2    Brown, I.R.3
  • 48
    • 0033845824 scopus 로고    scopus 로고
    • Formation of glycine receptor clusters and their accumulation at synapses
    • Meier J, Meunier-Durmort C, Forest C, Triller A, Vannier C (2000b) Formation of glycine receptor clusters and their accumulation at synapses. J Cell Sci 113:2783-2795.
    • (2000) J Cell Sci , vol.113 , pp. 2783-2795
    • Meier, J.1    Meunier-Durmort, C.2    Forest, C.3    Triller, A.4    Vannier, C.5
  • 49
    • 0035112736 scopus 로고    scopus 로고
    • Fast and reversible trapping of surface glycine receptors by gephyrin
    • Meier J, Vannier C, Sergé A, Triller A, Choquet D (2001) Fast and reversible trapping of surface glycine receptors by gephyrin. Nat Neurosci 4:253-260.
    • (2001) Nat Neurosci , vol.4 , pp. 253-260
    • Meier, J.1    Vannier, C.2    Sergé, A.3    Triller, A.4    Choquet, D.5
  • 50
    • 58849143814 scopus 로고    scopus 로고
    • From hatching to dispatching: The multiple cellular roles of the Hsp70 molecular chaperone machinery
    • Meimaridou E, Gooljar SB, Chapple JP (2009) From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery. J Mol Endocrinol 42:1-9.
    • (2009) J Mol Endocrinol , vol.42 , pp. 1-9
    • Meimaridou, E.1    Gooljar, S.B.2    Chapple, J.P.3
  • 51
    • 0029124881 scopus 로고
    • Identification of a gephyrin binding motif on the glycine receptor beta subunit
    • Meyer G, Kirsch J, Betz H, Langosch D (1995) Identification of a gephyrin binding motif on the glycine receptor beta subunit. Neuron 15:563-572.
    • (1995) Neuron , vol.15 , pp. 563-572
    • Meyer, G.1    Kirsch, J.2    Betz, H.3    Langosch, D.4
  • 52
    • 0035098083 scopus 로고    scopus 로고
    • Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses
    • Moon IS, Park IS, Schenker LT, Kennedy MB, Moon JI, Jin I (2001) Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses. Cereb Cortex 11:238-248.
    • (2001) Cereb Cortex , vol.11 , pp. 238-248
    • Moon, I.S.1    Park, I.S.2    Schenker, L.T.3    Kennedy, M.B.4    Moon, J.I.5    Jin, I.6
  • 53
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A (2002) A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 20:87-90.
    • (2002) Nat Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 54
    • 33845975648 scopus 로고    scopus 로고
    • Mass spectrometric analysis of glycine receptor-associated gephyrin splice variants
    • Paarmann I, Schmitt B, Meyer B, Karas M, Betz H (2006) Mass spectrometric analysis of glycine receptor-associated gephyrin splice variants. J Biol Chem 281:34918-34925.
    • (2006) J Biol Chem , vol.281 , pp. 34918-34925
    • Paarmann, I.1    Schmitt, B.2    Meyer, B.3    Karas, M.4    Betz, H.5
  • 55
    • 0030480767 scopus 로고    scopus 로고
    • The morphology of synapses
    • Peters A, Palay SL (1996) The morphology of synapses. J Neurocytol 25:687-700.
    • (1996) J Neurocytol , vol.25 , pp. 687-700
    • Peters, A.1    Palay, S.L.2
  • 57
    • 33947279578 scopus 로고    scopus 로고
    • Visualization and quantification of vesicle trafficking on a three-dimensional cytoskeleton network in living cells
    • Racine V, Sachse M, Salamero J, Fraisier V, Trubuil A, Sibarita JB (2007) Visualization and quantification of vesicle trafficking on a three-dimensional cytoskeleton network in living cells. J Microsc 225:214-228.
    • (2007) J Microsc , vol.225 , pp. 214-228
    • Racine, V.1    Sachse, M.2    Salamero, J.3    Fraisier, V.4    Trubuil, A.5    Sibarita, J.B.6
  • 58
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • Rassow J, Voos W, Pfanner N (1995) Partner proteins determine multiple functions of Hsp70. Trends Cell Biol 5:207-212.
    • (1995) Trends Cell Biol , vol.5 , pp. 207-212
    • Rassow, J.1    Voos, W.2    Pfanner, N.3
  • 60
    • 0035879179 scopus 로고    scopus 로고
    • Dynamics of glycine receptor insertion in the neuronal plasma membrane
    • Rosenberg M, Meier J, Triller A, Vannier C (2001) Dynamics of glycine receptor insertion in the neuronal plasma membrane. J Neurosci 21:5036-5044.
    • (2001) J Neurosci , vol.21 , pp. 5036-5044
    • Rosenberg, M.1    Meier, J.2    Triller, A.3    Vannier, C.4
  • 64
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 65
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman DM, Schmid SL, Braell WA, Rothman JE (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 99:723-733.
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 66
    • 2442629473 scopus 로고    scopus 로고
    • Biochemical characterization of the high affinity binding between the glycine receptor and gephyrin
    • Schrader N, Kim EY, Winking J, Paulukat J, Schindelin H, Schwarz G (2004) Biochemical characterization of the high affinity binding between the glycine receptor and gephyrin. J Biol Chem 279:18733-18741.
    • (2004) J Biol Chem , vol.279 , pp. 18733-18741
    • Schrader, N.1    Kim, E.Y.2    Winking, J.3    Paulukat, J.4    Schindelin, H.5    Schwarz, G.6
  • 67
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: A more quantitative view
    • Sheng M, Hoogenraad CC (2007) The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu Rev Biochem 76:823-847.
    • (2007) Annu Rev Biochem , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 69
    • 0031023590 scopus 로고    scopus 로고
    • Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat
    • Spacek J, Harris KM (1997) Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat. J Neurosci 17:190-203.
    • (1997) J Neurosci , vol.17 , pp. 190-203
    • Spacek, J.1    Harris, K.M.2
  • 70
    • 58149158079 scopus 로고    scopus 로고
    • The dynamics of synaptic scaffolds
    • Specht CG, Triller A (2008) The dynamics of synaptic scaffolds. Bioessays 30:1062-1074.
    • (2008) Bioessays , vol.30 , pp. 1062-1074
    • Specht, C.G.1    Triller, A.2
  • 71
    • 0033573767 scopus 로고    scopus 로고
    • Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain
    • Suzuki T, Usuda N, Murata S, Nakazawa A, Ohtsuka K, Takagi H (1999) Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain. Brain Res 816:99-110.
    • (1999) Brain Res , vol.816 , pp. 99-110
    • Suzuki, T.1    Usuda, N.2    Murata, S.3    Nakazawa, A.4    Ohtsuka, K.5    Takagi, H.6
  • 73
    • 48749085218 scopus 로고    scopus 로고
    • New concepts in synaptic biology derived from single-molecule imaging
    • Triller A, Choquet D (2008) New concepts in synaptic biology derived from single-molecule imaging. Neuron 59:359-374.
    • (2008) Neuron , vol.59 , pp. 359-374
    • Triller, A.1    Choquet, D.2
  • 74
    • 0032766645 scopus 로고    scopus 로고
    • Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2
    • Uma S, Thulasiraman V, Matts RL (1999) Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol 19:5861-5871.
    • (1999) Mol Cell Biol , vol.19 , pp. 5861-5871
    • Uma, S.1    Thulasiraman, V.2    Matts, R.L.3
  • 75
    • 0030821830 scopus 로고    scopus 로고
    • Biology of the postsynaptic glycine receptor
    • Vannier C, Triller A (1997) Biology of the postsynaptic glycine receptor. Int Rev Cytol 176:201-244.
    • (1997) Int Rev Cytol , vol.176 , pp. 201-244
    • Vannier, C.1    Triller, A.2
  • 77
    • 0034880831 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin
    • Xiang S, Nichols J, Rajagopalan KV, Schindelin H (2001) The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure 9:299-310.
    • (2001) Structure , vol.9 , pp. 299-310
    • Xiang, S.1    Nichols, J.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 78
    • 34247204919 scopus 로고    scopus 로고
    • Postphosphorylation prolyl isomerization of gephyrin represents a mechanism to modulate glycine receptors function
    • Zita MM, Marchionni I, Bottos E, Righi M, Del Sal G, Cherubini E, Zacchi P (2007) Postphosphorylation prolyl isomerization of gephyrin represents a mechanism to modulate glycine receptors function. EMBO J 26:1761-1771.
    • (2007) EMBO J , vol.26 , pp. 1761-1771
    • Zita, M.M.1    Marchionni, I.2    Bottos, E.3    Righi, M.4    Del Sal, G.5    Cherubini, E.6    Zacchi, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.