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Volumn 111, Issue 18, 2014, Pages

A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1

Author keywords

NMR; Nucleocytoplasmic shuttling; RNA deamination; RNA binding protein

Indexed keywords

ADENOSINE DEAMINASE; DOUBLE STRANDED RNA; MOLECULAR SCAFFOLD; NUCLEAR PROTEIN; RNA BINDING PROTEIN; TRANSPORTIN 1; UNCLASSIFIED DRUG;

EID: 84899893118     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1323698111     Document Type: Article
Times cited : (63)

References (59)
  • 1
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gö rlich D, Kutay U (1999) Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 15:607-660.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 2
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried H, Kutay U (2003) Nucleocytoplasmic transport: Taking an inventory. Cell Mol Life Sci 60(8):1659-1688
    • (2003) Cell Mol Life Sci , vol.60 , Issue.8 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 3
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A, Bono F, Jinek M, Conti E (2007) Structural biology of nucleocytoplasmic transport. Annu Rev Biochem 76:647-671
    • (2007) Annu Rev Biochem , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 4
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-s: Recognition and inhibition
    • Chook YM, Sü el KE (2011) Nuclear import by karyopherin-s: Recognition and inhibition. Biochim Biophys Acta 1813(9):1593-1606
    • (2011) Biochim Biophys Acta , vol.1813 , Issue.9 , pp. 1593-1606
    • Chook, Y.M.1    Süel, K.E.2
  • 5
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin alpha
    • Lange A, et al. (2007) Classical nuclear localization signals: Definition, function, and interaction with importin alpha. J Biol Chem 282(8):5101-5105
    • (2007) J Biol Chem , vol.282 , Issue.8 , pp. 5101-5105
    • Lange, A.1
  • 6
    • 0030595342 scopus 로고    scopus 로고
    • A novel receptor-mediated nuclear protein import pathway
    • Pollard VW, et al. (1996) A novel receptor-mediated nuclear protein import pathway. Cell 86(6):985-994
    • (1996) Cell , vol.86 , Issue.6 , pp. 985-994
    • Pollard, V.W.1
  • 7
    • 0030612604 scopus 로고    scopus 로고
    • Karyopherin beta2 mediates nuclear import of a mRNA binding protein
    • Bonifaci N, Moroianu J, Radu A, Blobel G (1997) Karyopherin beta2 mediates nuclear import of a mRNA binding protein. Proc Natl Acad Sci USA 94(10):5055-5060
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.10 , pp. 5055-5060
    • Bonifaci, N.1    Moroianu, J.2    Radu, A.3    Blobel, G.4
  • 8
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, et al. (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126(3):543-558
    • (2006) Cell , vol.126 , Issue.3 , pp. 543-558
    • Lee, B.J.1
  • 10
    • 34948857985 scopus 로고    scopus 로고
    • Structural basis for substrate recognition and dissociation by human transportin
    • Imasaki T, et al. (2007) Structural basis for substrate recognition and dissociation by human transportin Mol Cell 28(1):57-67
    • (2007) Mol Cell , vol.28 , Issue.1 , pp. 57-67
    • Imasaki, T.1
  • 11
    • 45849096845 scopus 로고    scopus 로고
    • Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals
    • Sü el KE, Gu H, Chook YM (2008) Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals. PLoS Biol 6(6):e137
    • (2008) PLoS Biol , vol.6 , Issue.6
    • Süel, K.E.1    Gu, H.2    Chook, Y.M.3
  • 12
    • 0040251482 scopus 로고    scopus 로고
    • Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells
    • Jäkel S, G örlich D (1998) Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. EMBO J 17(15):4491-4502
    • (1998) EMBO J , vol.17 , Issue.15 , pp. 4491-4502
    • Jäkel, S.1    Görlich, D.2
  • 13
    • 0034859839 scopus 로고    scopus 로고
    • Multiple pathways contribute to nuclear import of core histones
    • Mühlhä usser P, Müller EC, Otto A, Kutay U (2001) Multiple pathways contribute to nuclear import of core histones. EMBO Rep 2(8):690-696
    • (2001) EMBO Rep , vol.2 , Issue.8 , pp. 690-696
    • Mühlhäusser, P.1    Müller, E.C.2    Otto, A.3    Kutay, U.4
  • 14
    • 33746374437 scopus 로고    scopus 로고
    • Multiple importins function a s nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1
    • Arnold M, Nath A, Hauber J, Kehlenbach RH (2006) Multiple importins function a s nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1. J Biol Chem 281(30):20883-20890
    • (2006) J Biol Chem , vol.281 , Issue.30 , pp. 20883-20890
    • Arnold, M.1    Nath, A.2    Hauber, J.3    Kehlenbach, R.H.4
  • 15
    • 34948906397 scopus 로고    scopus 로고
    • Nuclear import of c-Jun is mediated by multiple transport receptors
    • Waldmann I, Wä lde S, Kehlenbach RH (2007) Nuclear import of c-Jun is mediated by multiple transport receptors. J Biol Chem 282(38):27685-27692
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 27685-27692
    • Waldmann, I.1    WälSmith, D.E.2    Kehlenbach, R.H.3
  • 16
    • 77952293063 scopus 로고    scopus 로고
    • Functions and regulation of RNA editing by ADAR deaminases
    • Nishikura K (2010) Functions and regulation of RNA editing by ADAR deaminases. Annu Rev Biochem 79:321-349.
    • (2010) Annu Rev Biochem , vol.79 , pp. 321-349
    • Nishikura, K.1
  • 18
    • 81855205059 scopus 로고    scopus 로고
    • ADAR proteins: Double-stranded RNA and Z-DNA binding domains
    • Barraud P, Allain FH (2012) ADAR proteins: Double-stranded RNA and Z-DNA binding domains. Curr Top Microbiol Immunol 353:35-60
    • (2012) Curr Top Microbiol Immunol , vol.353 , pp. 35-60
    • Barraud, P.1    Allain, F.H.2
  • 19
    • 0029164692 scopus 로고
    • Expression and regulation by interferon of a doublestranded- RNA-specific adenosine deaminase from human cells: Evidence for two forms of the deaminase
    • Patterson JB, Samuel CE (1995) Expression and regulation by interferon of a doublestranded- RNA-specific adenosine deaminase from human cells: Evidence for two forms of the deaminase. Mol Cell Biol 15(10):5376-5388
    • (1995) Mol Cell Biol , vol.15 , Issue.10 , pp. 5376-5388
    • Patterson, J.B.1    Samuel, C.E.2
  • 20
    • 0034779253 scopus 로고    scopus 로고
    • CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain
    • Poulsen H, Nilsson J, Damgaard CK, Egebjerg J, Kjems J (2001) CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain. Mol Cell Biol 21(22):7862-7871
    • (2001) Mol Cell Biol , vol.21 , Issue.22 , pp. 7862-7871
    • Poulsen, H.1    Nilsson, J.2    Damgaard, C.K.3    Egebjerg, J.4    Kjems, J.5
  • 21
    • 0038664237 scopus 로고    scopus 로고
    • Dynamic association of RNA-editing enzymes with the nucleolus
    • Desterro JM, et al. (2003) Dynamic association of RNA-editing enzymes with the nucleolus. J Cell Sci 116(Pt 9):1805-1818.
    • (2003) J Cell Sci , vol.116 , Issue.PART 9 , pp. 1805-1818
    • Desterro, J.M.1
  • 22
    • 0036856310 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-ric h export signal, and a putative dimerization domain
    • Strehblow A Hallegger M Jantsch MF, 2002, Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-ric h export signal, and a putative dimerization domain, Mol Biol Cell, 13,11, 3822-3835..
    • (2002) Mol Biol Cell , vol.13 , Issue.11 , pp. 3822-3835
    • Strehblow, A.1    Hallegger, M.2    Jantsch, M.F.3
  • 23
    • 62849103689 scopus 로고    scopus 로고
    • RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1
    • Fritz J, et al. (2009) RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1. Mol Cell Biol 29(6):1487-1497
    • (2009) Mol Cell Biol , vol.29 , Issue.6 , pp. 1487-1497
    • Fritz, J.1
  • 24
    • 0035150231 scopus 로고    scopus 로고
    • The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein
    • Eckmann CR, Neunteufl A, Pfaffstetter L, Jantsch MF (2001) The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein. Mol Biol Cell 12(7):1911-1924
    • (2001) Mol Biol Cell , vol.12 , Issue.7 , pp. 1911-1924
    • Eckmann, C.R.1    Neunteufl, A.2    Pfaffstetter, L.3    Jantsch, M.F.4
  • 26
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter JM, Schultz SC (1998) Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA. EMBO J 17(24): 7505-7513
    • (1998) EMBO J , vol.17 , Issue.24 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 27
    • 84878270899 scopus 로고    scopus 로고
    • RNA recognition by double-stranded RNA binding domains: A matter of shape and sequence
    • Masl iah G, Barraud P, Allain FH (2013) RNA recognition by double-stranded RNA binding domains: A matter of shape and sequence. Cell Mol Life Sci 70(11):1875 -1895
    • (2013) Cell Mol Life Sci , vol.70 , Issue.11 , pp. 1875-1895
    • Masl Iah, G.1    Barraud, P.2    Allain, F.H.3
  • 28
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. Coli RNase III
    • Kharrat A, Macias MJ, G ibson TJ, Nilges M, Pastore A (1995) Structure of the dsRNA binding domain of E. coli RNase III. EMBO J 14(14):3572-3584
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Ibson, T.J.G.3    Nilges, M.4    Pastore, A.5
  • 29
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M, Grü nert S, Murzin AG, Proctor M, St Johns ton D (1995) NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J 14(14):3563-3571
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 30
    • 0037033792 scopus 로고    scopus 로고
    • Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins
    • Brownawell A M, Macara IG (2002) Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins. J Cell Biol 156(1):53-64
    • (2002) J Cell Biol , vol.156 , Issue.1 , pp. 53-64
    • Brownawell, A.M.1    Macara, I.G.2
  • 31
    • 0037112842 scopus 로고    scopus 로고
    • Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
    • Calado A, Treichel N, Mü ller EC, Otto A, Kutay U (2002) Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J 21(22):6216-6224
    • (2002) EMBO J , vol.21 , Issue.22 , pp. 6216-6224
    • Calado, A.1    Treichel, N.2    Müller, E.C.3    Otto, A.4    Kutay, U.5
  • 32
    • 0347093422 scopus 로고    scopus 로고
    • Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3
    • Gwizdek C, et al. (2004) Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3. J Biol Chem 279(2): 884-891
    • (2004) J Biol Chem , vol.279 , Issue.2 , pp. 884-891
    • Gwizdek, C.1
  • 33
    • 3843145108 scopus 로고    scopus 로고
    • The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export
    • Macchi P, et al. (2004) The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export. J Biol Chem 279(30):31440-31444
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31440-31444
    • Macchi, P.1
  • 34
    • 84883197339 scopus 로고    scopus 로고
    • The double-stranded RNA binding domain of human Dicer functions as a nuclear localization signal
    • Doyle M, et al. (2013) The double-stranded RNA binding domain of human Dicer functions as a nuclear localization signal. RNA 19(9):1238-1252
    • (2013) RNA , vol.19 , Issue.9 , pp. 1238-1252
    • Doyle, M.1
  • 35
    • 74049138689 scopus 로고    scopus 로고
    • Nuclear retention of fission yeast dicer is a prerequisite for RNAi-mediated heterochromatin assembly
    • Emmerth S, et al. (2010) Nuclear retention of fission yeast dicer is a prerequisite for RNAi-mediated heterochromatin assembly. Dev Cell 18(1):102-113
    • (2010) Dev Cell , vol.18 , Issue.1 , pp. 102-113
    • Emmerth, S.1
  • 36
    • 80054907588 scopus 로고    scopus 로고
    • An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer
    • Barraud P, et al. (2011) An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer. EMBO J 30(20):4223-4235
    • (2011) EMBO J , vol.30 , Issue.20 , pp. 4223-4235
    • Barraud, P.1
  • 37
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • Callebaut I, et al. (1997) Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives. Cell Mol Life Sci 53(8): 621-645
    • (1997) Cell Mol Life Sci , vol.53 , Issue.8 , pp. 621-645
    • Callebaut, I.1
  • 38
    • 84864366184 scopus 로고    scopus 로고
    • Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
    • Zhang ZC, Chook YM (2012) Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). Proc Natl Acad Sci USA 109(30):12017- 12021
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.30 , pp. 12017-12021
    • Zhang, Z.C.1    Chook, Y.M.2
  • 39
    • 84879234011 scopus 로고    scopus 로고
    • Crystal structure of human Karyopherin 2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2
    • Soniat M, et al. (2013) Crystal structure of human Karyopherin 2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2. J Struct Funct Genomics 14(2):31-35
    • (2013) J Struct Funct Genomics , vol.14 , Issue.2 , pp. 31-35
    • Soniat, M.1
  • 40
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherinbeta2- Ran x GppNHp
    • Chook YM , Blobel G (1999) Structure of the nuclear transport complex karyopherinbeta2- Ran x GppNHp. Nature 399(6733):230-237
    • (1999) Nature , vol.399 , Issue.6733 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 41
    • 77957822421 scopus 로고    scopus 로고
    • The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove
    • Stefl R, et al. (2010) The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove. Cell 143(2):225-237
    • (2010) Cell , vol.143 , Issue.2 , pp. 225-237
    • Stefl, R.1
  • 42
    • 84861599510 scopus 로고    scopus 로고
    • Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA
    • Barraud P, Heale BS, O ?Connell MA, Allain FH (2012) Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA. Biochimie 94(7):1499-1509.
    • (2012) Biochimie , vol.94 , Issue.7 , pp. 1499-1509
    • Barraud, P.1    Heale, B.S.2    Oconnell, M.A.3    Allain, F.H.4
  • 43
    • 3342907152 scopus 로고    scopus 로고
    • A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III
    • Leulliot N et al. 2004, A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III, EMBO J23,13, 2468-2477..
    • (2004) EMBO J , vol.23 , Issue.13 , pp. 2468-2477
    • Leulliot, N.1
  • 44
    • 3042704491 scopus 로고    scopus 로고
    • Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III
    • Wu H, Henras A, Chanfreau G, Feigon J (2004) Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III. Proc Natl Acad Sci USA 101(22):8307-8312
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.22 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 45
    • 84876169592 scopus 로고    scopus 로고
    • Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRN A decay
    • Gleghorn ML, Gong C, Kielkopf CL, Maquat LE (2013) Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRN A decay. Nat Struct Mol Biol 20(4):515-524
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.4 , pp. 515-524
    • Gleghorn, M.L.1    Gong, C.2    Kielkopf, C.L.3    Maquat, L.E.4
  • 46
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin- proteins
    • Xu D, Farmer A, Chook YM (2010) Recognition of nuclear targeting signals by Karyopherin- proteins. Curr Opin Struct Biol 20(6):782-790
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.6 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 47
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS
    • Dormann D, et al. (2012) Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. EMBO J 31(22):4258-4275
    • (2012) EMBO J , vol.31 , Issue.22 , pp. 4258-4275
    • Dormann, D.1
  • 48
    • 84874253916 scopus 로고    scopus 로고
    • Redox-dependent control of FOXO/DAF-16 by transportin-1
    • Putker M, et al. (2013) Redox-dependent control of FOXO/DAF-16 by transportin-1. Mol Cell 49(4):730-742
    • (2013) Mol Cell , vol.49 , Issue.4 , pp. 730-742
    • Putker, M.1
  • 49
    • 0027456412 scopus 로고
    • Tautomeric states of the active-sit e histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • Pelton JG, Torchia DA, Meadow ND, Roseman S (1993) Tautomeric states of the active-sit e histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci 2(4):543-558
    • (1993) Protein Sci , vol.2 , Issue.4 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 50
    • 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, G üntert P, Wü thrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319(1):209-227
    • (2002) J Mol Biol , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 51
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Gü ntert P, Mumenthaler C, Wüthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273(1):283-298
    • (1997) J Mol Biol , vol.273 , Issue.1 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 52
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Gü ntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353-378
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 53
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated N OE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Gü ntert P, Wüthrich K (2002) Protein NMR structure determination with automated N OE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24(3):171-189
    • (2002) J Biomol NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 54
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brü nger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54(Pt 5): 905-921
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , Issue.PART 5 , pp. 905-921
    • Brünger, A.T.1
  • 55
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2(11):2728-2733
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 56
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8(4):477- 486
    • (1996) J Biomol NMR , vol.8 , Issue.4 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Mac Arthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 57
    • 84868207831 scopus 로고    scopus 로고
    • CING: An integrated residue-based structure validation program suite
    • Doreleijers JF, et al. (2012) CING: An integrated residue-based structure validation program suite. J Biomol NMR 54(3):267-283
    • (2012) J Biomol NMR , vol.54 , Issue.3 , pp. 267-283
    • Doreleijers, J.F.1
  • 58
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam SA, Marr RS, Gerace L (1990) Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J Cell Biol 111(3):807-816
    • (1990) J Cell Biol , vol.111 , Issue.3 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 59
    • 23644436824 scopus 로고    scopus 로고
    • Calcium phosphate-mediated transfection of eukaryotic cells
    • Anonymous
    • Anonymous (2005) Calcium phosphate-mediated transfection of eukaryotic cells. Nat Methods 2(4):319-320
    • (2005) Nat Methods , vol.2 , Issue.4 , pp. 319-320


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