메뉴 건너뛰기




Volumn 16, Issue 10, 2005, Pages 4660-4671

Cross-talk between snurportin1 subdomains

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEIN; GUANOSINE DERIVATIVE; KARYOPHERIN ALPHA; KARYOPHERIN BETA; LEPTOMYCIN B; SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; SNURPORTIN 1; TRIMETHYLGUANOSINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 26244433138     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-04-0316     Document Type: Article
Times cited : (28)

References (61)
  • 1
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope
    • Adam, E.J., and Adam, S. A. (1994). Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555.
    • (1994) J. Cell Biol. , vol.125 , pp. 547-555
    • Adam, E.J.1    Adam, S.A.2
  • 2
    • 0026042170 scopus 로고
    • Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import
    • Adam, S. A., and Gerace, L. (1991). Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import. Cell 66, 837-847.
    • (1991) Cell , vol.66 , pp. 837-847
    • Adam, S.A.1    Gerace, L.2
  • 3
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam, S. A., Marr, R. S., and Gerace, L. (1990). Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111, 807-816.
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 5
    • 0032509524 scopus 로고    scopus 로고
    • The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP
    • Askjaer, P., Jensen, T. H., Nilsson, J., Englmeier, L., and Kjems, J. (1998). The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J. Biol. Chem. 273, 33414-33422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33414-33422
    • Askjaer, P.1    Jensen, T.H.2    Nilsson, J.3    Englmeier, L.4    Kjems, J.5
  • 6
    • 0041731883 scopus 로고    scopus 로고
    • Importin-β contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • Bednenko, J., Cingolani, G., and Gerace, L. (2003). Importin-β contains a COOH-terminal nucleoporin binding region important for nuclear transport. J. Cell Biol. 162, 391-401.
    • (2003) J. Cell Biol. , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 8
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importing bound to the IBB domain of importin-α
    • Cingolani, G., Petosa, C., Weis, K., and Muller, C. W. (1999). Structure of importing bound to the IBB domain of importin-α. Nature 399, 221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 9
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
    • Conti, E., Uy, M., Leighton, L., Blobel, G., and Kuriyan, J. (1998). Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 94, 193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 10
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G., Kim, V. N., and Kataoka, N. (2002). Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3, 195-205.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 11
    • 18144398494 scopus 로고    scopus 로고
    • Recognition of mRNA cap structures by viral and cellular proteins
    • Fechter, P., and Brownlee, G. G. (2005). Recognition of mRNA cap structures by viral and cellular proteins. J. Gen. Virol. 86, 1239-1249.
    • (2005) J. Gen. Virol. , vol.86 , pp. 1239-1249
    • Fechter, P.1    Brownlee, G.G.2
  • 12
    • 0027396947 scopus 로고
    • Nucleo-cytoplasmic transport of U snRNPs: Definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap
    • Fischer, U., Sumpter, V., Sekine, M., Satoh, T., and Lührmann, R. (1993). Nucleo-cytoplasmic transport of U snRNPs: definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap. EMBO J. 12, 573-583.
    • (1993) EMBO J. , vol.12 , pp. 573-583
    • Fischer, U.1    Sumpter, V.2    Sekine, M.3    Satoh, T.4    Lührmann, R.5
  • 13
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M., and Mattaj, I. W. (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
  • 14
    • 0029064131 scopus 로고
    • Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase cells
    • Frey, M. R., and Matera, A. G. (1995). Coiled Bodies Contain U7 Small Nuclear RNA and Associate with Specific DNA Sequences in Interphase Cells. Proc. Natl. Acad. Sci. USA 92, 5915-5919.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5915-5919
    • Frey, M.R.1    Matera, A.G.2
  • 15
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried, H., and Kutay, U. (2003). Nucleocytoplasmic transport: taking an inventory. Cell Mol. Life Sci. 60, 1659-1688.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 16
    • 0029921174 scopus 로고    scopus 로고
    • A 41 amino acid motif in importin-α confers binding to importin-beta and hence transit into the nucleus
    • Görlich, D., Henklein, P., Laskey, R. A., and Hartmann, E. (1996). A 41 amino acid motif in importin-α confers binding to importin-beta and hence transit into the nucleus. EMBO J. 15, 1810-1817.
    • (1996) EMBO J. , vol.15 , pp. 1810-1817
    • Görlich, D.1    Henklein, P.2    Laskey, R.A.3    Hartmann, E.4
  • 17
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich, D., and Mattaj, I. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.2
  • 18
    • 8644262258 scopus 로고    scopus 로고
    • Importin β: Conducting a much larger cellular symphony
    • Harel, A., and Forbes, D. J. (2004). Importin β: 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
  • 19
    • 0038691610 scopus 로고    scopus 로고
    • Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha
    • Harreman, M. T., Cohen, P. E., Hodel, M. R., Truscott, G. J., Corbett, A. H., and Hodel, A. E. (2003a). Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha. J. Biol. Chem. 278, 21361-21369.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21361-21369
    • Harreman, M.T.1    Cohen, P.E.2    Hodel, M.R.3    Truscott, G.J.4    Corbett, A.H.5    Hodel, A.E.6
  • 20
    • 0037458580 scopus 로고    scopus 로고
    • The auto-inhibitory function of importin alpha is essential in vivo
    • Harreman, M. T., Hodel, M. R., Fanara, P., Hodel, A. E., and Corbett, A. H. (2003b). The auto-inhibitory function of importin alpha is essential in vivo. J. Biol. Chem. 278, 5854-5863.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5854-5863
    • Harreman, M.T.1    Hodel, M.R.2    Fanara, P.3    Hodel, A.E.4    Corbett, A.H.5
  • 21
    • 0033593805 scopus 로고    scopus 로고
    • A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells
    • Hieda, M., Tachibana, T., Yokoya, F., Kose, S., Imamoto, N., and Yoneda, Y. (1999). A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells. J. Cell Biol. 144, 645-655.
    • (1999) J. Cell Biol. , vol.144 , pp. 645-655
    • Hieda, M.1    Tachibana, T.2    Yokoya, F.3    Kose, S.4    Imamoto, N.5    Yoneda, Y.6
  • 22
    • 0032527283 scopus 로고    scopus 로고
    • Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure
    • Huber, J., Cronshagen, U., Kadokura, M., Marshallsay, C., Wada, T., Sekine, M., and Lührmann, R. (1998). Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. EMBO J. 17, 4114-4126.
    • (1998) EMBO J. , vol.17 , pp. 4114-4126
    • Huber, J.1    Cronshagen, U.2    Kadokura, M.3    Marshallsay, C.4    Wada, T.5    Sekine, M.6    Lührmann, R.7
  • 23
    • 0037017403 scopus 로고    scopus 로고
    • The importin-β binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro
    • Huber, J., Dickmanns, A., and Lührmann, R. (2002). The importin-β binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro. J. Cell Biol. 156, 467-479.
    • (2002) J. Cell Biol. , vol.156 , pp. 467-479
    • Huber, J.1    Dickmanns, A.2    Lührmann, R.3
  • 24
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde, E., Kutay, U., von Kobbe, C., Mattaj, I. W., and Gorlich, D. (1997). The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 16, 6535-6547.
    • (1997) EMBO J. , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, I.W.4    Gorlich, D.5
  • 25
    • 0028205891 scopus 로고
    • Nuclear export of different classes of RNA is mediated by specific factors
    • Jarmolowski, A., Boelens, W. C., Izaurralde, E., and Mattaj, I. W. (1994). Nuclear export of different classes of RNA is mediated by specific factors. J. Cell Biol. 124, 627-635.
    • (1994) J. Cell Biol. , vol.124 , pp. 627-635
    • Jarmolowski, A.1    Boelens, W.C.2    Izaurralde, E.3    Mattaj, I.W.4
  • 26
    • 12344275917 scopus 로고    scopus 로고
    • Biogenesis of small nuclear RNPs
    • Kiss, T. (2004). Biogenesis of small nuclear RNPs. J. Cell Sci. 117, 5949-5951.
    • (2004) J. Cell Sci. , vol.117 , pp. 5949-5951
    • Kiss, T.1
  • 27
    • 0027443340 scopus 로고
    • Functional expression in Escherichia coli of the mitotic regulator proteins p24ran and p45rcc1 and fluorescence measurements of their interaction
    • Klebe, C., Nishimoto, T., and Wittinghofer, F. (1993). Functional expression in Escherichia coli of the mitotic regulator proteins p24ran and p45rcc1 and fluorescence measurements of their interaction. Biochemistry 32, 11923-11928.
    • (1993) Biochemistry , vol.32 , pp. 11923-11928
    • Klebe, C.1    Nishimoto, T.2    Wittinghofer, F.3
  • 28
    • 0032950628 scopus 로고    scopus 로고
    • Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α
    • Kobe, B. (1999). Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α. Nat. Struct. Biol. 6, 388-397.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 388-397
    • Kobe, B.1
  • 30
    • 0027958413 scopus 로고
    • In vitro nuclear import of snRNPs: Cytosolic factors mediate m3G-cap dependence of U1 and U2 snRNP transport
    • Marshallsay, C., and Lührmann, R. (1994). In vitro nuclear import of snRNPs: cytosolic factors mediate m3G-cap dependence of U1 and U2 snRNP transport. EMBO J. 13, 222-231.
    • (1994) EMBO J. , vol.13 , pp. 222-231
    • Marshallsay, C.1    Lührmann, R.2
  • 32
    • 0036809734 scopus 로고    scopus 로고
    • SMN-mediated assembly of RNPs: A complex story
    • Meister, G., Eggert, C., and Fischer, U. (2002). SMN-mediated assembly of RNPs: a complex story. Trends Cell Biol. 12, 472-478.
    • (2002) Trends Cell Biol. , vol.12 , pp. 472-478
    • Meister, G.1    Eggert, C.2    Fischer, U.3
  • 33
    • 0028962511 scopus 로고
    • Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes
    • Moroianu, J., Blobel, G., and Radu, A. (1995). Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. Proc. Natl. Acad. Sci. USA 92, 2008-2011.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 34
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast, N., and Pemberton, L. F. (2004). Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14, 547-556.
    • (2004) Trends Cell Biol. , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 35
    • 0344012478 scopus 로고    scopus 로고
    • Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase
    • Mouaikel, J., Bujnicki, J. M., Tazi, J., and Bordonne, R. (2003). Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase. Nucleic Acids Res. 31, 4899-4909.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4899-4909
    • Mouaikel, J.1    Bujnicki, J.M.2    Tazi, J.3    Bordonne, R.4
  • 36
    • 0036238278 scopus 로고    scopus 로고
    • Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus
    • Mouaikel, J., Verheggen, C., Bertrand, E., Tazi, J., and Bordonne, R. (2002). Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Mol. Cell 9, 891-901.
    • (2002) Mol. Cell , vol.9 , pp. 891-901
    • Mouaikel, J.1    Verheggen, C.2    Bertrand, E.3    Tazi, J.4    Bordonne, R.5
  • 37
    • 6344258807 scopus 로고    scopus 로고
    • Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein
    • Narayanan, U., Achsel, T., Lührmann, R., and Matera, A. G. (2004). Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein. Mol. Cell 16, 223-234.
    • (2004) Mol. Cell , vol.16 , pp. 223-234
    • Narayanan, U.1    Achsel, T.2    Lührmann, R.3    Matera, A.G.4
  • 38
    • 0037098960 scopus 로고    scopus 로고
    • SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin β
    • Narayanan, U., Ospina, J. K., Frey, M. R., Hebert, M. D., and Matera, A. G. (2002). SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin β. Hum. Mol. Genet. 11, 1785-1795.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1785-1795
    • Narayanan, U.1    Ospina, J.K.2    Frey, M.R.3    Hebert, M.D.4    Matera, A.G.5
  • 39
    • 5444231229 scopus 로고    scopus 로고
    • A role for Cajal bodies in the final steps of U2 snRNP biogenesis
    • Nesic, D., Tanackovic, G., and Krämer, A. (2004). A role for Cajal bodies in the final steps of U2 snRNP biogenesis. J. Cell Sci. 117, 4423-4433.
    • (2004) J. Cell Sci. , vol.117 , pp. 4423-4433
    • Nesic, D.1    Tanackovic, G.2    Krämer, A.3
  • 40
    • 0035847054 scopus 로고    scopus 로고
    • A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin β, CRM1 and RanBP1
    • Nilsson, J., Askjaer, P., and Kjems, J. (2001). A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin β, CRM1 and RanBP1. J. Mol. Biol. 305, 231-243.
    • (2001) J. Mol. Biol. , vol.305 , pp. 231-243
    • Nilsson, J.1    Askjaer, P.2    Kjems, J.3
  • 41
    • 0034646512 scopus 로고    scopus 로고
    • PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
    • Ohno, M., Segref, A., Bachi, A., Wilm, M., and Mattaj, I. W. (2000). PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation. Cell 202, 187-198.
    • (2000) Cell , vol.202 , pp. 187-198
    • Ohno, M.1    Segref, A.2    Bachi, A.3    Wilm, M.4    Mattaj, I.W.5
  • 42
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., Bachelerie, F., and Dargemont, C. (1997). Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278, 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 43
    • 0030775693 scopus 로고    scopus 로고
    • Nuclear import of U snRNPs requires importin β
    • Palacios, I., Hetzer, M., Adam, S. A., and Mattaj, I. W. (1997). Nuclear import of U snRNPs requires importin β. EMBO J. 16, 6783-6792.
    • (1997) EMBO J. , vol.16 , pp. 6783-6792
    • Palacios, I.1    Hetzer, M.2    Adam, S.A.3    Mattaj, I.W.4
  • 44
    • 10644245871 scopus 로고    scopus 로고
    • Nuclear pore complex structure: Unplugged and dynamic pores
    • Pante, N. (2004). Nuclear pore complex structure: unplugged and dynamic pores. Dev. Cell 7, 780-781.
    • (2004) Dev. Cell , vol.7 , pp. 780-781
    • Pante, N.1
  • 46
    • 2242443509 scopus 로고    scopus 로고
    • Essential role for the SMN complex in the specificity of snRNP assembly
    • Pellizzoni, L., Yong, J., and Dreyfuss, G. (2002). Essential role for the SMN complex in the specificity of snRNP assembly. Science 298, 1775-1779.
    • (2002) Science , vol.298 , pp. 1775-1779
    • Pellizzoni, L.1    Yong, J.2    Dreyfuss, G.3
  • 48
    • 0033975417 scopus 로고    scopus 로고
    • Structural basis of mRNA cap recognition by proteins
    • Quiocho, F. A., Hu, G., and Gershon, P. D. (2000). Structural basis of mRNA cap recognition by proteins. Curr. Opin. Struct. Biol. 10, 78-86.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 78-86
    • Quiocho, F.A.1    Hu, G.2    Gershon, P.D.3
  • 49
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout, M. P., and Aitchison, J. D. (2001). The nuclear pore complex as a transport machine. J. Biol. Chem. 276, 16593-16596.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 50
    • 0029124901 scopus 로고
    • In vitro reconstitution of mammalian U2 and U5 snRNPs active in splicing: Sm proteins are functionally interchangeable and are essential for the formation of functional U2 and U5 snRNPs
    • Segault, V., Will, C. L., Sproat, B. S., and Lührmann, R. (1995). In vitro reconstitution of mammalian U2 and U5 snRNPs active in splicing: Sm proteins are functionally interchangeable and are essential for the formation of functional U2 and U5 snRNPs. EMBO J. 14, 4010-4021.
    • (1995) EMBO J. , vol.14 , pp. 4010-4021
    • Segault, V.1    Will, C.L.2    Sproat, B.S.3    Lührmann, R.4
  • 51
    • 0033533730 scopus 로고    scopus 로고
    • Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway
    • Sleeman, J. E., and Lamond, A. I. (1999). Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway. Curr. Biol. 9, 1065-1074.
    • (1999) Curr. Biol. , vol.9 , pp. 1065-1074
    • Sleeman, J.E.1    Lamond, A.I.2
  • 52
    • 22744441209 scopus 로고    scopus 로고
    • Structural basis for m(3)G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1
    • Strasser, A., Dickmanns, A., Lührmann, R., and Ficner, R. (2005). Structural basis for m(3)G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1. EMBO J. 24, 2235-2243.
    • (2005) EMBO J. , vol.24 , pp. 2235-2243
    • Strasser, A.1    Dickmanns, A.2    Lührmann, R.3    Ficner, R.4
  • 54
    • 0026919628 scopus 로고
    • In vitro reconstitution of U1 and U2 snRNPs from isolated proteins and snRNA
    • Sumpter, V., Kahrs, A., Fischer, U., Kornstadt, U., and Lührmann, R. (1992). In vitro reconstitution of U1 and U2 snRNPs from isolated proteins and snRNA. Mol. Biol. Rep. 16, 229-240.
    • (1992) Mol. Biol. Rep. , vol.16 , pp. 229-240
    • Sumpter, V.1    Kahrs, A.2    Fischer, U.3    Kornstadt, U.4    Lührmann, R.5
  • 55
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam, M., and Wente, S. R. (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
  • 56
    • 14844312915 scopus 로고    scopus 로고
    • Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo
    • Tanackovic, G., and Krämer, A. (2005). Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo. Mol. Biol. Cell 26, 1366-1377.
    • (2005) Mol. Biol. Cell , vol.26 , pp. 1366-1377
    • Tanackovic, G.1    Krämer, A.2
  • 58
    • 0028988731 scopus 로고
    • Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences
    • Weis, K., Mattaj, I., and Lamond, A. (1995). Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science 268, 1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.2    Lamond, A.3
  • 59
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • Will, C. L., and Lührmann, R. (2001). Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell Biol. 13, 290-301.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 290-301
    • Will, C.L.1    Lührmann, R.2
  • 60
    • 0037119975 scopus 로고    scopus 로고
    • Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein
    • Will, C. L., Urlaub, H., Achsel, T., Gentzel, M., Wilm, M., and Lührmann, R. (2002). Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 21, 4978-4988.
    • (2002) EMBO J. , vol.21 , pp. 4978-4988
    • Will, C.L.1    Urlaub, H.2    Achsel, T.3    Gentzel, M.4    Wilm, M.5    Lührmann, R.6
  • 61
    • 1642406961 scopus 로고    scopus 로고
    • snRNAs contain specific SMN-binding domains that are essential for snRNP assembly
    • Yong, J., Golembe, T. J., Battle, D. J., Pellizzoni, L., and Dreyfuss, G. (2004). snRNAs contain specific SMN-binding domains that are essential for snRNP assembly. Mol. Cell Biol. 24, 2747-2756.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 2747-2756
    • Yong, J.1    Golembe, T.J.2    Battle, D.J.3    Pellizzoni, L.4    Dreyfuss, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.