메뉴 건너뛰기




Volumn 28, Issue 5, 2008, Pages 1755-1769

Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export

Author keywords

[No Author keywords available]

Indexed keywords

CENTRIN; DIGITONIN; MESSENGER RNA; NUCLEOPORIN; CALCIUM BINDING PROTEIN; CELL CYCLE PROTEIN; CENTRIN 2 PROTEIN, XENOPUS; CETN2 PROTEIN, HUMAN; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEIN; KARYOPHERIN; NUCLEAR PROTEIN; NUP160 PROTEIN, XENOPUS; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; XENOPUS PROTEIN;

EID: 40749091704     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01697-07     Document Type: Article
Times cited : (69)

References (142)
  • 1
    • 0034687059 scopus 로고    scopus 로고
    • Structure, expression, and chromosomal localization of the human gene encoding a germinal center-associated nuclear protein (GANP) that associates with MCM3 involved in the initiation of DNA replication
    • Abe, E., K. Kuwahara, M. Yoshida, M. Suzuki, H. Terasaki, Y. Matsuo, E. I. Takahashi, and N. Sakaguchi. 2000. Structure, expression, and chromosomal localization of the human gene encoding a germinal center-associated nuclear protein (GANP) that associates with MCM3 involved in the initiation of DNA replication. Gene 255:219-227.
    • (2000) Gene , vol.255 , pp. 219-227
    • Abe, E.1    Kuwahara, K.2    Yoshida, M.3    Suzuki, M.4    Terasaki, H.5    Matsuo, Y.6    Takahashi, E.I.7    Sakaguchi, N.8
  • 2
    • 0029592161 scopus 로고
    • Nup120p: A yeast nucleoporin required for NPC distribution and mRNA transport
    • Aitchison, J. D., G. Blobel, and M. P. Rout. 1995. Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transport. J. Cell Biol. 131:1659-1675.
    • (1995) J. Cell Biol , vol.131 , pp. 1659-1675
    • Aitchison, J.D.1    Blobel, G.2    Rout, M.P.3
  • 3
    • 0034126815 scopus 로고    scopus 로고
    • The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm
    • Allen, T. D., J. M. Cronshaw, S. Bagley, E. Kiseleva, and M. W. Goldberg. 2000. The nuclear pore complex: mediator of translocation between nucleus and cytoplasm. J. Cell Sci. 113:1651-1659.
    • (2000) J. Cell Sci , vol.113 , pp. 1651-1659
    • Allen, T.D.1    Cronshaw, J.M.2    Bagley, S.3    Kiseleva, E.4    Goldberg, M.W.5
  • 4
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki, M., C. Masutani, M. Takemura, A. Uchida, K. Sugasawa, J. Kondoh, Y. Ohkuma, and F. Hanaoka. 2001. Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J. Biol. Chem. 276:18665-18672.
    • (2001) J. Biol. Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 7
    • 3042712133 scopus 로고    scopus 로고
    • The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution, and proper cell division
    • Baï, S. W., J. Rouquette, M. Umeda, W. Faigle, D. Loew, S. Sazer, and V. Doye. 2004. The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution, and proper cell division. Mol. Cell. Biol. 24:6379-6392.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6379-6392
    • Baï, S.W.1    Rouquette, J.2    Umeda, M.3    Faigle, W.4    Loew, D.5    Sazer, S.6    Doye, V.7
  • 8
    • 0029743063 scopus 로고    scopus 로고
    • Targeting and function in mRNA export of nuclear pore complex protein Nup153
    • Bastos, R., A. Lin, M. Enarson, and B. Burke. 1996. Targeting and function in mRNA export of nuclear pore complex protein Nup153. J. Cell Biol. 134:1141-1156.
    • (1996) J. Cell Biol , vol.134 , pp. 1141-1156
    • Bastos, R.1    Lin, A.2    Enarson, M.3    Burke, B.4
  • 9
    • 0029951644 scopus 로고    scopus 로고
    • The SAC3 gene encodes a nuclear protein required for normal progression of mitosis
    • Bauer, A., and R. Kolling. 1996. The SAC3 gene encodes a nuclear protein required for normal progression of mitosis. J. Cell Sci. 109:1575-1583.
    • (1996) J. Cell Sci , vol.109 , pp. 1575-1583
    • Bauer, A.1    Kolling, R.2
  • 10
    • 0022501926 scopus 로고
    • Yeast gene required for spindle pole body duplication: Homology of its product with Ca2+-binding proteins
    • Baum, P., C. Furlong, and B. Byers. 1986. Yeast gene required for spindle pole body duplication: homology of its product with Ca2+-binding proteins. Proc. Natl. Acad. Sci. USA 83:5512-5516.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5512-5516
    • Baum, P.1    Furlong, C.2    Byers, B.3
  • 12
    • 17444411537 scopus 로고    scopus 로고
    • A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly
    • Blower, M. D., M. Nachury, R. Heald, and K. Weis. 2005. A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. Cell 121:223-234.
    • (2005) Cell , vol.121 , pp. 223-234
    • Blower, M.D.1    Nachury, M.2    Heald, R.3    Weis, K.4
  • 13
    • 0031935821 scopus 로고    scopus 로고
    • Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis
    • Boer, J., J. Bonten-Surtel, and G. Grosveld. 1998. Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis. Mol. Cell. Biol. 18:1236-1247.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1236-1247
    • Boer, J.1    Bonten-Surtel, J.2    Grosveld, G.3
  • 14
    • 0141764733 scopus 로고    scopus 로고
    • Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans
    • Cohen, M., N. Feinstein, K. L. Wilson, and Y. Gruenbaum. 2003. Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans. Mol. Biol. Cell 14:4230-4237.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4230-4237
    • Cohen, M.1    Feinstein, N.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 15
    • 33646516400 scopus 로고    scopus 로고
    • Transport of messenger RNA from the nucleus to the cytoplasm
    • Cole, C. N., and J. J. Scarcelli. 2006. Transport of messenger RNA from the nucleus to the cytoplasm. Curr. Opin. Cell Biol. 18:299-306.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 299-306
    • Cole, C.N.1    Scarcelli, J.J.2
  • 16
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • Conti, E., and E. Izaurralde. 2001. Nucleocytoplasmic transport enters the atomic age. Curr. Opin. Cell Biol. 13:310-319.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 17
    • 0028858573 scopus 로고
    • High content of a nuclear pore complex protein in cytoplasmic annulate lamellae of Xenopus oocytes
    • Cordes, V. C., S. Reidenbach, and W. W. Franke. 1995. High content of a nuclear pore complex protein in cytoplasmic annulate lamellae of Xenopus oocytes. Eur. J. Cell Biol. 68:240-255.
    • (1995) Eur. J. Cell Biol , vol.68 , pp. 240-255
    • Cordes, V.C.1    Reidenbach, S.2    Franke, W.W.3
  • 19
    • 0026099941 scopus 로고
    • Spontaneous assembly of pore complex-containing membranes ("annulate lamellae") in Xenopus egg extract in the absence of chromatin
    • Dabauvalle, M. C., K. Loos, H. Merkert, and U. Scheer. 1991. Spontaneous assembly of pore complex-containing membranes ("annulate lamellae") in Xenopus egg extract in the absence of chromatin. J. Cell Biol. 112:1073-1082.
    • (1991) J. Cell Biol , vol.112 , pp. 1073-1082
    • Dabauvalle, M.C.1    Loos, K.2    Merkert, H.3    Scheer, U.4
  • 20
    • 0036932209 scopus 로고    scopus 로고
    • In situ analysis of spatial relationships between proteins of the nuclear pore complex
    • Damelin, M., and P. A. Silver. 2002. In situ analysis of spatial relationships between proteins of the nuclear pore complex. Biophys. J. 83:3626-3636.
    • (2002) Biophys. J , vol.83 , pp. 3626-3636
    • Damelin, M.1    Silver, P.A.2
  • 21
    • 0035226671 scopus 로고    scopus 로고
    • GFP-centrin as a marker for centriole dynamics in the human breast cancer cell line MCF-7
    • D'Assoro, A. B., F. Stivala, S. Barrett, G. Ferrigno, and J. L. Salisbury. 2001. GFP-centrin as a marker for centriole dynamics in the human breast cancer cell line MCF-7. Ital. J. Anat. Embryol. 106:103-110.
    • (2001) Ital. J. Anat. Embryol , vol.106 , pp. 103-110
    • D'Assoro, A.B.1    Stivala, F.2    Barrett, S.3    Ferrigno, G.4    Salisbury, J.L.5
  • 22
    • 0031038521 scopus 로고    scopus 로고
    • C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure
    • Dockendorff, T. C., C. V. Heath, A. L. Goldstein, C. A. Snay, and C. N. Cole. 1997. C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure. Mol. Cell. Biol. 17:906-920.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 906-920
    • Dockendorff, T.C.1    Heath, C.V.2    Goldstein, A.L.3    Snay, C.A.4    Cole, C.N.5
  • 23
    • 0028607144 scopus 로고
    • A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution
    • Doye, V., R. Wepf, and E. C. Hurt. 1994. A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution. EMBO J. 13:6062-6075.
    • (1994) EMBO J , vol.13 , pp. 6062-6075
    • Doye, V.1    Wepf, R.2    Hurt, E.C.3
  • 24
    • 0037043334 scopus 로고    scopus 로고
    • Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation
    • Drummond, S. P., and K. L. Wilson. 2002. Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation. J. Cell Biol. 158:53-62.
    • (2002) J. Cell Biol , vol.158 , pp. 53-62
    • Drummond, S.P.1    Wilson, K.L.2
  • 25
    • 0141529759 scopus 로고    scopus 로고
    • Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex
    • Enninga, J., A. Levay, and B. M. Fontoura. 2003. Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex. Mol. Cell. Biol. 23:7271-7284.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7271-7284
    • Enninga, J.1    Levay, A.2    Fontoura, B.M.3
  • 27
    • 2142826777 scopus 로고    scopus 로고
    • Nuclear export of mRNA: From the site of transcription to the cytoplasm
    • Erkmann, J. A., and U. Kutay. 2004. Nuclear export of mRNA: from the site of transcription to the cytoplasm. Exp. Cell Res. 296:12-20.
    • (2004) Exp. Cell Res , vol.296 , pp. 12-20
    • Erkmann, J.A.1    Kutay, U.2
  • 28
    • 11144335418 scopus 로고    scopus 로고
    • Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP
    • Erkmann, J. A., R. Sanchez, N. Treichel, W. F. Marzluff, and U. Kutay. 2005. Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP. RNA 11:45-58.
    • (2005) RNA , vol.11 , pp. 45-58
    • Erkmann, J.A.1    Sanchez, R.2    Treichel, N.3    Marzluff, W.F.4    Kutay, U.5
  • 29
    • 0027958218 scopus 로고
    • Cloning of a cDNA encoding human centrin, an EF-hand protein of centrosomes and mitotic spindle poles
    • Errabolu, R., M. A. Sanders, and J. L. Salisbury. 1994. Cloning of a cDNA encoding human centrin, an EF-hand protein of centrosomes and mitotic spindle poles. J. Cell Sci. 107:9-16.
    • (1994) J. Cell Sci , vol.107 , pp. 9-16
    • Errabolu, R.1    Sanders, M.A.2    Salisbury, J.L.3
  • 30
    • 0025162266 scopus 로고
    • Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored
    • Finlay, D. R., and D. J. Forbes. 1990. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60:17-29.
    • (1990) Cell , vol.60 , pp. 17-29
    • Finlay, D.R.1    Forbes, D.J.2
  • 32
    • 18744370194 scopus 로고    scopus 로고
    • The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores
    • Fischer, T., K. Strasser, A. Racz, S. Rodriguez-Navarro, M. Oppizzi, P. Ihrig, J. Lechner, and E. Hurt. 2002. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 21:5843-5852.
    • (2002) EMBO J , vol.21 , pp. 5843-5852
    • Fischer, T.1    Strasser, K.2    Racz, A.3    Rodriguez-Navarro, S.4    Oppizzi, M.5    Ihrig, P.6    Lechner, J.7    Hurt, E.8
  • 33
    • 0029130169 scopus 로고
    • The HIV-1 Rev. activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., J. Huber, W. C. Boelens, I. W. Mattaj, and R. Luhrmann. 1995. The HIV-1 Rev. activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 34
  • 35
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 37
    • 0029911192 scopus 로고    scopus 로고
    • Binding of centrins and yeast calmodulin to synthetic peptides corresponding to binding sites in the spindle pole body components Kar1p and Spc110p
    • Geier, B. M., H. Wiech, and E. Schiebel. 1996. Binding of centrins and yeast calmodulin to synthetic peptides corresponding to binding sites in the spindle pole body components Kar1p and Spc110p. J. Biol. Chem. 271:28366-28374.
    • (1996) J. Biol. Chem , vol.271 , pp. 28366-28374
    • Geier, B.M.1    Wiech, H.2    Schiebel, E.3
  • 38
    • 0029982655 scopus 로고    scopus 로고
    • Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p
    • Goldstein, A. L., C. A. Snay, C. V. Heath, and C. N. Cole. 1996. Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p. Mol. Biol. Cell 7:917-934.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 917-934
    • Goldstein, A.L.1    Snay, C.A.2    Heath, C.V.3    Cole, C.N.4
  • 39
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D., and U. Kutay. 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
    • Gorlich, D.1    Kutay, U.2
  • 40
    • 0030824317 scopus 로고    scopus 로고
    • Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly
    • Grandi, P., T. Dang, N. Pane, A. Shevchenko, M. Mann, D. Forbes, and E. Hurt. 1997. Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly. Mol. Biol. Cell 8:2017-2038.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2017-2038
    • Grandi, P.1    Dang, T.2    Pane, N.3    Shevchenko, A.4    Mann, M.5    Forbes, D.6    Hurt, E.7
  • 41
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus
    • Greber, U. F., and L. Gerace. 1995. Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell Biol. 128:5-14.
    • (1995) J. Cell Biol , vol.128 , pp. 5-14
    • Greber, U.F.1    Gerace, L.2
  • 42
    • 0026500909 scopus 로고
    • Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein
    • Greber, U. F., and L. Gerace. 1992. Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein. J. Cell Biol. 116:15-30.
    • (1992) J. Cell Biol , vol.116 , pp. 15-30
    • Greber, U.F.1    Gerace, L.2
  • 43
    • 0036223543 scopus 로고    scopus 로고
    • Nup98 is a mobile nucleoporin with transcription-dependent dynamics
    • Griffis, E. R., N. Altan, J. Lippincott-Schwartz, and M. A. Powers. 2002. Nup98 is a mobile nucleoporin with transcription-dependent dynamics. Mol. Biol Cell 13:1282-1297.
    • (2002) Mol. Biol Cell , vol.13 , pp. 1282-1297
    • Griffis, E.R.1    Altan, N.2    Lippincott-Schwartz, J.3    Powers, M.A.4
  • 44
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition
    • Gustin, K. E., and P. Sarnow. 2001. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J. 20:240-249.
    • (2001) EMBO J , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 45
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg, E., R. W. Wozniak, and G. Blobel. 1993. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J. Cell Biol. 122:513-521.
    • (1993) J. Cell Biol , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 46
    • 0345374574 scopus 로고    scopus 로고
    • Importin beta negatively regulates nuclear membrane fusion and nuclear pore complex assembly
    • Harel, A., R. C. Chan, A. Lachish-Zalait, E. Zimmerman, M. Elbaum, and D. J. Forbes. 2003. Importin beta negatively regulates nuclear membrane fusion and nuclear pore complex assembly. Mol. Biol. Cell 14:4387-4396.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4387-4396
    • Harel, A.1    Chan, R.C.2    Lachish-Zalait, A.3    Zimmerman, E.4    Elbaum, M.5    Forbes, D.J.6
  • 47
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • Harel, A., and D. J. Forbes. 2004. Importin beta: conducting a much larger cellular symphony. Mol. Cell 16:319-330.
    • (2004) Mol. Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 48
    • 0033200239 scopus 로고    scopus 로고
    • Testis-specific murine centrin, Cetn1: Genomic characterization and evidence for retroposition of a gene encoding a centrosome protein
    • Hart, P. E., J. N. Glantz, J. D. Orth, G. M. Poynter, and J. L. Salisbury. 1999. Testis-specific murine centrin, Cetn1: genomic characterization and evidence for retroposition of a gene encoding a centrosome protein. Genomics 60:111-120.
    • (1999) Genomics , vol.60 , pp. 111-120
    • Hart, P.E.1    Glantz, J.N.2    Orth, J.D.3    Poynter, G.M.4    Salisbury, J.L.5
  • 50
    • 0029590122 scopus 로고
    • Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene
    • Heath, C. V., C. S. Copeland, D. C. Amberg, V. Del Priore, M. Snyder, and C. N. Cole. 1995. Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene. J. Cell Biol. 131:1677-1697.
    • (1995) J. Cell Biol , vol.131 , pp. 1677-1697
    • Heath, C.V.1    Copeland, C.S.2    Amberg, D.C.3    Del Priore, V.4    Snyder, M.5    Cole, C.N.6
  • 51
    • 3242891685 scopus 로고    scopus 로고
    • Transgenic mouse line with green-fluorescent protein-labeled centrin 2 allows visualization of the centrosome in living cells
    • Higginbotham, H., S. Bielas, T. Tanaka, and J. G. Gleeson. 2004. Transgenic mouse line with green-fluorescent protein-labeled centrin 2 allows visualization of the centrosome in living cells. Transgenic Res. 13:155-164.
    • (2004) Transgenic Res , vol.13 , pp. 155-164
    • Higginbotham, H.1    Bielas, S.2    Tanaka, T.3    Gleeson, J.G.4
  • 52
    • 33748657386 scopus 로고    scopus 로고
    • Nup214 is required for CRM1-dependent nuclear protein export in vivo
    • Hutten, S., and R. H. Kehlenbach. 2006. Nup214 is required for CRM1-dependent nuclear protein export in vivo. Mol. Cell. Biol. 26:6772-6785.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6772-6785
    • Hutten, S.1    Kehlenbach, R.H.2
  • 53
    • 0035101661 scopus 로고    scopus 로고
    • Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication
    • Ivanovska, I., and M. D. Rose. 2001. Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication. Genetics 157:503-518.
    • (2001) Genetics , vol.157 , pp. 503-518
    • Ivanovska, I.1    Rose, M.D.2
  • 54
    • 0036861279 scopus 로고    scopus 로고
    • A novel family of nuclear transport receptors mediates the export of messenger RNA to the cytoplasm
    • Izaurralde, E. 2002. A novel family of nuclear transport receptors mediates the export of messenger RNA to the cytoplasm. Eur. J. Cell Biol. 81:577-584.
    • (2002) Eur. J. Cell Biol , vol.81 , pp. 577-584
    • Izaurralde, E.1
  • 56
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph, J., S. T. Liu, S. A. Jablonski, T. J. Yen, and M. Dasso. 2004. The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr. Biol. 14:611-617.
    • (2004) Curr. Biol , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 57
    • 0345643313 scopus 로고    scopus 로고
    • The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human
    • Katahira, J., K. Strasser, A. Podtelejnikov, M. Mann, J. U. Jung, and E. Hurt. 1999. The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18:2593-2609.
    • (1999) EMBO J , vol.18 , pp. 2593-2609
    • Katahira, J.1    Strasser, K.2    Podtelejnikov, A.3    Mann, M.4    Jung, J.U.5    Hurt, E.6
  • 59
    • 0141864663 scopus 로고    scopus 로고
    • Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication
    • Kilmartin, J. V. 2003. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J. Cell Biol. 162:1211-1221.
    • (2003) J. Cell Biol , vol.162 , pp. 1211-1221
    • Kilmartin, J.V.1
  • 62
    • 0034054694 scopus 로고    scopus 로고
    • Differential expression and cellular distribution of centrin isoforms during human ciliated cell differentiation in vitro
    • Laoukili, J., E. Perret, S. Middendorp, O. Houcine, C. Guennou, F. Marano, M. Bornens, and F. Tournier. 2000. Differential expression and cellular distribution of centrin isoforms during human ciliated cell differentiation in vitro. J. Cell Sci. 113:1355-1364.
    • (2000) J. Cell Sci , vol.113 , pp. 1355-1364
    • Laoukili, J.1    Perret, E.2    Middendorp, S.3    Houcine, O.4    Guennou, C.5    Marano, F.6    Bornens, M.7    Tournier, F.8
  • 65
    • 0027367158 scopus 로고
    • Molecular cloning and centrosomal localization of human caltractin
    • Lee, V. D., and B. Huang. 1993. Molecular cloning and centrosomal localization of human caltractin. Proc. Natl. Acad. Sci. USA 90:11039-11043.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11039-11043
    • Lee, V.D.1    Huang, B.2
  • 66
    • 0036196670 scopus 로고    scopus 로고
    • Protein and RNA export from the nucleus
    • Lei, E. P., and P. A. Silver. 2002. Protein and RNA export from the nucleus. Dev. Cell 2:261-272.
    • (2002) Dev. Cell , vol.2 , pp. 261-272
    • Lei, E.P.1    Silver, P.A.2
  • 67
    • 0037342695 scopus 로고    scopus 로고
    • Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex
    • Lei, E. P., C. A. Stern, B. Fahrenkrog, H. Krebber, T. I. Moy, U. Aebi, and P. A. Silver. 2003. Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex. Mol. Biol. Cell 14:836-847.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 836-847
    • Lei, E.P.1    Stern, C.A.2    Fahrenkrog, B.3    Krebber, H.4    Moy, T.I.5    Aebi, U.6    Silver, P.A.7
  • 70
    • 0029040699 scopus 로고
    • Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes
    • Li, O., C. V. Heath, D. C. Amberg, T. C. Dockendorff, C. S. Copeland, M. Snyder, and C. N. Cole. 1995. Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes. Mol. Biol. Cell 6:401-417.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 401-417
    • Li, O.1    Heath, C.V.2    Amberg, D.C.3    Dockendorff, T.C.4    Copeland, C.S.5    Snyder, M.6    Cole, C.N.7
  • 71
    • 33745281934 scopus 로고    scopus 로고
    • Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication
    • Li, S., A. M. Sandercock, P. Conduit, C. V. Robinson, R. L. Williams, and J. V. Kilmartin. 2006. Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. J. Cell Biol. 173:867-877.
    • (2006) J. Cell Biol , vol.173 , pp. 867-877
    • Li, S.1    Sandercock, A.M.2    Conduit, P.3    Robinson, C.V.4    Williams, R.L.5    Kilmartin, J.V.6
  • 72
    • 33745220131 scopus 로고    scopus 로고
    • CENTRIN2 interacts with the Arabidopsis homolog of the human XPC protein (AtRAD4) and contributes to efficient synthesis-dependent repair of bulky DNA lesions
    • Liang, L., S. Flury, V. Kalck, B. Hohn, and J. Molinier. 2006. CENTRIN2 interacts with the Arabidopsis homolog of the human XPC protein (AtRAD4) and contributes to efficient synthesis-dependent repair of bulky DNA lesions. Plant Mol. Biol. 61:345-356.
    • (2006) Plant Mol. Biol , vol.61 , pp. 345-356
    • Liang, L.1    Flury, S.2    Kalck, V.3    Hohn, B.4    Molinier, J.5
  • 73
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka, M. J., and Y. Masui. 1983. Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220:719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 74
    • 17044457744 scopus 로고    scopus 로고
    • The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis
    • Loiodice, I., A. Alves, G. Rabut, M. Van Overbeek, J. Ellenberg, J. B. Sibarita, and V. Doye. 2004. The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol. Biol. Cell 15:3333-3344.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3333-3344
    • Loiodice, I.1    Alves, A.2    Rabut, G.3    Van Overbeek, M.4    Ellenberg, J.5    Sibarita, J.B.6    Doye, V.7
  • 75
    • 0032169412 scopus 로고    scopus 로고
    • Reconstitution of HIV-1 rev nuclear export: Independent requirements for nuclear import and export
    • Love, D. C., T. D. Sweitzer, and J. A. Hanover. 1998. Reconstitution of HIV-1 rev nuclear export: independent requirements for nuclear import and export. Proc. Natl. Acad. Sci. USA 95:10608-10613.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10608-10613
    • Love, D.C.1    Sweitzer, T.D.2    Hanover, J.A.3
  • 76
    • 0035827607 scopus 로고    scopus 로고
    • Phosphorylation of centrin during the cell cycle and its role in centriole separation preceding centrosome duplication
    • Lutz, W., W. L. Lingle, D. McCormick, T. M. Greenwood, and J. L. Salisbury. 2001. Phosphorylation of centrin during the cell cycle and its role in centriole separation preceding centrosome duplication. J. Biol. Chem. 276:20774-20780.
    • (2001) J. Biol. Chem , vol.276 , pp. 20774-20780
    • Lutz, W.1    Lingle, W.L.2    McCormick, D.3    Greenwood, T.M.4    Salisbury, J.L.5
  • 77
    • 0036469369 scopus 로고    scopus 로고
    • Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins
    • Lutzmann, M., R. Kunze, A. Buerer, U. Aebi, and E. Hurt. 2002. Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J. 21:387-397.
    • (2002) EMBO J , vol.21 , pp. 387-397
    • Lutzmann, M.1    Kunze, R.2    Buerer, A.3    Aebi, U.4    Hurt, E.5
  • 79
    • 0035833249 scopus 로고    scopus 로고
    • Nuclear pore complexes: Dynamics in unexpected places
    • Lyman, S. K., and L. Gerace. 2001. Nuclear pore complexes: dynamics in unexpected places. J. Cell Biol. 154:17-20.
    • (2001) J. Cell Biol , vol.154 , pp. 17-20
    • Lyman, S.K.1    Gerace, L.2
  • 80
    • 0030047960 scopus 로고    scopus 로고
    • Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA
    • Macaulay, C., and D. J. Forbes. 1996. Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA. J. Cell Biol. 132:5-20.
    • (1996) J. Cell Biol , vol.132 , pp. 5-20
    • Macaulay, C.1    Forbes, D.J.2
  • 84
    • 33748451717 scopus 로고    scopus 로고
    • Isolation and fractionation of rat liver nuclear envelopes and nuclear pore complexes
    • Matunis, M. J. 2006. Isolation and fractionation of rat liver nuclear envelopes and nuclear pore complexes. Methods 39:277-283.
    • (2006) Methods , vol.39 , pp. 277-283
    • Matunis, M.J.1
  • 85
    • 33645217661 scopus 로고    scopus 로고
    • The integral membrane protein Pom34p functionally links nucleoporin subcomplexes
    • Miao, M., K. J. Ryan, and S. R. Wente. 2006. The integral membrane protein Pom34p functionally links nucleoporin subcomplexes. Genetics 172:1441-1457.
    • (2006) Genetics , vol.172 , pp. 1441-1457
    • Miao, M.1    Ryan, K.J.2    Wente, S.R.3
  • 87
    • 0030790789 scopus 로고    scopus 로고
    • Identification of a new mammalian centrin gene, more closely related to Saccharomyces cerevisiae CDC31 gene
    • Middendorp, S., A. Paoletti, E. Schiebel, and M. Bornens. 1997. Identification of a new mammalian centrin gene, more closely related to Saccharomyces cerevisiae CDC31 gene. Proc. Natl. Acad. Sci. USA 94:9141-9146.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9141-9146
    • Middendorp, S.1    Paoletti, A.2    Schiebel, E.3    Bornens, M.4
  • 88
    • 0034569590 scopus 로고    scopus 로고
    • Purification of the vertebrate nuclear pore complex by biochemical criteria
    • Miller, B. R., and D. J. Forbes. 2000. Purification of the vertebrate nuclear pore complex by biochemical criteria. Traffic 1:941-951.
    • (2000) Traffic , vol.1 , pp. 941-951
    • Miller, B.R.1    Forbes, D.J.2
  • 89
    • 0033790322 scopus 로고    scopus 로고
    • Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay
    • Miller, B. R., M. Powers, M. Park, W. Fischer, and D. J. Forbes. 2000. Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay. Mol. Biol. Cell 11:3381-3396.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3381-3396
    • Miller, B.R.1    Powers, M.2    Park, M.3    Fischer, W.4    Forbes, D.J.5
  • 90
    • 2942657727 scopus 로고    scopus 로고
    • CENTRIN2 modulates homologous recombination and nucleotide excision repair in Arabidopsis
    • Molinier, J., C. Ramos, O. Fritsch, and B. Hohn. 2004. CENTRIN2 modulates homologous recombination and nucleotide excision repair in Arabidopsis. Plant Cell 16:1633-1643.
    • (2004) Plant Cell , vol.16 , pp. 1633-1643
    • Molinier, J.1    Ramos, C.2    Fritsch, O.3    Hohn, B.4
  • 91
    • 0033118942 scopus 로고    scopus 로고
    • Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain
    • Nakielny, S., S. Shaikh, B. Burke, and G. Dreyfuss. 1999. Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain. EMBO J. 18:1982-1995.
    • (1999) EMBO J , vol.18 , pp. 1982-1995
    • Nakielny, S.1    Shaikh, S.2    Burke, B.3    Dreyfuss, G.4
  • 92
    • 20744446570 scopus 로고    scopus 로고
    • Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein
    • Nishi, R., Y. Okuda, E. Watanabe, T. Mori, S. Iwai, C. Masutani, K. Sugasawa, and F. Hanaoka. 2005. Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein. Mol. Cell. Biol. 25:5664-5674.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 5664-5674
    • Nishi, R.1    Okuda, Y.2    Watanabe, E.3    Mori, T.4    Iwai, S.5    Masutani, C.6    Sugasawa, K.7    Hanaoka, F.8
  • 94
    • 0030447537 scopus 로고    scopus 로고
    • Most of centrin in animal cells is not centrosome-associated and centrosomal centrin is confined to the distal lumen of centrioles
    • Paoletti, A., M. Moudjou, M. Paintrand, J. L. Salisbury, and M. Bornens. 1996. Most of centrin in animal cells is not centrosome-associated and centrosomal centrin is confined to the distal lumen of centrioles. J. Cell Sci. 109:3089-3102.
    • (1996) J. Cell Sci , vol.109 , pp. 3089-3102
    • Paoletti, A.1    Moudjou, M.2    Paintrand, M.3    Salisbury, J.L.4    Bornens, M.5
  • 95
    • 33748783074 scopus 로고    scopus 로고
    • Changes in nucleoporin domain topology in response to chemical effectors
    • Paulillo, S. M., M. A. Powers, K. S. Ullman, and B. Fahrenkrog. 2006. Changes in nucleoporin domain topology in response to chemical effectors. J. Mol. Biol. 363:39-50.
    • (2006) J. Mol. Biol , vol.363 , pp. 39-50
    • Paulillo, S.M.1    Powers, M.A.2    Ullman, K.S.3    Fahrenkrog, B.4
  • 96
    • 0028855758 scopus 로고
    • Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexes
    • Pemberton, L. F., M. P. Rout, and G. Blobel. 1995. Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexes. Proc. Natl. Acad. Sci. USA 92:1187-1191.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1187-1191
    • Pemberton, L.F.1    Rout, M.P.2    Blobel, G.3
  • 97
    • 0141924869 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin
    • Popescu, A., S. Miron, Y. Blouquit, P. Duchambon, P. Christova, and C. T. Craescu. 2003. Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin. J. Biol. Chem. 278:40252-40261.
    • (2003) J. Biol. Chem , vol.278 , pp. 40252-40261
    • Popescu, A.1    Miron, S.2    Blouquit, Y.3    Duchambon, P.4    Christova, P.5    Craescu, C.T.6
  • 98
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways
    • Powers, M. A., D. J. Forbes, J. E. Dahlberg, and E. Lund. 1997. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J. Cell Biol. 136:241-250.
    • (1997) J. Cell Biol , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 99
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers, M. A., C. Macaulay, F. R. Masiarz, and D. J. Forbes. 1995. Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication. J. Cell Biol. 128:721-736.
    • (1995) J. Cell Biol , vol.128 , pp. 721-736
    • Powers, M.A.1    Macaulay, C.2    Masiarz, F.R.3    Forbes, D.J.4
  • 100
    • 0028338928 scopus 로고
    • Nup107 is a novel nuclear pore complex protein that contains a leucine zipper
    • Radu, A., G. Blobel, and R. W. Wozniak. 1994. Nup107 is a novel nuclear pore complex protein that contains a leucine zipper. J. Biol. Chem. 269:17600-17605.
    • (1994) J. Biol. Chem , vol.269 , pp. 17600-17605
    • Radu, A.1    Blobel, G.2    Wozniak, R.W.3
  • 101
    • 33845227470 scopus 로고    scopus 로고
    • ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division
    • Rasala, B. A., A. V. Orjalo, Z. Shen, S. Briggs, and D. J. Forbes. 2006. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc. Natl. Acad. Sci. USA 103:17801-17806.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17801-17806
    • Rasala, B.A.1    Orjalo, A.V.2    Shen, Z.3    Briggs, S.4    Forbes, D.J.5
  • 102
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt, R., A. Holzenburg, E. L. Buhle, Jr., M. Jarnik, A. Engel, and U. Aebi. 1990. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110:883-894.
    • (1990) J. Cell Biol , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle Jr., E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 103
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., J. D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B. T. Chait. 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635-651.
    • (2000) J. Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 104
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kinetochore assembly
    • Salina, D., P. Enarson, J. B. Rattner, and B. Burke. 2003. Nup358 integrates nuclear envelope breakdown with kinetochore assembly. J. Cell Biol. 162:991-1001.
    • (2003) J. Cell Biol , vol.162 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 105
    • 0028928790 scopus 로고
    • Centrin, centrosomes, and mitotic spindle poles
    • Salisbury, J. L. 1995. Centrin, centrosomes, and mitotic spindle poles. Curr. Opin. Cell Biol. 7:39-45.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 39-45
    • Salisbury, J.L.1
  • 106
    • 0348226550 scopus 로고    scopus 로고
    • Centrosomes: Sfi1p and centrin unravel a structural riddle
    • Salisbury, J. L. 2004. Centrosomes: Sfi1p and centrin unravel a structural riddle. Curr. Biol. 14:R27-R29.
    • (2004) Curr. Biol , vol.14
    • Salisbury, J.L.1
  • 107
    • 0021132972 scopus 로고
    • Striated flagellar roots: Isolation and partial characterization of a calcium-modulated contractile organelle
    • Salisbury, J. L., A. Baron, B. Surek, and M. Melkonian. 1984. Striated flagellar roots: isolation and partial characterization of a calcium-modulated contractile organelle. J. Cell Biol. 99:962-970.
    • (1984) J. Cell Biol , vol.99 , pp. 962-970
    • Salisbury, J.L.1    Baron, A.2    Surek, B.3    Melkonian, M.4
  • 108
    • 0037031146 scopus 로고    scopus 로고
    • Centrin-2 is required for centriole duplication in mammalian cells
    • Salisbury, J. L., K. M. Suino, R. Busby, and M. Springett. 2002. Centrin-2 is required for centriole duplication in mammalian cells. Curr. Biol. 12:1287-1292.
    • (2002) Curr. Biol , vol.12 , pp. 1287-1292
    • Salisbury, J.L.1    Suino, K.M.2    Busby, R.3    Springett, M.4
  • 109
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • Segura-Totten, M., A. K. Kowalski, R. Craigie, and K. L. Wilson. 2002. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J. Cell Biol. 158:475-485.
    • (2002) J. Cell Biol , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 111
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou, S., C. Wimmer, M. Rieger, V. Doye, H. Tekotte, C. Weise, S. Emig, A. Segref, and E. C. Hurt. 1996. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84:265-275.
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 112
    • 28644434170 scopus 로고    scopus 로고
    • Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export
    • Soop, T., B. Ivarsson, B. Bjorkroth, N. Fomproix, S. Masich, V. C. Cordes, and B. Daneholt. 2005. Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export. Mol. Biol. Cell 16:5610-5620.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5610-5620
    • Soop, T.1    Ivarsson, B.2    Bjorkroth, B.3    Fomproix, N.4    Masich, S.5    Cordes, V.C.6    Daneholt, B.7
  • 113
    • 0027366227 scopus 로고
    • The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body
    • Spang, A., I. Courtney, U. Fackler, M. Matzner, and E. Schiebel. 1993. The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body. J. Cell Biol. 123:405-416.
    • (1993) J. Cell Biol , vol.123 , pp. 405-416
    • Spang, A.1    Courtney, I.2    Fackler, U.3    Matzner, M.4    Schiebel, E.5
  • 114
    • 33646804467 scopus 로고    scopus 로고
    • NDC1: A crucial membrane-integral nucleoporin of metazoan nuclear pore complexes
    • Stavru, F., B. B. Hulsmann, A. Spang, E. Hartmann, V. C. Cordes, and D. Gorlich. 2006. NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes. J. Cell Biol. 173:509-519.
    • (2006) J. Cell Biol , vol.173 , pp. 509-519
    • Stavru, F.1    Hulsmann, B.B.2    Spang, A.3    Hartmann, E.4    Cordes, V.C.5    Gorlich, D.6
  • 116
    • 0033537992 scopus 로고    scopus 로고
    • Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy
    • Stoffler, D., K. N. Goldie, B. Feja, and U. Aebi. 1999. Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J. Mol. Biol. 287:741-752.
    • (1999) J. Mol. Biol , vol.287 , pp. 741-752
    • Stoffler, D.1    Goldie, K.N.2    Feja, B.3    Aebi, U.4
  • 117
    • 0034698683 scopus 로고    scopus 로고
    • Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export
    • Strasser, K., J. Bassler, and E. Hurt. 2000. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol. 150:695-706.
    • (2000) J. Cell Biol , vol.150 , pp. 695-706
    • Strasser, K.1    Bassler, J.2    Hurt, E.3
  • 118
    • 0035794237 scopus 로고    scopus 로고
    • The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex
    • Strawn, L. A., T. Shen, and S. R. Wente. 2001. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J. Biol. Chem. 276:6445-6452.
    • (2001) J. Biol. Chem , vol.276 , pp. 6445-6452
    • Strawn, L.A.1    Shen, T.2    Wente, S.R.3
  • 120
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam, M., and S. R. Wente. 2003. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 4:775-789.
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 121
    • 0037044723 scopus 로고    scopus 로고
    • The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA replication via interaction with MCM3
    • Takei, Y., M. Assenberg, G. Tsujimoto, and R. Laskey. 2002. The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA replication via interaction with MCM3. J. Biol. Chem. 277:43121-43125.
    • (2002) J. Biol. Chem , vol.277 , pp. 43121-43125
    • Takei, Y.1    Assenberg, M.2    Tsujimoto, G.3    Laskey, R.4
  • 122
  • 123
    • 0032575659 scopus 로고    scopus 로고
    • Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization
    • Takei, Y., and G. Tsujimoto. 1998. Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization. J. Biol. Chem. 273:22177-22180.
    • (1998) J. Biol. Chem , vol.273 , pp. 22177-22180
    • Takei, Y.1    Tsujimoto, G.2
  • 124
    • 33745868296 scopus 로고    scopus 로고
    • The structure of the human centrin 2-xeroderma pigmentosum group C protein complex
    • Thompson, J. R., Z. C. Ryan, J. L. Salisbury, and R. Kumar. 2006. The structure of the human centrin 2-xeroderma pigmentosum group C protein complex. J. Biol. Chem. 281:18746-18752.
    • (2006) J. Biol. Chem , vol.281 , pp. 18746-18752
    • Thompson, J.R.1    Ryan, Z.C.2    Salisbury, J.L.3    Kumar, R.4
  • 125
    • 33846993756 scopus 로고    scopus 로고
    • Role of Ca2+ activation and bilobal structure of calmodulin in nuclear and nucleolar localization
    • Thorogate, R., and K. Torok. 2007. Role of Ca2+ activation and bilobal structure of calmodulin in nuclear and nucleolar localization. Biochem. J. 402:71-80.
    • (2007) Biochem. J , vol.402 , pp. 71-80
    • Thorogate, R.1    Torok, K.2
  • 127
    • 0032963082 scopus 로고    scopus 로고
    • The nucleoporin nup153 plays a critical role in multiple types of nuclear export
    • Ullman, K. S., S. Shah, M. A. Powers, and D. J. Forbes. 1999. The nucleoporin nup153 plays a critical role in multiple types of nuclear export. Mol. Biol. Cell 10:649-664.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 649-664
    • Ullman, K.S.1    Shah, S.2    Powers, M.A.3    Forbes, D.J.4
  • 128
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • Vasu, S., S. Shah, A. Orjalo, M. Park, W. H. Fischer, and D. J. Forbes. 2001. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J. Cell Biol. 155:339-354.
    • (2001) J. Cell Biol , vol.155 , pp. 339-354
    • Vasu, S.1    Shah, S.2    Orjalo, A.3    Park, M.4    Fischer, W.H.5    Forbes, D.J.6
  • 129
    • 0035370938 scopus 로고    scopus 로고
    • Nuclear pores and nuclear assembly
    • Vasu, S. K., and D. J. Forbes. 2001. Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13:363-375.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 363-375
    • Vasu, S.K.1    Forbes, D.J.2
  • 130
    • 2342523175 scopus 로고    scopus 로고
    • mRNA export: An assembly line from genes to nuclear pores
    • Vinciguerra, P., and F. Stutz. 2004. mRNA export: an assembly line from genes to nuclear pores. Curr. Opin. Cell Biol. 16:285-292.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 285-292
    • Vinciguerra, P.1    Stutz, F.2
  • 133
    • 0035887310 scopus 로고    scopus 로고
    • The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins
    • Walther, T. C., M. Fornerod, H. Pickersgill, M. Goldberg, T. D. Allen, and I. W. Mattaj. 2001. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. EMBO J. 20:5703-5714.
    • (2001) EMBO J , vol.20 , pp. 5703-5714
    • Walther, T.C.1    Fornerod, M.2    Pickersgill, H.3    Goldberg, M.4    Allen, T.D.5    Mattaj, I.W.6
  • 134
    • 0036591883 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Cargo trafficking across the border
    • Weis, K. 2002. Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14:328-335.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 328-335
    • Weis, K.1
  • 135
    • 0034214267 scopus 로고    scopus 로고
    • GFP-centrin as a marker for centriole dynamics in living cells
    • White, R. A., Z. Pan, and J. L. Salisbury. 2000. GFP-centrin as a marker for centriole dynamics in living cells. Microsc. Res. Tech. 49:451-457.
    • (2000) Microsc. Res. Tech , vol.49 , pp. 451-457
    • White, R.A.1    Pan, Z.2    Salisbury, J.L.3
  • 136
    • 33751160346 scopus 로고    scopus 로고
    • Microtubule nucleation: Gamma-tubulin and beyond
    • Wiese, C., and Y. Zheng. 2006. Microtubule nucleation: gamma-tubulin and beyond. J. Cell Sci. 119:4143-4153.
    • (2006) J. Cell Sci , vol.119 , pp. 4143-4153
    • Wiese, C.1    Zheng, Y.2
  • 137
    • 12444252559 scopus 로고    scopus 로고
    • Centrins, a novel group of Ca2+-binding proteins in vertebrate photoreceptor cells
    • Wolfrum, U., A. Giessl, and A. Pulvermuller. 2002. Centrins, a novel group of Ca2+-binding proteins in vertebrate photoreceptor cells. Adv. Exp. Med. Biol. 514:155-178.
    • (2002) Adv. Exp. Med. Biol , vol.514 , pp. 155-178
    • Wolfrum, U.1    Giessl, A.2    Pulvermuller, A.3
  • 138
    • 0031817982 scopus 로고    scopus 로고
    • Expression of centrin isoforms in the mammalian retina
    • Wolfrum, U., and J. L. Salisbury. 1998. Expression of centrin isoforms in the mammalian retina. Exp. Cell Res. 242:10-17.
    • (1998) Exp. Cell Res , vol.242 , pp. 10-17
    • Wolfrum, U.1    Salisbury, J.L.2
  • 139
    • 31044436187 scopus 로고    scopus 로고
    • The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly
    • Yang, A., S. Miron, P. Duchambon, L. Assairi, Y. Blouquit, and C. T. Craescu. 2006. The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly. Biochemistry 45:880-889.
    • (2006) Biochemistry , vol.45 , pp. 880-889
    • Yang, A.1    Miron, S.2    Duchambon, P.3    Assairi, L.4    Blouquit, Y.5    Craescu, C.T.6
  • 140
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang, Q., M. P. Rout, and C. W. Akey. 1998. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1:223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 141
    • 1842835691 scopus 로고    scopus 로고
    • Concentration of Ran on chromatin induces decondensation, nuclear envelope formation and nuclear pore complex assembly
    • Zhang, C., M. W. Goldberg, W. J. Moore, T. D. Allen, and P. R. Clarke. 2002. Concentration of Ran on chromatin induces decondensation, nuclear envelope formation and nuclear pore complex assembly. Eur. J. Cell Biol. 81:623-633.
    • (2002) Eur. J. Cell Biol , vol.81 , pp. 623-633
    • Zhang, C.1    Goldberg, M.W.2    Moore, W.J.3    Allen, T.D.4    Clarke, P.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.