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Volumn 69, Issue 1, 2007, Pages 192-198

Structural characterization of the neurabin sterile alpha motif domain

Author keywords

Coiled coil; Neurabin; NMR spectroscopy; SAM; Shank3; Spinophilin; Sterile alpha motif

Indexed keywords

MONOMER; NEURABIN; SPINOPHILIN; UNCLASSIFIED DRUG;

EID: 34548299656     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21513     Document Type: Article
Times cited : (6)

References (45)
  • 2
    • 0030922920 scopus 로고    scopus 로고
    • Allen PB, Ouimet CC, Greengard P. Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc Natl Acad Sci USA 1997;94:9956-9961.
    • Allen PB, Ouimet CC, Greengard P. Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc Natl Acad Sci USA 1997;94:9956-9961.
  • 5
    • 0035798093 scopus 로고    scopus 로고
    • The neurobiology of slow synaptic transmission
    • Greengard P. The neurobiology of slow synaptic transmission. Science 2001;294:1024-1030.
    • (2001) Science , vol.294 , pp. 1024-1030
    • Greengard, P.1
  • 8
    • 33847682529 scopus 로고    scopus 로고
    • NMR assignment of the spinophilin PDZ domain (493-602)
    • Kelker MS, Peti W. NMR assignment of the spinophilin PDZ domain (493-602). J Biomol NMR 2006;36 (Suppl 5):24.
    • (2006) J Biomol NMR , vol.36 , Issue.SUPPL. 5 , pp. 24
    • Kelker, M.S.1    Peti, W.2
  • 10
    • 0036357311 scopus 로고    scopus 로고
    • The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines
    • Grossman SD, Hsieh-Wilson LC, Allen PB, Nairn AC, Greengard P. The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines. Neuromolecular Med 2002;2:61-69.
    • (2002) Neuromolecular Med , vol.2 , pp. 61-69
    • Grossman, S.D.1    Hsieh-Wilson, L.C.2    Allen, P.B.3    Nairn, A.C.4    Greengard, P.5
  • 12
  • 14
    • 21544454679 scopus 로고    scopus 로고
    • The rho-specific GEF Lfc interacts with neurabin and spinophilin to regulate dendritic spine morphology
    • Ryan XP, Alldritt J, Svenningsson P, Allen PB, Wu GY, Nairn AC, Greengard P. The rho-specific GEF Lfc interacts with neurabin and spinophilin to regulate dendritic spine morphology. Neuron 2005;47: 85-100.
    • (2005) Neuron , vol.47 , pp. 85-100
    • Ryan, X.P.1    Alldritt, J.2    Svenningsson, P.3    Allen, P.B.4    Wu, G.Y.5    Nairn, A.C.6    Greengard, P.7
  • 15
    • 0035099354 scopus 로고    scopus 로고
    • The 62E early-late puff of Drosophila contains D-spinophilin, an ecdysone-inducible PDZ-domain protein dynamically expressed during metamorphosis
    • Keegan J, Schmerer M, Ring B, Garza D. The 62E early-late puff of Drosophila contains D-spinophilin, an ecdysone-inducible PDZ-domain protein dynamically expressed during metamorphosis. Genet Res 2001;77:27-39.
    • (2001) Genet Res , vol.77 , pp. 27-39
    • Keegan, J.1    Schmerer, M.2    Ring, B.3    Garza, D.4
  • 16
    • 0029091904 scopus 로고
    • A novel motif in yeast sterile and Drosophila polyhomeotic proteins
    • Ponting CP. SAM. A novel motif in yeast sterile and Drosophila polyhomeotic proteins. Protein Sci 1995;4:1928-1930.
    • (1995) Protein Sci , vol.4 , pp. 1928-1930
    • Ponting, C.S.1
  • 17
    • 0344196904 scopus 로고    scopus 로고
    • SAM domains: Uniform structure, diversity of function
    • Kim CA, Bowie JU. SAM domains: uniform structure, diversity of function. Trends Biochem Sci 2003;28:625-628.
    • (2003) Trends Biochem Sci , vol.28 , pp. 625-628
    • Kim, C.A.1    Bowie, J.U.2
  • 22
    • 0036828330 scopus 로고    scopus 로고
    • Structural role of zinc ions bound to postsynaptic densities
    • Jan HH, Chen IT, Tsai YY, Chang YC. Structural role of zinc ions bound to postsynaptic densities. J Neurochem 2002;83:525-534.
    • (2002) J Neurochem , vol.83 , pp. 525-534
    • Jan, H.H.1    Chen, I.T.2    Tsai, Y.Y.3    Chang, Y.C.4
  • 23
    • 33751419975 scopus 로고    scopus 로고
    • Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost
    • Peti W, Page R. Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 2007; 51:1-10.
    • (2007) Protein Expr Purif , vol.51 , pp. 1-10
    • Peti, W.1    Page, R.2
  • 24
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler J, Schleucher J, Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spectrosc 1999;34:93-158.
    • (1999) Prog NMR Spectrosc , vol.34 , pp. 93-158
    • Sattler, J.1    Schleucher, J.2    Griesinger, C.3
  • 25
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 2002;24:171-189.
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 26
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 2002;319:209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 27
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P. Automated NMR structure calculation with CYANA. Methods Mol Biol 2004;278:353-378.
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 31
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wúthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14: 29-32, 51-55.
    • (1996) J Mol Graph , vol.14
    • Koradi, R.1    Billeter, M.2    Wúthrich, K.3
  • 35
    • 0042490664 scopus 로고    scopus 로고
    • The RNA-binding SAM domain of Smaug defines a new family of posttranscriptional regulators
    • Aviv T, Lin Z, Lau S, Rendl LM, Sicheri F, Smibert CA. The RNA-binding SAM domain of Smaug defines a new family of posttranscriptional regulators. Nat Struct Biol 2003;10:614-621.
    • (2003) Nat Struct Biol , vol.10 , pp. 614-621
    • Aviv, T.1    Lin, Z.2    Lau, S.3    Rendl, L.M.4    Sicheri, F.5    Smibert, C.A.6
  • 40
    • 0033524982 scopus 로고    scopus 로고
    • Oligomeric structure of the human EphB2 receptor SAM domain
    • Thanos CD, Goodwill KE, Bowie JU. Oligomeric structure of the human EphB2 receptor SAM domain. Science 1999;283:833-836.
    • (1999) Science , vol.283 , pp. 833-836
    • Thanos, C.D.1    Goodwill, K.E.2    Bowie, J.U.3
  • 41
    • 4444326603 scopus 로고    scopus 로고
    • Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A
    • Kelker MS, Foss TR, Peti W, Teyton L, Kelly JW, Wüthrich K, Wilson IA. Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A. J Mol Biol 2004;342:1237-1248.
    • (2004) J Mol Biol , vol.342 , pp. 1237-1248
    • Kelker, M.S.1    Foss, T.R.2    Peti, W.3    Teyton, L.4    Kelly, J.W.5    Wüthrich, K.6    Wilson, I.A.7
  • 42
    • 0000521134 scopus 로고
    • Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra
    • Sklena V, Bax A. Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra. J Magn Reson 1987;74: 469-479.
    • (1987) J Magn Reson , vol.74 , pp. 469-479
    • Sklena, V.1    Bax, A.2
  • 43
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm L, Sander C. Searching protein structure databases has come of age. Proteins 1994;19:165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 44
    • 3242881211 scopus 로고    scopus 로고
    • Maiti R, Van Domselaar GH, Zhang H, Wishart DS. SuperPose: a simple server for sophisticated structural superposition. Nucleic Acids Res 2004;32(Web Server issue):W590-W594.
    • Maiti R, Van Domselaar GH, Zhang H, Wishart DS. SuperPose: a simple server for sophisticated structural superposition. Nucleic Acids Res 2004;32(Web Server issue):W590-W594.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.