메뉴 건너뛰기




Volumn 40, Issue 14, 2012, Pages 6850-6862

The transition in spliceosome assembly from complex e to complex A purges surplus U1 snRNPs from alternative splice sites

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN U1; UNCLASSIFIED DRUG;

EID: 84864940859     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks322     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan, Q., Shai, O., Lee, L.J., Frey, B.J. and Blencowe, B.J. (2008) Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat. Genet., 40, 1413-1415.
    • (2008) Nat. Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 4
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • DOI 10.1038/nsmb1135, PII NSMB1135
    • Listerman, I., Sapra, A.K. and Neugebauer, K.M. (2006) Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat. Struct. Mol. Biol., 13, 815-822. (Pubitemid 44338776)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.9 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 5
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • DOI 10.1016/S0955-0674(00)00211-8
    • Will, C.L. and Luhrmann, R. (2001) Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell. Biol., 13, 290-301. (Pubitemid 32429493)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 7
    • 0032708815 scopus 로고    scopus 로고
    • Resolution of the mammalian E complex and the ATP-dependent spliceosomal complexes on native agarose mini-gels
    • DOI 10.1017/S1355838299991501
    • Das, R. and Reed, R. (1999) Resolution of the mammalian E complex and the ATP-dependent spliceosomal complexes on native agarose mini-gels. RNA, 5, 1504-1508. (Pubitemid 29530495)
    • (1999) RNA , vol.5 , Issue.11 , pp. 1504-1508
    • Das, R.1    Reed, R.2
  • 8
    • 0022549635 scopus 로고
    • Electrophoretic separation of complexes involved in the splicing of precursors to mRNAs
    • Konarska, M.M. and Sharp, P.A. (1986) Electrophoretic separation of complexes involved in the splicing of precursors to mRNAs. Cell, 46, 845-855. (Pubitemid 16027933)
    • (1986) Cell , vol.46 , Issue.6 , pp. 845-855
    • Konarska, M.M.1    Sharp, P.A.2
  • 9
    • 84859294938 scopus 로고    scopus 로고
    • Functional mammalian spliceosomal complex e contains SMN complex proteins in addition to U1 and U2 snRNPs
    • Makarov, E.M., Owen, N., Bottrill, A. and Makarova, O.V. (2012) Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs. Nucleic Acids Res., 40, 2639-2652.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2639-2652
    • Makarov, E.M.1    Owen, N.2    Bottrill, A.3    Makarova, O.V.4
  • 10
    • 78649656777 scopus 로고    scopus 로고
    • Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis
    • Bessonov, S., Anokhina, M., Krasauskas, A., Golas, M.M., Sander, B., Will, C.L., Urlaub, H., Stark, H. and Luhrmann, R. (2010) Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis. RNA, 16, 2384-2403.
    • (2010) RNA , vol.16 , pp. 2384-2403
    • Bessonov, S.1    Anokhina, M.2    Krasauskas, A.3    Golas, M.M.4    Sander, B.5    Will, C.L.6    Urlaub, H.7    Stark, H.8    Luhrmann, R.9
  • 11
    • 79959407313 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis method
    • Agafonov, D.E., Deckert, J., Wolf, E., Odenwä lder, P., Bessonov, S., Will, C.L., Urlaub, H. and Luhrmann, R. (2011) Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis method. Mol. Cell. Biol., 31, 2667-2682.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2667-2682
    • Agafonov, D.E.1    Deckert, J.2    Wolf, E.3    Odenwä Lder, P.4    Bessonov, S.5    Will, C.L.6    Urlaub, H.7    Luhrmann, R.8
  • 12
    • 0026655649 scopus 로고
    • The spliceosome assembly pathway in mammalian extracts
    • Jamison, S.F., Crow, A. and Garcia-Blanco, M.A. (1992) The spliceosome assembly pathway in mammalian extracts. Mol. Cell. Biol., 12, 4279-4287.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4279-4287
    • Jamison, S.F.1    Crow, A.2    Garcia-Blanco, M.A.3
  • 13
    • 0026263756 scopus 로고
    • An ATP-independent complex commits pre-mRNA to the mammalian spliceosome assembly pathway
    • Michaud, S. and Reed, R. (1991) An ATP-independent complex commits pre-mRNA to the mammalian spliceosome assembly pathway. Genes Dev., 5, 2534-2546. (Pubitemid 21905937)
    • (1991) Genes and Development , vol.5 , Issue.12 PART B , pp. 2534-2546
    • Michaud, S.1    Reed, R.2
  • 14
    • 0027215924 scopus 로고
    • A functional association between the 5' and 3' splice sites is established in the earliest prespliceosome complex (E) in mammals
    • Michaud, S. and Reed, R. (1993) A functional association between the 50 and 30 splice site is established in the earliest prespliceosome complex (E) in mammals. Genes Dev., 7, 1008-1020. (Pubitemid 23170825)
    • (1993) Genes and Development , vol.7 , Issue.6 , pp. 1008-1020
    • Michaud, S.1    Reed, R.2
  • 15
    • 0028006713 scopus 로고
    • SR proteins promote the first specific recognition of pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex
    • Staknis, D. and Reed, R. (1994) SR proteins promote the first specific recognition of pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex. Mol. Cell. Biol., 14, 7670-7682. (Pubitemid 24326433)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7670-7682
    • Staknis, D.1    Reed, R.2
  • 16
    • 79957784833 scopus 로고    scopus 로고
    • Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly
    • Cho, S., Hoang, A., Sinha, R., Zhong, X.Y., Fu, X.D., Krainer, A.R. and Ghosh, G. (2011) Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly. Proc. Natl Acad. Sci. USA, 108, 8233-8238.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 8233-8238
    • Cho, S.1    Hoang, A.2    Sinha, R.3    Zhong, X.Y.4    Fu, X.D.5    Krainer, A.R.6    Ghosh, G.7
  • 17
    • 0027313349 scopus 로고
    • Pathways for selection of 5' splice sites by U1 snRNPs and SF2/ASF
    • Eperon, I.C., Ireland, D.C., Smith, R.A., Mayeda, A. and Krainer, A.R. (1993) Pathways for selection of 50 splice sites by U1 snRNPs and SF2/ASF. EMBO J., 12, 3607-3617. (Pubitemid 23256447)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3607-3617
    • Eperon, I.C.1    Ireland, D.C.2    Smith, R.A.3    Mayeda, A.4    Krainer, A.R.5
  • 19
    • 84863022278 scopus 로고    scopus 로고
    • A U1-U2 snRNP interaction network during intron definition
    • Shao, W., Kim, H.S., Cao, Y., Xu, Y.Z. and Query, C.C. (2012) A U1-U2 snRNP interaction network during intron definition. Mol. Cell. Biol., 32, 470-478.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 470-478
    • Shao, W.1    Kim, H.S.2    Cao, Y.3    Xu, Y.Z.4    Query, C.C.5
  • 20
    • 0036315512 scopus 로고    scopus 로고
    • Early organization of pre-mRNA during spliceosome assembly
    • DOI 10.1038/nsb822
    • Kent, O.A. and MacMillan, A.M. (2002) Early organization of pre-mRNA during spliceosome assembly. Nat. Struct. Biol., 9, 576-581. (Pubitemid 34816136)
    • (2002) Nature Structural Biology , vol.9 , Issue.8 , pp. 576-581
    • Kent, O.A.1    MacMillan, A.M.2
  • 21
    • 33846665912 scopus 로고    scopus 로고
    • The 5′ End of U2 snRNA Is in Close Proximity to U1 and Functional Sites of the Pre-mRNA in Early Spliceosomal Complexes
    • DOI 10.1016/j.molcel.2006.12.019, PII S1097276506008872
    • Dö nmez, G., Hartmuth, K., Kastner, B., Will, C.L. and Luhrmann, R. (2007) The 50 end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes. Mol. Cell, 25, 399-411. (Pubitemid 46199285)
    • (2007) Molecular Cell , vol.25 , Issue.3 , pp. 399-411
    • Donmez, G.1    Hartmuth, K.2    Kastner, B.3    Will, C.L.4    Luhrmann, R.5
  • 22
    • 59449100357 scopus 로고    scopus 로고
    • Spliceosome assembly pathways for different types of alternative splicing converge during commitment to splice site pairing in the A complex
    • Kotlajich, M.V., Crabb, T.L. and Hertel, K.J. (2009) Spliceosome assembly pathways for different types of alternative splicing converge during commitment to splice site pairing in the A complex. Mol. Cell. Biol., 29, 1072-1082.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1072-1082
    • Kotlajich, M.V.1    Crabb, T.L.2    Hertel, K.J.3
  • 23
    • 4143078172 scopus 로고    scopus 로고
    • Commitment to splice site pairing coincides with a complex formation
    • DOI 10.1016/j.molcel.2004.06.025, PII S1097276504003739
    • Lim, S.R. and Hertel, K.J. (2004) Commitment to splice site pairing coincides with A complex formation. Mol. Cell, 15, 477-483. (Pubitemid 39092762)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 477-483
    • Lim, S.R.1    Hertel, K.J.2
  • 24
    • 0033762534 scopus 로고    scopus 로고
    • Selection of alternative 50 splice sites: Role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1
    • Eperon, I.C., Makarova, O.V., Mayeda, A., Munroe, S.H., Cá ceres, J.F., Hayward, D.G. and Krainer, A.R. (2000) Selection of alternative 50 splice sites: role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1. Mol. Cell. Biol., 20, 8303-8318.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8303-8318
    • Eperon, I.C.1    Makarova, O.V.2    Mayeda, A.3    Munroe, S.H.4    Cá Ceres, J.F.5    Hayward, D.G.6    Krainer, A.R.7
  • 27
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • DOI 10.1126/science.1068539
    • Zacharias, D.A., Violin, J.D., Newton, A.C. and Tsien, R.Y. (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science, 296, 913-916. (Pubitemid 34464897)
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 28
    • 0023895357 scopus 로고
    • A small-scale procedure for preparation of nuclear extracts that support efficient transcription and pre-mRNA splicing
    • Lee, K.A., Bindereif, A. and Green, M.R. (1988) A small-scale procedure for preparation of nuclear extracts that support efficient transcription and pre-mRNA splicing. Gene Anal. Tech., 5, 22-31.
    • (1988) Gene Anal. Tech. , vol.5 , pp. 22-31
    • Lee, K.A.1    Bindereif, A.2    Green, M.R.3
  • 29
    • 0026751769 scopus 로고
    • Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA
    • Kambach, C. and Mattaj, I.W. (1992) Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA. J. Cell. Biol., 118, 11-21.
    • (1992) J. Cell. Biol. , vol.118 , pp. 11-21
    • Kambach, C.1    Mattaj, I.W.2
  • 31
    • 41449108157 scopus 로고    scopus 로고
    • An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments
    • Aitken, C.E., Marshall, R.A. and Puglisi, J.D. (2008) An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments. Biophys. J., 94, 1826-1835.
    • (2008) Biophys. J. , vol.94 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 32
    • 78650273324 scopus 로고    scopus 로고
    • Functional organization of the Sm core in the crystal structure of human U1 snRNP
    • Weber, G., Trowitzsch, S., Kastner, B., Lü hrmann, R. and Wahl, M.C. (2010) Functional organization of the Sm core in the crystal structure of human U1 snRNP. EMBO J., 29, 4172-4184.
    • (2010) EMBO J. , vol.29 , pp. 4172-4184
    • Weber, G.1    Trowitzsch, S.2    Kastner, B.3    Lü Hrmann, R.4    Wahl, M.C.5
  • 34
    • 0025137186 scopus 로고
    • U1-specific protein C needed for efficient complex formation of U1 snRNP with a 50 splice site
    • Heinrichs, V., Bach, M., Winkelmann, G. and Luhrmann, R. (1990) U1-specific protein C needed for efficient complex formation of U1 snRNP with a 50 splice site. Science, 247, 69-72.
    • (1990) Science , vol.247 , pp. 69-72
    • Heinrichs, V.1    Bach, M.2    Winkelmann, G.3    Luhrmann, R.4
  • 35
    • 0028941920 scopus 로고
    • Modulation of 50 splice site choice in pre-messenger RNA by two distinct steps
    • Tarn, W.Y. and Steitz, J.A. (1995) Modulation of 50 splice site choice in pre-messenger RNA by two distinct steps. Proc. Natl. Acad. Sci. USA, 92, 2504-2508.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2504-2508
    • Tarn, W.Y.1    Steitz, J.A.2
  • 36
    • 0029847221 scopus 로고    scopus 로고
    • In vitro reconstitution of mammalian U1 snRNPs active in splicing: The U1-C protein enhances the formation of early (E) spliceosomal complexes
    • Will, C.L., Rü mpler, S., Klein Gunnewiek, J., van Venrooij, W.J. and Luhrmann, R. (1996) In vitro reconstitution of mammalian U1 snRNPs active in splicing: the U1-C protein enhances the formation of early (E) spliceosomal complexes. Nucleic Acids Res., 24, 4614-4623. (Pubitemid 26413336)
    • (1996) Nucleic Acids Research , vol.24 , Issue.23 , pp. 4614-4623
    • Will, C.L.1    Rumpler, S.2    Gunnewiek, J.K.3    Van Venrooij, W.J.4    Luhrmann, R.5
  • 37
    • 0032531261 scopus 로고    scopus 로고
    • Dynamic interactions between splicing snRNPs, coiled bodies and nucleoli revealed using snRNP protein fusions to the green fluorescent protein
    • DOI 10.1006/excr.1998.4135
    • Sleeman, J., Lyon, C.E., Platani, M., Kreivi, J.P. and Lamond, A.I. (1998) Dynamic interactions between splicing snRNPs, coiled bodies and nucleoli revealed using snRNP protein fusions to the green fluorescent protein. Exp. Cell Res., 243, 290-304. (Pubitemid 28488840)
    • (1998) Experimental Cell Research , vol.243 , Issue.2 , pp. 290-304
    • Sleeman, J.1    Lyon, C.E.2    Platani, M.3    Kreivi, J.-P.4    Lamond, A.I.5
  • 38
    • 58049196877 scopus 로고    scopus 로고
    • Role of Cajal bodies and nucleolus in the maturation of the U1 snRNP in Arabidopsis
    • Lorković , Z.J. and Barta, A. (2008) Role of Cajal bodies and nucleolus in the maturation of the U1 snRNP in Arabidopsis. PLoS One, 3, e3989.
    • (2008) PLoS One , vol.3
    • Lorković, Z.J.1    Barta, A.2
  • 40
    • 0028034324 scopus 로고
    • Complementation by SR proteins of pre-mRNA splicing reactions depleted of U1 snRNP
    • Crispino, J.D., Blencowe, B.J. and Sharp, P.A. (1994) Complementation by SR proteins of pre-mRNA splicing reactions depleted of U1 snRNP. Science, 265, 1866-1869. (Pubitemid 24324242)
    • (1994) Science , vol.265 , Issue.5180 , pp. 1866-1869
    • Crispino, J.D.1    Blencowe, B.J.2    Sharp, P.A.3
  • 41
    • 0029949594 scopus 로고    scopus 로고
    • Cis-acting elements distinct from the 5' splice site promote U1- independent pre-mRNA splicing
    • Crispino, J.D., Mermoud, J.E., Lamond, A.I. and Sharp, P.A. (1996) Cis-acting elements distinct from the 50 splice site promote U1-independent pre-mRNA splicing. RNA, 2, 664-673. (Pubitemid 26374218)
    • (1996) RNA , vol.2 , Issue.7 , pp. 664-673
    • Crispino, J.D.1    Mermoud, J.E.2    Lamond, A.I.3    Sharp, P.A.4
  • 42
    • 0028072388 scopus 로고
    • SR proteins can compensate for the loss of U1 snRNP functions in vitro
    • Tarn, W.Y. and Steitz, J.A. (1994) SR proteins can compensate for the loss of U1 snRNP functions in vitro. Genes Dev., 8, 2704-2717. (Pubitemid 24375420)
    • (1994) Genes and Development , vol.8 , Issue.22 , pp. 2704-2717
    • Tarn, W.-Y.1    Steitz, J.A.2
  • 43
    • 0033999614 scopus 로고    scopus 로고
    • Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation
    • DOI 10.1128/MCB.20.6.2209-2217.2000
    • Klein Gunnewiek, J.M., Hussein, R.I., van Aarssen, Y., Palacios, D., de Jong, R., van Venrooij, W.J. and Gunderson, S.I. (2000) Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation. Mol. Cell. Biol., 20, 2209-2217. (Pubitemid 30123836)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.6 , pp. 2209-2217
    • Gunnewiek, J.M.T.K.1    Hussein, R.I.2    Van Aarssen, Y.3    Palacios, D.4    De Jong, R.5    Van Venrooij, W.J.6    Gunderson, S.I.7
  • 44
    • 0034070741 scopus 로고    scopus 로고
    • The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
    • DOI 10.1038/74101
    • Varani, L., Gunderson, S.I., Mattaj, I.W., Kay, L.E., Neuhaus, D. and Varani, G. (2000) The NMR structure of the 38 kDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. Nat. Struct. Biol., 7, 329-335. (Pubitemid 30194458)
    • (2000) Nature Structural Biology , vol.7 , Issue.4 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, L.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6
  • 45
    • 58149092362 scopus 로고    scopus 로고
    • Stalling of spliceosome assembly at distinct stages by small-molecule inhibitors of protein acetylation and deacetylation
    • Kuhn, A.N., van Santen, M.A., Schwienhorst, A., Urlaub, H. and Luhrmann, R. (2009) Stalling of spliceosome assembly at distinct stages by small-molecule inhibitors of protein acetylation and deacetylation. RNA, 15, 153-175.
    • (2009) RNA , vol.15 , pp. 153-175
    • Kuhn, A.N.1    Van Santen, M.A.2    Schwienhorst, A.3    Urlaub, H.4    Luhrmann, R.5
  • 46
    • 0027471377 scopus 로고
    • The human U1 snRNP-specific U1A protein inhibits polyadenylation of its own pre-mRNA
    • DOI 10.1016/0092-8674(93)90577-D
    • Boelens, W.C., Jansen, E., Van, V.W., Stripecke, R., Mattal, I.W. and Gunderson, S.I. (1993) The human U1 snRNP-specific U1A protein inhibits polyadenylation of its own pre-mRNA. Cell, 72, 881-892. (Pubitemid 23110230)
    • (1993) Cell , vol.72 , Issue.6 , pp. 881-892
    • Boelens, W.C.1    Jansen, E.J.R.2    Van Venrooij, W.J.3    Stripecke, R.4    Mattal, I.W.5    Gunderson, S.I.6
  • 47
    • 0023088168 scopus 로고
    • Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes
    • Chabot, B. and Steitz, J.A. (1987) Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes. Mol. Cell. Biol., 7, 281-293. (Pubitemid 17230411)
    • (1987) Molecular and Cellular Biology , vol.7 , Issue.1 , pp. 281-293
    • Chabot, B.1    Steitz, J.A.2
  • 48
    • 0030611640 scopus 로고    scopus 로고
    • 65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction
    • Fleckner, J., Zhang, M., Valcá rcel, J. and Green, M.R. (1997) U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. Genes Dev., 11, 1864-1872. (Pubitemid 27315215)
    • (1997) Genes and Development , vol.11 , Issue.14 , pp. 1864-1872
    • Fleckner, J.1    Zhang, M.2    Valcarcel, J.3    Green, M.R.4
  • 49
    • 46249107277 scopus 로고    scopus 로고
    • Distinct activities of the DExD/H-box splicing factor hUAP56 facilitate stepwise assembly of the spliceosome
    • DOI 10.1101/gad.1657308
    • Shen, H., Zheng, X., Shen, J., Zhang, L., Zhao, R. and Green, M.R. (2008) Distinct activities of the DExD/H-box splicing factor hUAP56 facilitate stepwise assembly of the spliceosome. Genes Dev., 22, 1796-1803. (Pubitemid 351915504)
    • (2008) Genes and Development , vol.22 , Issue.13 , pp. 1796-1803
    • Shen, H.1    Zheng, X.2    Shen, J.3    Zhang, L.4    Zhao, R.5    Green, M.R.6
  • 50
    • 1542380571 scopus 로고    scopus 로고
    • Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA
    • DOI 10.1038/sj.emboj.7600050
    • Xu, Y.Z., Newnham, C.M., Kameoka, S., Huang, T., Konarska, M.M. and Query, C.C. (2004) Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA. EMBO J., 23, 376-385. (Pubitemid 38294502)
    • (2004) EMBO Journal , vol.23 , Issue.2 , pp. 376-385
    • Xu, Y.-Z.1    Newnham, C.M.2    Kameoka, S.3    Huang, T.4    Konarska, M.M.5    Query, C.C.6
  • 51
    • 77950643284 scopus 로고    scopus 로고
    • Competing upstream 50 splice sites enhance the rate of proximal splicing
    • Hicks, M.J., Mueller, W.F., Shepard, P.J. and Hertel, K.J. (2010) Competing upstream 50 splice sites enhance the rate of proximal splicing. Mol. Cell. Biol., 30, 1878-1886.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1878-1886
    • Hicks, M.J.1    Mueller, W.F.2    Shepard, P.J.3    Hertel, K.J.4
  • 52
    • 0022516779 scopus 로고
    • A role for exon sequences and splice-site proximity in splice-site selection
    • Reed, R. and Maniatis, T. (1986) A role for exon sequences and splice-site proximity in splice-site selection. Cell, 46, 681-690. (Pubitemid 16020060)
    • (1986) Cell , vol.46 , Issue.5 , pp. 681-690
    • Reed, R.1    Maniatis, T.2
  • 54
    • 79956071179 scopus 로고    scopus 로고
    • DEAD-box proteins as RNA helicases and chaperones
    • Jarmoskaite, I. and Russell, R. (2011) DEAD-box proteins as RNA helicases and chaperones. Wiley Interdiscip. Rev. RNA, 2, 135-152.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 135-152
    • Jarmoskaite, I.1    Russell, R.2
  • 55
    • 0035668536 scopus 로고    scopus 로고
    • Making contacts on a nucleic acid polymer
    • DOI 10.1016/S0968-0004(01)01978-8, PII S0968000401019788
    • Rippe, K. (2001) Making contacts on a nucleic acid polymer. Trends Biochem. Sci., 26, 733-740. (Pubitemid 34014840)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.12 , pp. 733-740
    • Rippe, K.1
  • 56
    • 0025981410 scopus 로고
    • Influences of separation and adjacent sequences on the use of alternative 5′ splice sites
    • Cunningham, S.A., Else, A.J., Potter, B. and Eperon, I.C. (1991) Influences of separation and adjacent sequences on the use of alternative 50 splice sites. J. Mol. Biol., 217, 265-281. (Pubitemid 121003939)
    • (1991) Journal of Molecular Biology , vol.217 , Issue.2 , pp. 265-281
    • Cunningham, S.A.1    Else, A.J.2    Potter, B.V.L.3    Eperon, I.C.4
  • 57
    • 0019851631 scopus 로고
    • Correlation of hnRNP structure and nascent transcript cleavage
    • Beyer, A.L., Bouton, A.H. and Miller, O.L. Jr (1981) Correlation of hnRNP structure and nascent transcript cleavage. Cell, 26, 155-165. (Pubitemid 12244495)
    • (1981) Cell , vol.26 , Issue.2 , pp. 155-165
    • Beyer, A.L.1    Bouton, A.H.2    Miller Jr., O.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.