메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Erratum: Nuclear import and export signals of human cohesins SA1/STAG1 and SA2/STAG2 expressed in Saccharomyces cerevisiae (PLoS ONE (2012) 7:6 (e38740) DOI: 10.1371/journal.pone.0038740);Nuclear import and export signals of human cohesins SA1/STAG1 and SA2/STAG2 expressed in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

COHESIN; PROTEIN SA1; PROTEIN SA2; PROTEIN STAG1; PROTEIN STAG2; UNCLASSIFIED DRUG; CELL NUCLEUS ANTIGEN; NUCLEAR EXPORT SIGNAL; NUCLEAR LOCALIZATION SIGNAL; NUCLEAR PROTEIN; RECOMBINANT PROTEIN; STAG1 PROTEIN, HUMAN; STAG2 PROTEIN, HUMAN;

EID: 84862023509     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0112338     Document Type: Erratum
Times cited : (9)

References (58)
  • 1
    • 0033083727 scopus 로고    scopus 로고
    • Yeast cohesin complex requires a conserved protein Eco1p(Ctf7) to establish cohesion between sister chromatids during DNA replication
    • Tóth A, Ciosk R, Uhlmann F, Galova M, Schleiffer A, (1999) Yeast cohesin complex requires a conserved protein Eco1p(Ctf7) to establish cohesion between sister chromatids during DNA replication. Genes Dev 13: 320 333.
    • (1999) Genes Dev , vol.13 , pp. 320
    • Tóth, A.1    Ciosk, R.2    Uhlmann, F.3    Galova, M.4    Schleiffer, A.5
  • 2
    • 0034618070 scopus 로고    scopus 로고
    • Identification and characterization of SA/Scc3p subunits in the Xenopus and human cohesin complexes
    • Losada A, Yokochi T, Kobayashi R, Hirano T, (2000) Identification and characterization of SA/Scc3p subunits in the Xenopus and human cohesin complexes. J Cell Biol 150: 405 416.
    • (2000) J Cell Biol , vol.150 , pp. 405
    • Losada, A.1    Yokochi, T.2    Kobayashi, R.3    Hirano, T.4
  • 3
    • 20544465434 scopus 로고    scopus 로고
    • SMC proteins and chromosome mechanics: from bacteria to humans
    • Hirano T, (2005) SMC proteins and chromosome mechanics: from bacteria to humans. Philos Trans R Soc Lond B Biol Sci 360: 507 514.
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , pp. 507
    • Hirano, T.1
  • 4
    • 58149192151 scopus 로고    scopus 로고
    • Cohesin complexes and sister chromatid cohesion in mammalian meiosis
    • Suja JA, Barbero JL, (2009) Cohesin complexes and sister chromatid cohesion in mammalian meiosis. Genome Dyn 5: 94 116.
    • (2009) Genome Dyn , vol.5 , pp. 94
    • Suja, J.A.1    Barbero, J.L.2
  • 5
    • 0034645067 scopus 로고    scopus 로고
    • Characterization of vertebrate cohesin complexes and their regulation in prophase
    • Sumara I, Vorlaufer E, Gieffers C, Peters BH, Peters JM, (2000) Characterization of vertebrate cohesin complexes and their regulation in prophase. J Cell Biol 151: 749 762.
    • (2000) J Cell Biol , vol.151 , pp. 749
    • Sumara, I.1    Vorlaufer, E.2    Gieffers, C.3    Peters, B.H.4    Peters, J.M.5
  • 7
    • 70449731229 scopus 로고    scopus 로고
    • Differential regulation of telomere and centromere cohesion by the Scc3 homologues SA1 and SA2 respectively in human cells
    • Canudas S, Smith S, (2009) Differential regulation of telomere and centromere cohesion by the Scc3 homologues SA1 and SA2 respectively in human cells. J Cell Biol 187: 165 173.
    • (2009) J Cell Biol , vol.187 , pp. 165
    • Canudas, S.1    Smith, S.2
  • 8
    • 79955433489 scopus 로고    scopus 로고
    • Lesson from the stoichiometry determination of the cohesin complex: A short protease mediated elution increases the recovery from cross-linked antibody-conjugated beads
    • Holzmann J, Fuchs J, Pichler P, Peters JM, Mechtler K, (2011) Lesson from the stoichiometry determination of the cohesin complex: A short protease mediated elution increases the recovery from cross-linked antibody-conjugated beads. J Proteome Res 10: 780 789.
    • (2011) J Proteome Res , vol.10 , pp. 780
    • Holzmann, J.1    Fuchs, J.2    Pichler, P.3    Peters, J.M.4    Mechtler, K.5
  • 9
    • 34347239300 scopus 로고    scopus 로고
    • Cohesin regulation: fashionable ways to wear a ring
    • Losada A, (2007) Cohesin regulation: fashionable ways to wear a ring. Chromosoma 116: 321 329.
    • (2007) Chromosoma , vol.116 , pp. 321
    • Losada, A.1
  • 10
    • 0037459376 scopus 로고    scopus 로고
    • Chromosomal Cohesin forms a ring
    • Gruber S, Haering CH, Nasmyth K, (2003) Chromosomal Cohesin forms a ring. Cell 112: 765 777.
    • (2003) Cell , vol.112 , pp. 765
    • Gruber, S.1    Haering, C.H.2    Nasmyth, K.3
  • 12
    • 33746486793 scopus 로고    scopus 로고
    • Live-cell imaging reveals a stable cohesin-chromatin interaction after but not before DNA replication
    • Gerlich D, Koch B, Dupeux F, Peters JM, Ellenberg J, (2006) Live-cell imaging reveals a stable cohesin-chromatin interaction after but not before DNA replication. Curr Biol 16: 1571 1578.
    • (2006) Curr Biol , vol.16 , pp. 1571
    • Gerlich, D.1    Koch, B.2    Dupeux, F.3    Peters, J.M.4    Ellenberg, J.5
  • 13
    • 63049136577 scopus 로고    scopus 로고
    • Intersection of ChIP and FLIP genomic methods to study the dynamics of the cohesin proteins
    • McNairn AJ, Gerton JL, (2009) Intersection of ChIP and FLIP genomic methods to study the dynamics of the cohesin proteins. Chromosome Res 17: 155 163.
    • (2009) Chromosome Res , vol.17 , pp. 155
    • McNairn, A.J.1    Gerton, J.L.2
  • 14
    • 34447514268 scopus 로고    scopus 로고
    • Structure and duplication of the centrosome J Cell Sci 120: (Part 13) 2139-2142
    • Azimzadeh J, Bornens M, (2007) Structure and duplication of the centrosome J Cell Sci 120: (Part 13) 2139-2142.
    • (2007)
    • Azimzadeh, J.1    Bornens, M.2
  • 15
    • 11844258789 scopus 로고    scopus 로고
    • Nuclear envelope: nuclear pore complexity
    • Sazer S, (2005) Nuclear envelope: nuclear pore complexity. Curr Biol 15: R23 R26.
    • (2005) Curr Biol , vol.15
    • Sazer, S.1
  • 16
    • 1342325423 scopus 로고    scopus 로고
    • Evidence of a transcriptional co-activator function of cohesin STAG/SA/Scc3
    • Lara-Pezzi E, Pezzi N, Prieto I, Barthelemy I, Carreiro C, (2004) Evidence of a transcriptional co-activator function of cohesin STAG/SA/Scc3. J Biol Chem 279: 6553 6559.
    • (2004) J Biol Chem , vol.279 , pp. 6553
    • Lara-Pezzi, E.1    Pezzi, N.2    Prieto, I.3    Barthelemy, I.4    Carreiro, C.5
  • 17
    • 79958065572 scopus 로고    scopus 로고
    • Specific sites in the C terminus of CTCF interact with the SA2 subunit of the cohesin complex and are required for cohesin-dependent insulation activity
    • Xiao T, Wallace J, Felsenfeld G, (2011) Specific sites in the C terminus of CTCF interact with the SA2 subunit of the cohesin complex and are required for cohesin-dependent insulation activity. Mol Cell Biol 31: 2174 2183.
    • (2011) Mol Cell Biol , vol.31 , pp. 2174
    • Xiao, T.1    Wallace, J.2    Felsenfeld, G.3
  • 18
    • 77956623136 scopus 로고
    • Variant mitoses in lower eukaryotes: indication of the evolution of mitosis?
    • Heath IB, (1980) Variant mitoses in lower eukaryotes: indication of the evolution of mitosis? Int Rev Cytol 64: 1 80.
    • (1980) Int Rev Cytol , vol.64 , pp. 1
    • Heath, I.B.1
  • 19
    • 0030748778 scopus 로고    scopus 로고
    • SA-1 a nuclear protein encoded by one member of a novel gene family: molecular cloning and detection in hemopoietic organs
    • Carramolino L, Lee BC, Zaballos A, Peled A, Barthelemy I, (1997) SA-1 a nuclear protein encoded by one member of a novel gene family: molecular cloning and detection in hemopoietic organs. Gene 195: 151 159.
    • (1997) Gene , vol.195 , pp. 151
    • Carramolino, L.1    Lee, B.C.2    Zaballos, A.3    Peled, A.4    Barthelemy, I.5
  • 20
    • 0036313652 scopus 로고    scopus 로고
    • STAG2 and Rad21mammalian mitotic cohesins are implicated in meiosis
    • Prieto I, Pezzi N, Buesa JM, Kremer L, Barthelemy I, (2002) STAG2 and Rad21mammalian mitotic cohesins are implicated in meiosis. EMBO Rep 3: 543 550.
    • (2002) EMBO Rep , vol.3 , pp. 543
    • Prieto, I.1    Pezzi, N.2    Buesa, J.M.3    Kremer, L.4    Barthelemy, I.5
  • 21
    • 51249091901 scopus 로고    scopus 로고
    • The F658G substitution in Saccharomyces cerevisiae cohesin Irr1/Scc3 is semi-dominant in the diploid and disturbs mitosis meiosis and the cell cycle
    • Cena A, Kozłowska E, Płochocka D, Grynberg M, Ishikawa T, (2008) The F658G substitution in Saccharomyces cerevisiae cohesin Irr1/Scc3 is semi-dominant in the diploid and disturbs mitosis meiosis and the cell cycle. Eur J Cell Biol 87: 831 844.
    • (2008) Eur J Cell Biol , vol.87 , pp. 831
    • Cena, A.1    Kozłowska, E.2    Płochocka, D.3    Grynberg, M.4    Ishikawa, T.5
  • 22
    • 71749098088 scopus 로고    scopus 로고
    • ELM: the status of the 2010 eukaryotic linear motif resource
    • (Database Issue)
    • Gould CM, Diella F, Via A, Puntervoll P, Gemünd C, (2009) ELM: the status of the 2010 eukaryotic linear motif resource. Nucleic Acids Res 38: (Database issue) D167-D180.
    • (2009) Nucleic Acids Res , vol.38
    • Gould, C.M.1    Diella, F.2    Via, A.3    Puntervoll, P.4    Gemünd, C.5
  • 23
    • 0030624540 scopus 로고    scopus 로고
    • Better prediction of protein cellular localization sites with the nearest neighbors classifier
    • Horton P, Nakai K, (1997) Better prediction of protein cellular localization sites with the nearest neighbors classifier. Proc Int Conf Intell Syst Mol Biol 5: 147 152.
    • (1997) Proc Int Conf Intell Syst Mol Biol , vol.5 , pp. 147
    • Horton, P.1    Nakai, K.2
  • 25
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F, (1991) Getting started with yeast. Methods Enzymol 194: 3 21.
    • (1991) Methods Enzymol , vol.194 , pp. 3
    • Sherman, F.1
  • 27
    • 0035897406 scopus 로고    scopus 로고
    • Nuclear import of histone H2A and H2B is mediated by a network of karyopherins
    • Mosammaparast N, Jackson KR, Guo Y, Brame C, J, Shabanowitz J, (2001) Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J Cell Biol 153: 251 262.
    • (2001) J Cell Biol , vol.153 , pp. 251
    • Mosammaparast, N.1    Jackson, K.R.2    Guo, Y.3    Brame, C.J.4    Shabanowitz, J.5
  • 28
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich 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
    • Görlich, D.1    Kutay, U.2
  • 29
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff B, Sanglier JJ, Wang Y, (1997) Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem Biol 4: 139 147.
    • (1997) Chem Biol , vol.4 , pp. 139
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 30
    • 0033168194 scopus 로고    scopus 로고
    • The NES-Crm1p export pathway is not a major mRNA export route in Saccharomyces cerevisiae
    • Neville M, Rosbash M, (1999) The NES-Crm1p export pathway is not a major mRNA export route in Saccharomyces cerevisiae. EMBO J 18: 3746 3756.
    • (1999) EMBO J , vol.18 , pp. 3746
    • Neville, M.1    Rosbash, M.2
  • 31
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade K, Ford C, S, Guthrie C, Weis K, (1997) Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90: 1041 1050.
    • (1997) Cell , vol.90 , pp. 1041
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 32
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • Kutay U, Guttinger S, (2005) Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol 15: 121 124.
    • (2005) Trends Cell Biol , vol.15 , pp. 121
    • Kutay, U.1    Guttinger, S.2
  • 33
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M, Asano S, Nakamura T, Adachi M, Yoshida M, (1997) CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390: 308 311.
    • (1997) Nature , vol.390 , pp. 308
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5
  • 34
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich D, Mattaj IW, (1996) Nucleocytoplasmic transport. Science 271: 1513 1518.
    • (1996) Science , vol.271 , pp. 1513
    • Görlich, D.1    Mattaj, I.W.2
  • 35
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: signals mechanisms and regulation
    • Nigg EA, (1997) Nucleocytoplasmic transport: signals mechanisms and regulation. Nature 386: 779 787.
    • (1997) Nature , vol.386 , pp. 779
    • Nigg, E.A.1
  • 36
    • 0032078933 scopus 로고    scopus 로고
    • Importins and exportins: how to get in and out of the nucleus
    • Weis K, (1998) Importins and exportins: how to get in and out of the nucleus. Trends Biochem Sci 23: 185 189.
    • (1998) Trends Biochem Sci , vol.23 , pp. 185
    • Weis, K.1
  • 37
    • 0037099061 scopus 로고    scopus 로고
    • The molecular mechanism of translocation through the nuclear pore complex is highly conserved
    • Feldherr C, Akin D, Littlewood T, Stewart M, (2002) The molecular mechanism of translocation through the nuclear pore complex is highly conserved. J, Cell Sci 115: 2997 3005.
    • (2002) J, Cell Sci , vol.115 , pp. 2997
    • Feldherr, C.1    Akin, D.2    Littlewood, T.3    Stewart, M.4
  • 38
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: from nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast N, Pemberton LF, (2004) Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol 14: 547 556.
    • (2004) Trends Cell Biol , vol.14 , pp. 547
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 39
    • 8644262258 scopus 로고    scopus 로고
    • Importin: conducting a much larger cellular symphony
    • Harel A, Forbes DJ, (2004) Importin: conducting a much larger cellular symphony. Mol Cell 16: 319 330.
    • (2004) Mol Cell , vol.16 , pp. 319
    • Harel, A.1    Forbes, D.J.2
  • 40
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • Mosammaparast N, Ewart CS, Pemberton LF, (2002) A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J 21: 6527 6538.
    • (2002) EMBO J , vol.21 , pp. 6527
    • Mosammaparast, N.1    Ewart, C.S.2    Pemberton, L.F.3
  • 41
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport
    • Terry LJ, Shows EB, Wente SR, (2007) Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 318: 1412 1416.
    • (2007) Science , vol.318 , pp. 1412
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 42
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, Boesche M, Krause R, Grandi P, Marzioch M, (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141 147.
    • (2002) Nature , vol.415 , pp. 141
    • Gavin, A.C.1    Boesche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5
  • 43
    • 18044372415 scopus 로고    scopus 로고
    • Yeast as a model for medical and medicinal research
    • Mager WH, Winderickx J, (2005) Yeast as a model for medical and medicinal research. Trends Pharmacol Sci 26: 265 273.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 265
    • Mager, W.H.1    Winderickx, J.2
  • 44
    • 34247565146 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae as a Tool for Human Gene Function Discovery
    • In: Stansfield I, Stark MJR, editors, editors
    • Waterham HR, Wanders RJA, (2007) Saccharomyces cerevisiae as a Tool for Human Gene Function Discovery. In: Stansfield I, Stark MJR, editors. pp. 577 595 editors. Methods in Microbiology. Academic Press.
    • (2007) , pp. 577
    • Waterham, H.R.1    Wanders, R.J.A.2
  • 45
    • 79955422755 scopus 로고    scopus 로고
    • Cohesin plays a dual role in gene regulation and sister-chromatid cohesion during meiosis in Saccharomyces cerevisiae
    • Lin W, Wang M, Jin H, Yu HG, (2011) Cohesin plays a dual role in gene regulation and sister-chromatid cohesion during meiosis in Saccharomyces cerevisiae. Genetics 187: 1041 1051.
    • (2011) Genetics , vol.187 , pp. 1041
    • Lin, W.1    Wang, M.2    Jin, H.3    Yu, H.G.4
  • 48
    • 52949096859 scopus 로고    scopus 로고
    • The function of Stat3 in tumor cells and their microenvironment
    • Groner B, Lucks P, Borghouts C, (2008) The function of Stat3 in tumor cells and their microenvironment. Semin Cell Dev Biol 19: 341 350.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 341
    • Groner, B.1    Lucks, P.2    Borghouts, C.3
  • 49
    • 38449087713 scopus 로고    scopus 로고
    • ChREBP a transcriptional regulator of glucose and lipid metabolism
    • Postic C, Dentin R, Denechaud PD, Girard J, (2007) ChREBP a transcriptional regulator of glucose and lipid metabolism. Annu Rev Nutr 27: 179 192.
    • (2007) Annu Rev Nutr , vol.27 , pp. 179
    • Postic, C.1    Dentin, R.2    Denechaud, P.D.3    Girard, J.4
  • 50
    • 18044393595 scopus 로고    scopus 로고
    • Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2
    • Hauf S, Roitinger E, Koch B, Dittrich CM, Mechtler K, Peters JM, (2005) Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2. PLoS Biol 3: e69.
    • (2005) PLoS Biol , vol.3
    • Hauf, S.1    Roitinger, E.2    Koch, B.3    Dittrich, C.M.4    Mechtler, K.5    Peters, J.M.6
  • 51
    • 0034906982 scopus 로고    scopus 로고
    • Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I. Nat, Cell Biol
    • Prieto I, Suja JA, Pezzi N, Kremer L, Martinez AC, (2001) Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I. Nat, Cell Biol 3: 761 766.
    • (2001) , vol.3 , pp. 761
    • Prieto, I.1    Suja, J.A.2    Pezzi, N.3    Kremer, L.4    Martinez, A.C.5
  • 52
    • 33751202679 scopus 로고    scopus 로고
    • Nuclear exclusion of separase prevents cohesin cleavage in interphase cells
    • Sun Y, Yu H, Zou H, (2006) Nuclear exclusion of separase prevents cohesin cleavage in interphase cells. Cell Cycle 5: 2537 2542.
    • (2006) Cell Cycle , vol.5 , pp. 2537
    • Sun, Y.1    Yu, H.2    Zou, H.3
  • 53
    • 0037440429 scopus 로고    scopus 로고
    • Regulation of tumor suppressors by nuclear-cytoplasmic shuttling
    • Fabbro M, Henderson BR, (2003) Regulation of tumor suppressors by nuclear-cytoplasmic shuttling. Exp Cell Res 282: 59 69.
    • (2003) Exp Cell Res , vol.282 , pp. 59
    • Fabbro, M.1    Henderson, B.R.2
  • 54
    • 26244466612 scopus 로고    scopus 로고
    • Regulation of BRCA1 BRCA2 and BARD1 intracellular trafficking
    • Henderson BR, (2005) Regulation of BRCA1 BRCA2 and BARD1 intracellular trafficking. Bioessays 27: 884 893.
    • (2005) Bioessays , vol.27 , pp. 884
    • Henderson, B.R.1
  • 55
    • 19744367092 scopus 로고    scopus 로고
    • Identification of multiple nuclear export sequences in Fanconi anemia group A protein that contribute to CRM1-dependent nuclear export
    • Ferrer M, Rodriguez JA, Spierings EA, de Winter JP, Giaccone G, (2005) Identification of multiple nuclear export sequences in Fanconi anemia group A protein that contribute to CRM1-dependent nuclear export. Hum Mol Genet 14: 1271 1281.
    • (2005) Hum Mol Genet , vol.14 , pp. 1271
    • Ferrer, M.1    Rodriguez, J.A.2    Spierings, E.A.3    de Winter, J.P.4    Giaccone, G.5
  • 56
    • 32444448831 scopus 로고    scopus 로고
    • Importin-beta family members mediate alpharetrovirus gag nuclear entry via interactions with matrix and nucleocapsid
    • Butterfield-Gerson KL, Scheifele LZ, Ryan EP, Hopper AK, Parent LJ, (2006) Importin-beta family members mediate alpharetrovirus gag nuclear entry via interactions with matrix and nucleocapsid. J Virol 80: 1798 17806.
    • (2006) J Virol , vol.80 , pp. 1798
    • Butterfield-Gerson, K.L.1    Scheifele, L.Z.2    Ryan, E.P.3    Hopper, A.K.4    Parent, L.J.5
  • 57
    • 0032998951 scopus 로고    scopus 로고
    • Antagonistic effects of NES and NLS motifs determine S, cerevisiae Rna1p subcellular distribution
    • Feng W, Benko AL, Lee JH, Stanford DR, Hopper AK, (1999) Antagonistic effects of NES and NLS motifs determine S, cerevisiae Rna1p subcellular distribution. J Cell Sci 112: 339 347.
    • (1999) J Cell Sci , vol.112 , pp. 339
    • Feng, W.1    Benko, A.L.2    Lee, J.H.3    Stanford, D.R.4    Hopper, A.K.5
  • 58
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR, (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51 59.
    • (1989) Gene , vol.77 , pp. 51
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.