메뉴 건너뛰기




Volumn 113, Issue 22, 2016, Pages E3081-E3090

A binding site outside the canonical PDZ domain determines the specific interaction between Shank and SAPAP and their function

Author keywords

PDZ; SAPAP; Shank; Specific interaction; Synapse

Indexed keywords

NEUROLIGIN 1; SCAFFOLD PROTEIN; SHANK PROTEIN; SYNAPSE ASSOCIATED PROTEIN 90 POSTSYNAPTIC DENSITY 95 ASSOCIATED PROTEIN; UNCLASSIFIED DRUG; NERVE PROTEIN; PROTEIN BINDING; SAPAP PROTEINS; SHANK1 PROTEIN, MOUSE;

EID: 84973137968     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1523265113     Document Type: Article
Times cited : (37)

References (72)
  • 1
    • 0017408222 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex, II: Characterization and arrangement of some of the major proteins within the structure
    • Blomberg F, Cohen RS, Siekevitz P (1977) The structure of postsynaptic densities isolated from dog cerebral cortex, II: Characterization and arrangement of some of the major proteins within the structure. J Cell Biol 74(1):204-225.
    • (1977) J Cell Biol , vol.74 , Issue.1 , pp. 204-225
    • Blomberg, F.1    Cohen, R.S.2    Siekevitz, P.3
  • 2
    • 0019134836 scopus 로고
    • Isolation and characterization of postsynaptic densities from various brain regions: Enrichment of different types of postsynaptic densities
    • Carlin RK, Grab DJ, Cohen RS, Siekevitz P (1980) Isolation and characterization of postsynaptic densities from various brain regions: Enrichment of different types of postsynaptic densities. J Cell Biol 86(3):831-845.
    • (1980) J Cell Biol , vol.86 , Issue.3 , pp. 831-845
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.4
  • 3
    • 0017396421 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex, I: Overall morphology and protein composition
    • Cohen RS, Blomberg F, Berzins K, Siekevitz P (1977) The structure of postsynaptic densities isolated from dog cerebral cortex, I: Overall morphology and protein composition. J Cell Biol 74(1):181-203.
    • (1977) J Cell Biol , vol.74 , Issue.1 , pp. 181-203
    • Cohen, R.S.1    Blomberg, F.2    Berzins, K.3    Siekevitz, P.4
  • 4
    • 84863891896 scopus 로고    scopus 로고
    • Ultrastructure of synapses in the mammalian brain
    • Harris KM, Weinberg RJ (2012) Ultrastructure of synapses in the mammalian brain. Cold Spring Harb Perspect Biol 4(5):a005587.
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , Issue.5 , pp. a005587
    • Harris, K.M.1    Weinberg, R.J.2
  • 5
    • 41949110159 scopus 로고    scopus 로고
    • Organization of the core structure of the postsynaptic density
    • Chen X, et al. (2008) Organization of the core structure of the postsynaptic density. Proc Natl Acad Sci USA 105(11):4453-4458.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.11 , pp. 4453-4458
    • Chen, X.1
  • 6
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E, Sheng M (2004) PDZ domain proteins of synapses. Nat Rev Neurosci 5(10): 771-781.
    • (2004) Nat Rev Neurosci , vol.5 , Issue.10 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 7
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S, et al. (1999) Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23(3): 569-582.
    • (1999) Neuron , vol.23 , Issue.3 , pp. 569-582
    • Naisbitt, S.1
  • 8
    • 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
  • 9
    • 0034237258 scopus 로고    scopus 로고
    • PDZ domains in synapse assembly and signalling
    • Garner CC, Nash J, Huganir RL (2000) PDZ domains in synapse assembly and signalling. Trends Cell Biol 10(7):274-280.
    • (2000) Trends Cell Biol , vol.10 , Issue.7 , pp. 274-280
    • Garner, C.C.1    Nash, J.2    Huganir, R.L.3
  • 11
    • 0031052970 scopus 로고    scopus 로고
    • GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules
    • Kim E, et al. (1997) GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules. J Cell Biol 136(3):669-678.
    • (1997) J Cell Biol , vol.136 , Issue.3 , pp. 669-678
    • Kim, E.1
  • 12
    • 0030957966 scopus 로고    scopus 로고
    • SAPAPs: A family of PSD-95/SAP90-associated proteins localized at postsynaptic density
    • Takeuchi M, et al. (1997) SAPAPs: A family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J Biol Chem 272(18):11943-11951.
    • (1997) J Biol Chem , vol.272 , Issue.18 , pp. 11943-11951
    • Takeuchi, M.1
  • 13
    • 0031159260 scopus 로고    scopus 로고
    • DAP-1, a novel protein that interacts with the guanylate kinaselike domains of hDLG and PSD-95
    • Satoh K, et al. (1997) DAP-1, a novel protein that interacts with the guanylate kinaselike domains of hDLG and PSD-95. Genes Cells 2(6):415-424.
    • (1997) Genes Cells , vol.2 , Issue.6 , pp. 415-424
    • Satoh, K.1
  • 14
    • 84862698733 scopus 로고    scopus 로고
    • Functional consequences of mutations in postsynaptic scaffolding proteins and relevance to psychiatric disorders
    • Ting JT, Peça J, Feng G (2012) Functional consequences of mutations in postsynaptic scaffolding proteins and relevance to psychiatric disorders. Annu Rev Neurosci 35(1):49-71.
    • (2012) Annu Rev Neurosci , vol.35 , Issue.1 , pp. 49-71
    • Ting, J.T.1    Peça, J.2    Feng, G.3
  • 15
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins
    • Tu JC, et al. (1999) Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins. Neuron 23(3):583-592.
    • (1999) Neuron , vol.23 , Issue.3 , pp. 583-592
    • Tu, J.C.1
  • 16
    • 84938580400 scopus 로고    scopus 로고
    • Synaptic consolidation normalizes AMPAR quantal size following MAGUK loss
    • Levy JM, Chen X, Reese TS, Nicoll RA (2015) Synaptic consolidation normalizes AMPAR quantal size following MAGUK loss. Neuron 87(3):534-548.
    • (2015) Neuron , vol.87 , Issue.3 , pp. 534-548
    • Levy, J.M.1    Chen, X.2    Reese, T.S.3    Nicoll, R.A.4
  • 17
    • 84962128761 scopus 로고    scopus 로고
    • Mechanistic basis of MAGUK-organized complexes in synaptic development and signalling
    • Zhu J, Shang Y, Zhang M (2016) Mechanistic basis of MAGUK-organized complexes in synaptic development and signalling. Nat Rev Neurosci 17(4):209-223.
    • (2016) Nat Rev Neurosci , vol.17 , Issue.4 , pp. 209-223
    • Zhu, J.1    Shang, Y.2    Zhang, M.3
  • 18
    • 84881139928 scopus 로고    scopus 로고
    • Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95
    • Nair D, et al. (2013) Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95. J Neurosci 33(32):13204-13224.
    • (2013) J Neurosci , vol.33 , Issue.32 , pp. 13204-13224
    • Nair, D.1
  • 19
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins
    • Kim E, Cho KO, Rothschild A, Sheng M (1996) Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Neuron 17(1):103-113.
    • (1996) Neuron , vol.17 , Issue.1 , pp. 103-113
    • Kim, E.1    Cho, K.O.2    Rothschild, A.3    Sheng, M.4
  • 20
    • 77954657070 scopus 로고    scopus 로고
    • Functional impact of global rare copy number variation in autism spectrum disorders
    • Pinto D, et al. (2010) Functional impact of global rare copy number variation in autism spectrum disorders. Nature 466(7304):368-372.
    • (2010) Nature , vol.466 , Issue.7304 , pp. 368-372
    • Pinto, D.1
  • 21
    • 84860739976 scopus 로고    scopus 로고
    • SHANK1 deletions in males with autism spectrum disorder
    • Sato D, et al. (2012) SHANK1 deletions in males with autism spectrum disorder. Am J Hum Genet 90(5):879-887.
    • (2012) Am J Hum Genet , vol.90 , Issue.5 , pp. 879-887
    • Sato, D.1
  • 22
    • 79952243302 scopus 로고    scopus 로고
    • Family-based genetic association study of DLGAP3 in Tourette Syndrome
    • Crane J, et al. (2011) Family-based genetic association study of DLGAP3 in Tourette Syndrome. Am J Med Genet B 156B(1):108-114.
    • (2011) Am J Med Genet B 156B , vol.1 , pp. 108-114
    • Crane, J.1
  • 23
    • 67649422311 scopus 로고    scopus 로고
    • Sapap3 and pathological grooming in humans: Results from the OCD collaborative genetics study
    • Bienvenu OJ, et al. (2009) Sapap3 and pathological grooming in humans: Results from the OCD collaborative genetics study. Am J Med Genet B 150B(5):710-720.
    • (2009) Am J Med Genet B , vol.150 B , Issue.5 , pp. 710-720
    • Bienvenu, O.J.1
  • 24
    • 58049192995 scopus 로고    scopus 로고
    • Multiple rare SAPAP3 missense variants in trichotillomania and OCD
    • Züchner S, et al. (2009) Multiple rare SAPAP3 missense variants in trichotillomania and OCD. Mol Psychiatry 14(1):6-9.
    • (2009) Mol Psychiatry , vol.14 , Issue.1 , pp. 6-9
    • Züchner, S.1
  • 25
    • 84879422520 scopus 로고    scopus 로고
    • Genome-wide association study of obsessive-compulsive disorder
    • Stewart SE, et al.; North American Brain Expression Consortium; UK Brain Expression Database (2013) Genome-wide association study of obsessive-compulsive disorder. Mol Psychiatry 18(7):788-798.
    • (2013) Mol Psychiatry , vol.18 , Issue.7 , pp. 788-798
    • Stewart, S.E.1
  • 26
    • 78649753616 scopus 로고    scopus 로고
    • Association of mouse Dlg4 (PSD-95) gene deletion and human DLG4 gene variation with phenotypes relevant to autism spectrum disorders and Williams' syndrome
    • Feyder M, et al. (2010) Association of mouse Dlg4 (PSD-95) gene deletion and human DLG4 gene variation with phenotypes relevant to autism spectrum disorders and Williams' syndrome. Am J Psychiatry 167(12):1508-1517.
    • (2010) Am J Psychiatry , vol.167 , Issue.12 , pp. 1508-1517
    • Feyder, M.1
  • 27
    • 84856225986 scopus 로고    scopus 로고
    • De novo CNV analysis implicates specific abnormalities of postsynaptic signalling complexes in the pathogenesis of schizophrenia
    • Kirov G, et al. (2012) De novo CNV analysis implicates specific abnormalities of postsynaptic signalling complexes in the pathogenesis of schizophrenia. Mol Psychiatry 17(2):142-153.
    • (2012) Mol Psychiatry , vol.17 , Issue.2 , pp. 142-153
    • Kirov, G.1
  • 28
    • 0042828948 scopus 로고    scopus 로고
    • Molecular characterisation of the 22q13 deletion syndrome supports the role of haploinsufficiency of SHANK3/PROSAP2 in the major neurological symptoms
    • Wilson HL, et al. (2003) Molecular characterisation of the 22q13 deletion syndrome supports the role of haploinsufficiency of SHANK3/PROSAP2 in the major neurological symptoms. J Med Genet 40(8):575-584.
    • (2003) J Med Genet , vol.40 , Issue.8 , pp. 575-584
    • Wilson, H.L.1
  • 29
    • 84862996059 scopus 로고    scopus 로고
    • The postsynaptic organization of synapses
    • Sheng M, Kim E (2011) The postsynaptic organization of synapses. Cold Spring Harb Perspect Biol 3(12):a005678.
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.12 , pp. a005678
    • Sheng, M.1    Kim, E.2
  • 30
    • 84878459382 scopus 로고    scopus 로고
    • Nanoscale scaffolding domains within the postsynaptic density concentrate synaptic AMPA receptors
    • MacGillavry HD, Song Y, Raghavachari S, Blanpied TA (2013) Nanoscale scaffolding domains within the postsynaptic density concentrate synaptic AMPA receptors. Neuron 78(4):615-622.
    • (2013) Neuron , vol.78 , Issue.4 , pp. 615-622
    • MacGillavry, H.D.1    Song, Y.2    Raghavachari, S.3    Blanpied, T.A.4
  • 31
    • 78649927344 scopus 로고    scopus 로고
    • Superresolution imaging of chemical synapses in the brain
    • Dani A, Huang B, Bergan J, Dulac C, Zhuang X (2010) Superresolution imaging of chemical synapses in the brain. Neuron 68(5):843-856.
    • (2010) Neuron , vol.68 , Issue.5 , pp. 843-856
    • Dani, A.1    Huang, B.2    Bergan, J.3    Dulac, C.4    Zhuang, X.5
  • 33
    • 83555172372 scopus 로고    scopus 로고
    • Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho-protein-binding modules
    • Zhu J, et al. (2011) Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho-protein-binding modules. EMBO J 30(24):4986-4997.
    • (2011) EMBO J , vol.30 , Issue.24 , pp. 4986-4997
    • Zhu, J.1
  • 34
    • 79955536349 scopus 로고    scopus 로고
    • Shank3 mutant mice display autistic-like behaviours and striatal dysfunction
    • Peça J, et al. (2011) Shank3 mutant mice display autistic-like behaviours and striatal dysfunction. Nature 472(7344):437-442.
    • (2011) Nature , vol.472 , Issue.7344 , pp. 437-442
    • Peça, J.1
  • 35
    • 80054889797 scopus 로고    scopus 로고
    • Haploinsufficiency of the autism-associated Shank3 gene leads to deficits in synaptic function, social interaction, and social communication
    • Bozdagi O, et al. (2010) Haploinsufficiency of the autism-associated Shank3 gene leads to deficits in synaptic function, social interaction, and social communication. Mol Autism 1(1):15.
    • (2010) Mol Autism , vol.1 , Issue.1 , pp. 15
    • Bozdagi, O.1
  • 36
    • 79960111638 scopus 로고    scopus 로고
    • Synaptic dysfunction and abnormal behaviors in mice lacking major isoforms of Shank3
    • Wang X, et al. (2011) Synaptic dysfunction and abnormal behaviors in mice lacking major isoforms of Shank3. Hum Mol Genet 20(15):3093-3108.
    • (2011) Hum Mol Genet , vol.20 , Issue.15 , pp. 3093-3108
    • Wang, X.1
  • 37
    • 34548147472 scopus 로고    scopus 로고
    • Cortico-striatal synaptic defects and OCD-like behaviours in Sapap3-mutant mice
    • Welch JM, et al. (2007) Cortico-striatal synaptic defects and OCD-like behaviours in Sapap3-mutant mice. Nature 448(7156):894-900.
    • (2007) Nature , vol.448 , Issue.7156 , pp. 894-900
    • Welch, J.M.1
  • 38
    • 84900482526 scopus 로고    scopus 로고
    • Autism-associated gene Dlgap2 mutant mice demonstrate exacerbated aggressive behaviors and orbitofrontal cortex deficits
    • Jiang-Xie LF, et al. (2014) Autism-associated gene Dlgap2 mutant mice demonstrate exacerbated aggressive behaviors and orbitofrontal cortex deficits. Mol Autism 5:32.
    • (2014) Mol Autism , vol.5 , pp. 32
    • Jiang-Xie, L.F.1
  • 39
    • 84862274500 scopus 로고    scopus 로고
    • Autistic-like behaviours and hyperactivity in mice lacking ProSAP1/Shank2
    • Schmeisser MJ, et al. (2012) Autistic-like behaviours and hyperactivity in mice lacking ProSAP1/Shank2. Nature 486(7402):256-260.
    • (2012) Nature , vol.486 , Issue.7402 , pp. 256-260
    • Schmeisser, M.J.1
  • 40
    • 84862297282 scopus 로고    scopus 로고
    • Autistic-like social behaviour in Shank2-mutant mice improved by restoring NMDA receptor function
    • Won H, et al. (2012) Autistic-like social behaviour in Shank2-mutant mice improved by restoring NMDA receptor function. Nature 486(7402):261-265.
    • (2012) Nature , vol.486 , Issue.7402 , pp. 261-265
    • Won, H.1
  • 41
    • 84876070991 scopus 로고    scopus 로고
    • Modeling autism by SHANK gene mutations in mice
    • Jiang YH, Ehlers MD (2013) Modeling autism by SHANK gene mutations in mice. Neuron 78(1):8-27.
    • (2013) Neuron , vol.78 , Issue.1 , pp. 8-27
    • Jiang, Y.H.1    Ehlers, M.D.2
  • 42
    • 0033998542 scopus 로고    scopus 로고
    • Genetic evaluation of pervasive developmental disorders: The terminal 22q13 deletion syndrome may represent a recognizable phenotype
    • Prasad C, et al. (2000) Genetic evaluation of pervasive developmental disorders: The terminal 22q13 deletion syndrome may represent a recognizable phenotype. Clin Genet 57(2):103-109.
    • (2000) Clin Genet , vol.57 , Issue.2 , pp. 103-109
    • Prasad, C.1
  • 43
    • 0031791686 scopus 로고    scopus 로고
    • Two 22q telomere deletions serendipitously detected by FISH
    • Precht KS, et al. (1998) Two 22q telomere deletions serendipitously detected by FISH. J Med Genet 35(11):939-942.
    • (1998) J Med Genet , vol.35 , Issue.11 , pp. 939-942
    • Precht, K.S.1
  • 44
    • 3442888530 scopus 로고    scopus 로고
    • Terminal 22q deletion syndrome: A newly recognized cause of speech and language disability in the autism spectrum
    • Manning MA, et al. (2004) Terminal 22q deletion syndrome: A newly recognized cause of speech and language disability in the autism spectrum. Pediatrics 114(2): 451-457.
    • (2004) Pediatrics , vol.114 , Issue.2 , pp. 451-457
    • Manning, M.A.1
  • 45
    • 24344488907 scopus 로고    scopus 로고
    • Molecular and phenotypic characterization of ring chromosome 22
    • Jeffries AR, et al. (2005) Molecular and phenotypic characterization of ring chromosome 22. Am J Med Genet A 137(2):139-147.
    • (2005) Am J Med Genet A , vol.137 , Issue.2 , pp. 139-147
    • Jeffries, A.R.1
  • 46
    • 54049144653 scopus 로고    scopus 로고
    • Copy-number variations associated with neuropsychiatric conditions
    • Cook EH, Jr, Scherer SW (2008) Copy-number variations associated with neuropsychiatric conditions. Nature 455(7215):919-923.
    • (2008) Nature , vol.455 , Issue.7215 , pp. 919-923
    • Cook, E.H.1    Scherer, S.W.2
  • 47
    • 84887404798 scopus 로고    scopus 로고
    • SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties
    • Han K, et al. (2013) SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties. Nature 503(7474):72-77.
    • (2013) Nature , vol.503 , Issue.7474 , pp. 72-77
    • Han, K.1
  • 48
    • 79960779323 scopus 로고    scopus 로고
    • FMRP stalls ribosomal translocation on mRNAs linked to synaptic function and autism
    • Darnell JC, et al. (2011) FMRP stalls ribosomal translocation on mRNAs linked to synaptic function and autism. Cell 146(2):247-261.
    • (2011) Cell , vol.146 , Issue.2 , pp. 247-261
    • Darnell, J.C.1
  • 49
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N (2001) Regulation of translation initiation by FRAP/mTOR. Genes Dev 15(7):807-826.
    • (2001) Genes Dev , vol.15 , Issue.7 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 50
  • 51
    • 84939220718 scopus 로고    scopus 로고
    • An autism-linked mutation disables phosphorylation control of UBE3A
    • Yi JJ, et al. (2015) An autism-linked mutation disables phosphorylation control of UBE3A. Cell 162(4):795-807.
    • (2015) Cell , vol.162 , Issue.4 , pp. 795-807
    • Yi, J.J.1
  • 53
    • 84953839767 scopus 로고    scopus 로고
    • Mice with Shank3 mutations associated with ASD and schizophrenia display both shared and distinct defects
    • Zhou Y, et al. (2016) Mice with Shank3 mutations associated with ASD and schizophrenia display both shared and distinct defects. Neuron 89(1):147-162.
    • (2016) Neuron , vol.89 , Issue.1 , pp. 147-162
    • Zhou, Y.1
  • 54
    • 5344247263 scopus 로고    scopus 로고
    • The complexity of PDZ domain-mediated interactions at glutamatergic synapses: A case study on neuroligin
    • Meyer G, Varoqueaux F, Neeb A, Oschlies M, Brose N (2004) The complexity of PDZ domain-mediated interactions at glutamatergic synapses: A case study on neuroligin. Neuropharmacology 47(5):724-733.
    • (2004) Neuropharmacology , vol.47 , Issue.5 , pp. 724-733
    • Meyer, G.1    Varoqueaux, F.2    Neeb, A.3    Oschlies, M.4    Brose, N.5
  • 55
    • 0037805671 scopus 로고    scopus 로고
    • The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42
    • Park E, et al. (2003) The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42. J Biol Chem 278(21):19220-19229.
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 19220-19229
    • Park, E.1
  • 56
    • 13944262462 scopus 로고    scopus 로고
    • G-protein-coupled receptor modulation of striatal CaV1.3 L-type Ca2+channels is dependent on a Shank-binding domain
    • Olson PA, et al. (2005) G-protein-coupled receptor modulation of striatal CaV1.3 L-type Ca2+channels is dependent on a Shank-binding domain. J Neurosci 25(5): 1050-1062.
    • (2005) J Neurosci , vol.25 , Issue.5 , pp. 1050-1062
    • Olson, P.A.1
  • 57
    • 13944250584 scopus 로고    scopus 로고
    • Association of CaV1.3 L-type calcium channels with Shank
    • Zhang H, et al. (2005) Association of CaV1.3 L-type calcium channels with Shank. J Neurosci 25(5):1037-1049.
    • (2005) J Neurosci , vol.25 , Issue.5 , pp. 1037-1049
    • Zhang, H.1
  • 58
    • 0034693141 scopus 로고    scopus 로고
    • The calciumindependent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins
    • Kreienkamp HJ, Zitzer H, Gundelfinger ED, Richter D, Bockers TM (2000) The calciumindependent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins. J Biol Chem 275(42):32387-32390.
    • (2000) J Biol Chem , vol.275 , Issue.42 , pp. 32387-32390
    • Kreienkamp, H.J.1    Zitzer, H.2    Gundelfinger, E.D.3    Richter, D.4    Bockers, T.M.5
  • 59
    • 77349107353 scopus 로고    scopus 로고
    • Structural basis for asymmetric association of the betaPIX coiled coil and shank PDZ
    • Im YJ, et al. (2010) Structural basis for asymmetric association of the betaPIX coiled coil and shank PDZ. J Mol Biol 397(2):457-466.
    • (2010) J Mol Biol , vol.397 , Issue.2 , pp. 457-466
    • Im, Y.J.1
  • 60
    • 84884245462 scopus 로고    scopus 로고
    • Structures and target recognition modes of PDZ domains: Recurring themes and emerging pictures
    • Ye F, Zhang M (2013) Structures and target recognition modes of PDZ domains: Recurring themes and emerging pictures. Biochem J 455(1):1-14.
    • (2013) Biochem J , vol.455 , Issue.1 , pp. 1-14
    • Ye, F.1    Zhang, M.2
  • 61
    • 0348111461 scopus 로고    scopus 로고
    • Crystal structure of the Shank PDZ-ligand complex reveals a class i PDZ interaction and a novel PDZ-PDZ dimerization
    • Im YJ, et al. (2003) Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization. J Biol Chem 278(48):48099-48104.
    • (2003) J Biol Chem , vol.278 , Issue.48 , pp. 48099-48104
    • Im, Y.J.1
  • 62
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • Sala C, et al. (2001) Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 31(1):115-130.
    • (2001) Neuron , vol.31 , Issue.1 , pp. 115-130
    • Sala, C.1
  • 63
    • 17044378032 scopus 로고    scopus 로고
    • Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons
    • Roussignol G, et al. (2005) Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons. J Neurosci 25(14):3560-3570.
    • (2005) J Neurosci , vol.25 , Issue.14 , pp. 3560-3570
    • Roussignol, G.1
  • 64
    • 79953153131 scopus 로고    scopus 로고
    • Extensions of PDZ domains as important structural and functional elements
    • Wang CK, Pan L, Chen J, Zhang M (2010) Extensions of PDZ domains as important structural and functional elements. Protein Cell 1(8):737-751.
    • (2010) Protein Cell , vol.1 , Issue.8 , pp. 737-751
    • Wang, C.K.1    Pan, L.2    Chen, J.3    Zhang, M.4
  • 65
    • 77951212822 scopus 로고    scopus 로고
    • A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation
    • Bhattacharya S, et al. (2010) A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. J Biol Chem 285(13): 9981-9994.
    • (2010) J Biol Chem , vol.285 , Issue.13 , pp. 9981-9994
    • Bhattacharya, S.1
  • 66
    • 77749239813 scopus 로고    scopus 로고
    • The structure of the harmonin/sans complex reveals an unexpected interaction mode of the two Usher syndrome proteins
    • Yan J, Pan L, Chen X, Wu L, Zhang M (2010) The structure of the harmonin/sans complex reveals an unexpected interaction mode of the two Usher syndrome proteins. Proc Natl Acad Sci USA 107(9):4040-4045.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.9 , pp. 4040-4045
    • Yan, J.1    Pan, L.2    Chen, X.3    Wu, L.4    Zhang, M.5
  • 67
    • 58549092371 scopus 로고    scopus 로고
    • Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density
    • Feng W, Zhang M (2009) Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density. Nat Rev Neurosci 10(2):87-99.
    • (2009) Nat Rev Neurosci , vol.10 , Issue.2 , pp. 87-99
    • Feng, W.1    Zhang, M.2
  • 68
    • 84955477826 scopus 로고    scopus 로고
    • Human post-mortem synapse proteome integrity screening for proteomic studies of postsynaptic complexes
    • Bayés À, et al. (2014) Human post-mortem synapse proteome integrity screening for proteomic studies of postsynaptic complexes. Mol Brain 7(1):88.
    • (2014) Mol Brain , vol.7 , Issue.1 , pp. 88
    • Bayés, A.1
  • 69
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 70
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 71
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.