메뉴 건너뛰기




Volumn 11, Issue 19, 2014, Pages 113-122

The supraspliceosome - A multi-task machine for regulated pre-mRNA processing in the cell nucleus

Author keywords

Alternative splicing; Intronic microRNA biogenesis; Pre mRNA splicing; Riponucleoproteins (RNPs); Suppression of splicing; U snRNPs

Indexed keywords

MAMMALIA;

EID: 84925855108     PISSN: None     EISSN: 20010370     Source Type: Journal    
DOI: 10.1016/j.csbj.2014.09.008     Document Type: Review
Times cited : (27)

References (98)
  • 2
    • 0003604405 scopus 로고    scopus 로고
    • R.F. Gesteland, T.R. Cech, J.F. Atkins, 2nd ed. Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • C.B. Burge, T.H. Tuschl, and P.A. Sharp The RNA world R.F. Gesteland, T.R. Cech, J.F. Atkins, 2nd ed. 1999 Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York 525 560
    • (1999) The RNA World , pp. 525-560
    • Burge, C.B.1    Tuschl, T.H.2    Sharp, P.A.3
  • 3
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: Motors, clocks, springs, and things
    • J.P. Staley, and C. Guthrie Mechanical devices of the spliceosome: motors, clocks, springs, and things Cell 92 1998 315 326
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 4
    • 0036948420 scopus 로고    scopus 로고
    • Allosteric cascade of spliceosome activation
    • D.A. Brow Allosteric cascade of spliceosome activation Annu Rev Genet 36 2002 333 360
    • (2002) Annu Rev Genet , vol.36 , pp. 333-360
    • Brow, D.A.1
  • 5
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • C.L. Will, and R. Lührmann Spliceosomal UsnRNP biogenesis, structure and function Curr Opin Cell Biol 13 2001 290 301
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 290-301
    • Will, C.L.1    Lührmann, R.2
  • 6
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • M.C. Wahl, C.L. Will, and R. Lührmann The spliceosome: design principles of a dynamic RNP machine Cell 136 2009 701 718
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Lührmann, R.3
  • 7
    • 84893110707 scopus 로고    scopus 로고
    • Structural studies of the spliceosome: Zooming into the heart of the machine
    • W.P. Galej, T.H. Nguyen, A.J. Newman, and K. Nagai Structural studies of the spliceosome: zooming into the heart of the machine Curr Opin Struct Biol 25C 2014 57 66
    • (2014) Curr Opin Struct Biol , vol.25 C , pp. 57-66
    • Galej, W.P.1    Nguyen, T.H.2    Newman, A.J.3    Nagai, K.4
  • 8
    • 84893716781 scopus 로고    scopus 로고
    • The spliceosome: Disorder and dynamics defined
    • W.J. Chen, and M.J. Moore The spliceosome: disorder and dynamics defined Curr Opin Struct Biol 24 2014 141 149
    • (2014) Curr Opin Struct Biol , vol.24 , pp. 141-149
    • Chen, W.J.1    Moore, M.J.2
  • 9
    • 55249093247 scopus 로고    scopus 로고
    • Structure and function of the pre-mRNA splicing machine
    • J. Sperling, M. Azubel, and R. Sperling Structure and function of the pre-mRNA splicing machine Structure 16 2008 1605 1615
    • (2008) Structure , vol.16 , pp. 1605-1615
    • Sperling, J.1    Azubel, M.2    Sperling, R.3
  • 10
    • 0029786763 scopus 로고    scopus 로고
    • Phosphorylated Ser/Arg-rich proteins: Limiting factors in the assembly of 200S large nuclear ribonucleoprotein particles
    • S. Yitzhaki, E. Miriami, J. Sperling, and R. Sperling Phosphorylated Ser/Arg-rich proteins: limiting factors in the assembly of 200S large nuclear ribonucleoprotein particles Proc Natl Acad Sci U S A 93 1996 8830 8835
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8830-8835
    • Yitzhaki, S.1    Miriami, E.2    Sperling, J.3    Sperling, R.4
  • 12
    • 0028901789 scopus 로고
    • Magnesium cations are required for the association of U small nuclear ribonucleoproteins and SR proteins with pre-mRNA in 200 S large nuclear ribonucleoprotein particles
    • E. Miriami, M. Angenitzki, R. Sperling, and J. Sperling Magnesium cations are required for the association of U small nuclear ribonucleoproteins and SR proteins with pre-mRNA in 200 S large nuclear ribonucleoprotein particles J Mol Biol 246 1995 254 263
    • (1995) J Mol Biol , vol.246 , pp. 254-263
    • Miriami, E.1    Angenitzki, M.2    Sperling, R.3    Sperling, J.4
  • 13
    • 33748603768 scopus 로고    scopus 로고
    • WT1 interacts with the splicing protein RBM4 and regulates its ability to modulate alternative splicing in vivo
    • M.A. Markus, B. Heinrich, O. Raitskin, D.J. Adams, H. Mangs, and C. Goy WT1 interacts with the splicing protein RBM4 and regulates its ability to modulate alternative splicing in vivo Exp Cell Res 312 2006 3379 3388
    • (2006) Exp Cell Res , vol.312 , pp. 3379-3388
    • Markus, M.A.1    Heinrich, B.2    Raitskin, O.3    Adams, D.J.4    Mangs, H.5    Goy, C.6
  • 14
    • 67649831277 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA
    • B. Heinrich, Z. Zhang, O. Raitskin, M. Hiller, N. Benderska, and A.M. Hartmann Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA J Biol Chem 284 2009 14303 14315
    • (2009) J Biol Chem , vol.284 , pp. 14303-14315
    • Heinrich, B.1    Zhang, Z.2    Raitskin, O.3    Hiller, M.4    Benderska, N.5    Hartmann, A.M.6
  • 15
    • 84883265250 scopus 로고    scopus 로고
    • ZRANB2 localizes to supraspliceosomes and influences the alternative splicing of multiple genes in the transcriptome
    • Y.-H.J. Yang, A.M. Markus, H.A. Mangs, O. Raitskin, R. Sperling, and B.J. Morris ZRANB2 localizes to supraspliceosomes and influences the alternative splicing of multiple genes in the transcriptome Mol Biol Rep 40 2013 5381 5395
    • (2013) Mol Biol Rep , vol.40 , pp. 5381-5395
    • Yang, Y.-H.J.1    Markus, A.M.2    Mangs, H.A.3    Raitskin, O.4    Sperling, R.5    Morris, B.J.6
  • 16
    • 0032561135 scopus 로고    scopus 로고
    • A supraspliceosome model for large nuclear ribonucleoprotein particles based on mass determinations by scanning transmission electron microscopy
    • S. Müller, B. Wolpensinger, M. Angenitzki, A. Engel, J. Sperling, and R. Sperling A supraspliceosome model for large nuclear ribonucleoprotein particles based on mass determinations by scanning transmission electron microscopy J Mol Biol 283 1998 383 394
    • (1998) J Mol Biol , vol.283 , pp. 383-394
    • Müller, S.1    Wolpensinger, B.2    Angenitzki, M.3    Engel, A.4    Sperling, J.5    Sperling, R.6
  • 17
    • 34547647038 scopus 로고    scopus 로고
    • Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes expands the catalog of participating factors
    • Y.I. Chen, R.E. Moore, H.Y. Ge, M.K. Young, T.D. Lee, and S.W. Stevens Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes expands the catalog of participating factors Nucleic Acids Res 35 2007 3928 3944
    • (2007) Nucleic Acids Res , vol.35 , pp. 3928-3944
    • Chen, Y.I.1    Moore, R.E.2    Ge, H.Y.3    Young, M.K.4    Lee, T.D.5    Stevens, S.W.6
  • 18
    • 84903698579 scopus 로고    scopus 로고
    • Supraspliceosomes at defined functional states present portray the pre-assembled nature of the pre-mRNA processing machine in the cell nucleus
    • H. Kotzer-Nevo, F. de Lima Alves, J. Rappsilber, J. Sperling, and R. Sperling Supraspliceosomes at defined functional states present portray the pre-assembled nature of the pre-mRNA processing machine in the cell nucleus Int J Mol Sci 15 2014 11637 11664
    • (2014) Int J Mol Sci , vol.15 , pp. 11637-11664
    • Kotzer-Nevo, H.1    De Lima Alves, F.2    Rappsilber, J.3    Sperling, J.4    Sperling, R.5
  • 19
    • 31344454049 scopus 로고    scopus 로고
    • Native spliceosomes assemble with pre-mRNA to form supraspliceosomes
    • M. Azubel, N. Habib, J. Sperling, and R. Sperling Native spliceosomes assemble with pre-mRNA to form supraspliceosomes J Mol Biol 356 2006 955 966
    • (2006) J Mol Biol , vol.356 , pp. 955-966
    • Azubel, M.1    Habib, N.2    Sperling, J.3    Sperling, R.4
  • 21
    • 0024509154 scopus 로고
    • Isolation and visualization of large compact ribonucleoprotein particles of specific nuclear RNAs
    • P. Spann, M. Feinerman, J. Sperling, and R. Sperling Isolation and visualization of large compact ribonucleoprotein particles of specific nuclear RNAs Proc Natl Acad Sci U S A 86 1989 466 470
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 466-470
    • Spann, P.1    Feinerman, M.2    Sperling, J.3    Sperling, R.4
  • 22
    • 0028071845 scopus 로고
    • Heat shock affects 5′ splice site selection, cleavage and ligation of CAD pre-mRNA in hamster cells, but not its packaging in lnRNP particles
    • E. Miriami, J. Sperling, and R. Sperling Heat shock affects 5′ splice site selection, cleavage and ligation of CAD pre-mRNA in hamster cells, but not its packaging in lnRNP particles Nucleic Acids Res 22 1994 3084 3091
    • (1994) Nucleic Acids Res , vol.22 , pp. 3084-3091
    • Miriami, E.1    Sperling, J.2    Sperling, R.3
  • 23
    • 0036158942 scopus 로고    scopus 로고
    • Composition and functional characterization of the yeast spliceosomal penta-snRNP
    • S.W. Stevens, D.E. Ryan, H.Y. Ge, R.E. Moore, M.K. Young, and T.D. Lee Composition and functional characterization of the yeast spliceosomal penta-snRNP Mol Cell 9 2002 31 44
    • (2002) Mol Cell , vol.9 , pp. 31-44
    • Stevens, S.W.1    Ryan, D.E.2    Ge, H.Y.3    Moore, R.E.4    Young, M.K.5    Lee, T.D.6
  • 24
    • 34249053165 scopus 로고    scopus 로고
    • RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation
    • J.R. Hogg, and K. Collins RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation RNA 13 2007 868 880
    • (2007) RNA , vol.13 , pp. 868-880
    • Hogg, J.R.1    Collins, K.2
  • 25
    • 0003604405 scopus 로고    scopus 로고
    • R.F. Gesteland, J.F. Atkins, Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • S.J. Baserga, and J.A. Steitz The RNA world R.F. Gesteland, J.F. Atkins, 1993 Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York 359 381
    • (1993) The RNA World , pp. 359-381
    • Baserga, S.J.1    Steitz, J.A.2
  • 26
    • 0036161499 scopus 로고    scopus 로고
    • The spliceosome: No assembly required?
    • T.W. Nilsen The spliceosome: no assembly required? Mol Cell 9 2002 8 9
    • (2002) Mol Cell , vol.9 , pp. 8-9
    • Nilsen, T.W.1
  • 27
    • 0031413405 scopus 로고    scopus 로고
    • Automated electron tomography of large nuclear RNP (lnRNP) particles - The naturally assembled complexes of precursor messenger RNA and splicing factors
    • O. Medalia, A.J. Koster, A. Tocilj, M. Angenitzki, J. Sperling, and Y.Z. Berkovitch Automated electron tomography of large nuclear RNP (lnRNP) particles - the naturally assembled complexes of precursor messenger RNA and splicing factors J Struct Biol 120 1997 228 236
    • (1997) J Struct Biol , vol.120 , pp. 228-236
    • Medalia, O.1    Koster, A.J.2    Tocilj, A.3    Angenitzki, M.4    Sperling, J.5    Berkovitch, Y.Z.6
  • 28
    • 0036422206 scopus 로고    scopus 로고
    • Cryoelectron microscopy and cryoelectron tomography of the nuclear pre-mRNA processing machine
    • O. Medalia, D. Typke, R. Hegerl, M. Angenitzki, J. Sperling, and R. Sperling Cryoelectron microscopy and cryoelectron tomography of the nuclear pre-mRNA processing machine J Struct Biol 138 2002 74 84
    • (2002) J Struct Biol , vol.138 , pp. 74-84
    • Medalia, O.1    Typke, D.2    Hegerl, R.3    Angenitzki, M.4    Sperling, J.5    Sperling, R.6
  • 29
    • 33845437204 scopus 로고    scopus 로고
    • Intranuclear binding kinetics and mobility of single native U1 snRNP particles in living cells
    • D. Grunwald, B. Spottke, V. Buschmann, and U. Kubitscheck Intranuclear binding kinetics and mobility of single native U1 snRNP particles in living cells Mol Biol Cell 17 2006 5017 5027
    • (2006) Mol Biol Cell , vol.17 , pp. 5017-5027
    • Grunwald, D.1    Spottke, B.2    Buschmann, V.3    Kubitscheck, U.4
  • 30
    • 33947598952 scopus 로고    scopus 로고
    • Exploring the architecture of the intact supraspliceosome using electron microscopy
    • S. Cohen-Krausz, R. Sperling, and J. Sperling Exploring the architecture of the intact supraspliceosome using electron microscopy J Mol Biol 368 2007 319 327
    • (2007) J Mol Biol , vol.368 , pp. 319-327
    • Cohen-Krausz, S.1    Sperling, R.2    Sperling, J.3
  • 31
    • 4444233084 scopus 로고    scopus 로고
    • Three-dimensional structure of the native spliceosome by cryo-electron microscopy
    • M. Azubel, S.G. Wolf, J. Sperling, and R. Sperling Three-dimensional structure of the native spliceosome by cryo-electron microscopy Mol Cell 15 2004 833 839
    • (2004) Mol Cell , vol.15 , pp. 833-839
    • Azubel, M.1    Wolf, S.G.2    Sperling, J.3    Sperling, R.4
  • 32
    • 84861981718 scopus 로고    scopus 로고
    • A unique spatial arrangement of the snRNPs within the native spliceosome emerges from in silico studies
    • Z. Frankenstein, J. Sperling, R. Sperling, and M. Eisenstein A unique spatial arrangement of the snRNPs within the native spliceosome emerges from In silico studies Structure 20 2012 1097 1106
    • (2012) Structure , vol.20 , pp. 1097-1106
    • Frankenstein, Z.1    Sperling, J.2    Sperling, R.3    Eisenstein, M.4
  • 34
    • 0037107547 scopus 로고    scopus 로고
    • On the importance of being co-transcriptional
    • K.M. Neugebauer On the importance of being co-transcriptional J Cell Sci 115 2002 3865 3871
    • (2002) J Cell Sci , vol.115 , pp. 3865-3871
    • Neugebauer, K.M.1
  • 35
    • 42449089029 scopus 로고    scopus 로고
    • Coupling transcription and alternative splicing
    • A.R. Kornblihtt Coupling transcription and alternative splicing Adv Exp Med Biol 623 2007 175 189
    • (2007) Adv Exp Med Biol , vol.623 , pp. 175-189
    • Kornblihtt, A.R.1
  • 36
    • 44449142796 scopus 로고    scopus 로고
    • The CTD role in cotranscriptional RNA processing and surveillance
    • S.F. de Almeida, and M. Carmo-Fonseca The CTD role in cotranscriptional RNA processing and surveillance FEBS Lett 582 2008 1971 1976
    • (2008) FEBS Lett , vol.582 , pp. 1971-1976
    • De Almeida, S.F.1    Carmo-Fonseca, M.2
  • 37
    • 0027242177 scopus 로고
    • A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: Implications for the spliceosome assembly pathway
    • D.A. Wassarman, and J.A. Steitz A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: Implications for the spliceosome assembly pathway Proc Natl Acad Sci U S A 90 1993 7139 7143
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7139-7143
    • Wassarman, D.A.1    Steitz, J.A.2
  • 38
    • 0031670145 scopus 로고    scopus 로고
    • The path of transcripts from extra-nucleolar synthetic sites to nuclear pores: Transcripts in transit are concentrated in discrete structures containing SR proteins
    • F.J. Iborra, D.A. Jackson, and P.R. Cook The path of transcripts from extra-nucleolar synthetic sites to nuclear pores: transcripts in transit are concentrated in discrete structures containing SR proteins J Cell Sci 111 1998 2269 2282
    • (1998) J Cell Sci , vol.111 , pp. 2269-2282
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 39
    • 0036966352 scopus 로고    scopus 로고
    • Large nuclear RNP particles-the nuclear pre-mRNA processing machine
    • O. Raitskin, M. Angenitzki, J. Sperling, and R. Sperling Large nuclear RNP particles-the nuclear pre-mRNA processing machine J Struct Biol 140 2002 123 130
    • (2002) J Struct Biol , vol.140 , pp. 123-130
    • Raitskin, O.1    Angenitzki, M.2    Sperling, J.3    Sperling, R.4
  • 40
    • 77952293063 scopus 로고    scopus 로고
    • Functions and regulation of RNA editing by ADAR deaminases
    • K. Nishikura Functions and regulation of RNA editing by ADAR deaminases Annu Rev Biochem 79 79 2010 321 349
    • (2010) Annu Rev Biochem , vol.79 , Issue.79 , pp. 321-349
    • Nishikura, K.1
  • 42
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • B.L. Bass RNA editing by adenosine deaminases that act on RNA Annu Rev Biochem 71 2002 817 846
    • (2002) Annu Rev Biochem , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 43
    • 0035811009 scopus 로고    scopus 로고
    • RNA editing activity is associated with splicing factors in lnRNP particles: The nuclear pre-mRNA processing machinery
    • O. Raitskin, D.S. Cho, J. Sperling, K. Nishikura, and R. Sperling RNA editing activity is associated with splicing factors in lnRNP particles: the nuclear pre-mRNA processing machinery Proc Natl Acad Sci U S A 98 2001 6571 6576
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6571-6576
    • Raitskin, O.1    Cho, D.S.2    Sperling, J.3    Nishikura, K.4    Sperling, R.5
  • 44
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Q. Pan, O. Shai, L.J. Lee, B.J. Frey, and B.J. Blencowe Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing Nat Genet 40 2008 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
  • 45
    • 38349132539 scopus 로고    scopus 로고
    • Genome-wide analysis of alternative pre-mRNA splicing
    • C. Ben-Dov, B. Hartmann, J. Lundgren, and J. Valcarcel Genome-wide analysis of alternative pre-mRNA splicing J Biol Chem 283 2008 1229 1233
    • (2008) J Biol Chem , vol.283 , pp. 1229-1233
    • Ben-Dov, C.1    Hartmann, B.2    Lundgren, J.3    Valcarcel, J.4
  • 47
    • 84934435678 scopus 로고    scopus 로고
    • Regulation of alternative pre-mRNA splicing
    • M.B. Coelho, and C.W. Smith Regulation of alternative pre-mRNA splicing Methods Mol Biol 1126 2014 55 82
    • (2014) Methods Mol Biol , vol.1126 , pp. 55-82
    • Coelho, M.B.1    Smith, C.W.2
  • 48
    • 33746927884 scopus 로고    scopus 로고
    • The connection between splicing and cancer
    • A. Srebrow, and A.R. Kornblihtt The connection between splicing and cancer J Cell Sci 119 2006 2635 2641
    • (2006) J Cell Sci , vol.119 , pp. 2635-2641
    • Srebrow, A.1    Kornblihtt, A.R.2
  • 50
    • 73949128867 scopus 로고    scopus 로고
    • The pathobiology of splicing
    • A.J. Ward, and T.A. Cooper The pathobiology of splicing J Pathol 220 2010 152 163
    • (2010) J Pathol , vol.220 , pp. 152-163
    • Ward, A.J.1    Cooper, T.A.2
  • 51
    • 84861961269 scopus 로고    scopus 로고
    • Alternative splicing: Decoding an expansive regulatory layer
    • M. Irimia, and B.J. Blencowe Alternative splicing: decoding an expansive regulatory layer Curr Opin Cell Biol 24 2012 323 332
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 323-332
    • Irimia, M.1    Blencowe, B.J.2
  • 52
    • 77956687928 scopus 로고    scopus 로고
    • Functional diversity of the hnRNPs: Past, present and perspectives
    • S.P. Han, Y.H. Tang, and R. Smith Functional diversity of the hnRNPs: past, present and perspectives Biochem J 430 2010 379 392
    • (2010) Biochem J , vol.430 , pp. 379-392
    • Han, S.P.1    Tang, Y.H.2    Smith, R.3
  • 53
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors
    • A. Busch, and K.J. Hertel Evolution of SR protein and hnRNP splicing regulatory factors Wiley Interdiscip Rev 3 2012 1 12
    • (2012) Wiley Interdiscip Rev , vol.3 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 54
    • 42449159377 scopus 로고    scopus 로고
    • SR proteins and related factors in alternative splicing
    • S. Lin, and X.D. Fu SR proteins and related factors in alternative splicing Adv Exp Med Biol 623 2007 107 122
    • (2007) Adv Exp Med Biol , vol.623 , pp. 107-122
    • Lin, S.1    Fu, X.D.2
  • 56
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: Master regulators of gene expression
    • J.C. Long, and J.F. Caceres The SR protein family of splicing factors: master regulators of gene expression Biochem J 417 2009 15 27
    • (2009) Biochem J , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 57
    • 84876048680 scopus 로고    scopus 로고
    • Pyrvinium pamoate changes alternative splicing of the serotonin receptor 2C by influencing its RNA structure
    • M. Shen, S. Bellaousov, M. Hiller, P. de La Grange, T.P. Creame, and O. Malina Pyrvinium pamoate changes alternative splicing of the serotonin receptor 2C by influencing its RNA structure Nucleic Acids Res 41 2013 3819 3832
    • (2013) Nucleic Acids Res , vol.41 , pp. 3819-3832
    • Shen, M.1    Bellaousov, S.2    Hiller, M.3    De La Grange, P.4    Creame, T.P.5    Malina, O.6
  • 58
    • 37648998629 scopus 로고    scopus 로고
    • Getting to the root of miRNA-mediated gene silencing
    • A. Eulalio, E. Huntzinger, and E. Izaurralde Getting to the root of miRNA-mediated gene silencing Cell 132 2008 9 14
    • (2008) Cell , vol.132 , pp. 9-14
    • Eulalio, A.1    Huntzinger, E.2    Izaurralde, E.3
  • 59
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • D.P. Bartel MicroRNAs: target recognition and regulatory functions Cell 136 2009 215 233
    • (2009) Cell , vol.136 , pp. 215-233
    • Bartel, D.P.1
  • 60
    • 84861866572 scopus 로고    scopus 로고
    • The mechanics of miRNA-mediated gene silencing: A look under the hood of miRISC
    • M.R. Fabian, and N. Sonenberg The mechanics of miRNA-mediated gene silencing: a look under the hood of miRISC Nat Struct Mol Biol 19 2012 586 593
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 586-593
    • Fabian, M.R.1    Sonenberg, N.2
  • 61
    • 6344281172 scopus 로고    scopus 로고
    • Identification of mammalian microRNA host genes and transcription units
    • A. Rodriguez, S. Griffiths-Jones, J.L. Ashurst, and A. Bradley Identification of mammalian microRNA host genes and transcription units Genome Res 14 2004 1902 1910
    • (2004) Genome Res , vol.14 , pp. 1902-1910
    • Rodriguez, A.1    Griffiths-Jones, S.2    Ashurst, J.L.3    Bradley, A.4
  • 62
    • 33846945735 scopus 로고    scopus 로고
    • Processing of intronic microRNAs
    • Y.K. Kim, and V.N. Kim Processing of intronic microRNAs Embo J 26 2007 775 783
    • (2007) Embo J , vol.26 , pp. 775-783
    • Kim, Y.K.1    Kim, V.N.2
  • 63
    • 70350004858 scopus 로고    scopus 로고
    • An evolutionary perspective of animal microRNAs and their targets
    • N. Shomron, D. Golan, and E. Hornstein An evolutionary perspective of animal microRNAs and their targets J Biomed Biotechnol 2009 2009 594738
    • (2009) J Biomed Biotechnol , vol.2009 , pp. 594738
    • Shomron, N.1    Golan, D.2    Hornstein, E.3
  • 64
    • 84899008312 scopus 로고    scopus 로고
    • Interplay between pre-mRNA splicing and microRNA biogenesis within the supraspliceosome
    • L. Agranat-Tamir, N. Shomron, J. Sperling, and R. Sperling Interplay between pre-mRNA splicing and microRNA biogenesis within the supraspliceosome Nucl Acids Res 42 2014 4640 4651
    • (2014) Nucl Acids Res , vol.42 , pp. 4640-4651
    • Agranat-Tamir, L.1    Shomron, N.2    Sperling, J.3    Sperling, R.4
  • 65
    • 54249158400 scopus 로고    scopus 로고
    • Emerging role of miR-106b-25/miR-17-92 clusters in the control of transforming growth factor beta signaling
    • F. Petrocca, A. Vecchione, and C.M. Croce Emerging role of miR-106b-25/miR-17-92 clusters in the control of transforming growth factor beta signaling Cancer Res 68 2008 8191 8194
    • (2008) Cancer Res , vol.68 , pp. 8191-8194
    • Petrocca, F.1    Vecchione, A.2    Croce, C.M.3
  • 67
    • 36048958883 scopus 로고    scopus 로고
    • Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins
    • A. Shiohama, T. Sasaki, S. Noda, S. Minoshima, and N. Shimizu Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins Exp Cell Res 313 2007 4196 4207
    • (2007) Exp Cell Res , vol.313 , pp. 4196-4207
    • Shiohama, A.1    Sasaki, T.2    Noda, S.3    Minoshima, S.4    Shimizu, N.5
  • 68
    • 67649183172 scopus 로고    scopus 로고
    • Functional association of the microprocessor complex with the spliceosome
    • N. Kataoka, M. Fujita, and M. Ohno Functional association of the microprocessor complex with the spliceosome Mol Cell Biol 29 2009 3243 3254
    • (2009) Mol Cell Biol , vol.29 , pp. 3243-3254
    • Kataoka, N.1    Fujita, M.2    Ohno, M.3
  • 69
    • 84885656908 scopus 로고    scopus 로고
    • The 5′ untranslated region of the serotonin receptor 2C pre-mRNA generates miRNAs and is expressed in non-neuronal cells
    • Z. Zhang, M. Falaleeva, L. Agranat-Tamur, A.P. Pages, E.E. Eyras, and J. Sperling The 5′ untranslated region of the serotonin receptor 2C pre-mRNA generates miRNAs and is expressed in non-neuronal cells Exp Brain Res 230 2013 387 394
    • (2013) Exp Brain Res , vol.230 , pp. 387-394
    • Zhang, Z.1    Falaleeva, M.2    Agranat-Tamur, L.3    Pages, A.P.4    Eyras, E.E.5    Sperling, J.6
  • 70
    • 0028176806 scopus 로고
    • Distribution of the serotonin 5-HT2 receptor family mRNAs: Comparison between 5-HT2A and 5-HT2C receptors
    • M. Pompeiano, J.M. Palacios, and G. Mengod Distribution of the serotonin 5-HT2 receptor family mRNAs: comparison between 5-HT2A and 5-HT2C receptors Brain Res 23 1994 163 178
    • (1994) Brain Res , vol.23 , pp. 163-178
    • Pompeiano, M.1    Palacios, J.M.2    Mengod, G.3
  • 71
  • 72
    • 2442694425 scopus 로고    scopus 로고
    • Transcriptome and genome conservation of alternative splicing events in humans and mice
    • C.W. Sugnet, W.J. Kent, M. Ares Jr., and D. Haussler Transcriptome and genome conservation of alternative splicing events in humans and mice Pac Symp Biocomput 66-77 2004
    • (2004) Pac Symp Biocomput , vol.66-77
    • Sugnet, C.W.1    Kent, W.J.2    Ares, Jr.M.3    Haussler, D.4
  • 74
    • 84888617099 scopus 로고    scopus 로고
    • Organizing principles of mammalian nonsense-mediated mRNA decay
    • M.W. Popp, and L.E. Maquat Organizing principles of mammalian nonsense-mediated mRNA decay Annu Rev Genet 47 2013 139 165
    • (2013) Annu Rev Genet , vol.47 , pp. 139-165
    • Popp, M.W.1    Maquat, L.E.2
  • 76
    • 34249870085 scopus 로고    scopus 로고
    • MRNA quality control: An ancient machinery recognizes and degrades mRNAs with nonsense codons
    • I. Behm-Ansmant, I. Kashima, J. Rehwinkel, J. Sauliere, N. Wittkopp, and E. Izaurralde mRNA quality control: an ancient machinery recognizes and degrades mRNAs with nonsense codons FEBS Lett 581 2007 2845 2853
    • (2007) FEBS Lett , vol.581 , pp. 2845-2853
    • Behm-Ansmant, I.1    Kashima, I.2    Rehwinkel, J.3    Sauliere, J.4    Wittkopp, N.5    Izaurralde, E.6
  • 77
    • 34247197937 scopus 로고    scopus 로고
    • The nonsense-mediated decay RNA surveillance pathway
    • Y.F. Chang, J.S. Imam, and M.F. Wilkinson The nonsense-mediated decay RNA surveillance pathway Annu Rev Biochem 76 2007 51 74
    • (2007) Annu Rev Biochem , vol.76 , pp. 51-74
    • Chang, Y.F.1    Imam, J.S.2    Wilkinson, M.F.3
  • 78
    • 77949904260 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in human cells: Mechanistic insights, functions beyond quality control and the double-life of NMD factors
    • P. Nicholson, H. Yepiskoposyan, S. Metze, R. Zamudio Orozco, N. Kleinschmidt, and O. Muhlemann Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors Cell Mol Life Sci 67 2010 677 700
    • (2010) Cell Mol Life Sci , vol.67 , pp. 677-700
    • Nicholson, P.1    Yepiskoposyan, H.2    Metze, S.3    Zamudio Orozco, R.4    Kleinschmidt, N.5    Muhlemann, O.6
  • 80
    • 7044227587 scopus 로고    scopus 로고
    • Stop codon-mediated suppression of splicing is a novel nuclear scanning mechanism not affected by elements of protein synthesis and NMD
    • C. Wachtel, B. Li, J. Sperling, and R. Sperling Stop codon-mediated suppression of splicing is a novel nuclear scanning mechanism not affected by elements of protein synthesis and NMD RNA 10 2004 1740 1750
    • (2004) RNA , vol.10 , pp. 1740-1750
    • Wachtel, C.1    Li, B.2    Sperling, J.3    Sperling, R.4
  • 81
    • 33746835444 scopus 로고    scopus 로고
    • AUG sequences are required to sustain nonsense-codon-mediated suppression of splicing
    • E. Kamhi, G. Yahalom, G. Kass, Y. Hacham, R. Sperling, and J. Sperling AUG sequences are required to sustain nonsense-codon-mediated suppression of splicing Nucleic Acids Res 34 2006 3421 3433
    • (2006) Nucleic Acids Res , vol.34 , pp. 3421-3433
    • Kamhi, E.1    Yahalom, G.2    Kass, G.3    Hacham, Y.4    Sperling, R.5    Sperling, J.6
  • 82
    • 1842682946 scopus 로고    scopus 로고
    • The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
    • S.Y. Chiu, F. Lejeune, A.C. Ranganathan, and L.E. Maquat The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex Genes Dev 18 2004 745 754
    • (2004) Genes Dev , vol.18 , pp. 745-754
    • Chiu, S.Y.1    Lejeune, F.2    Ranganathan, A.C.3    Maquat, L.E.4
  • 83
    • 0037064145 scopus 로고    scopus 로고
    • Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts
    • J.T. Mendell, C.M.J. ap Rhys, and H.C. Dietz Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts Science 298 2002 419 422
    • (2002) Science , vol.298 , pp. 419-422
    • Mendell, J.T.1    Ap Rhys, C.M.J.2    Dietz, H.C.3
  • 84
    • 25844512736 scopus 로고    scopus 로고
    • Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements
    • N.H. Gehring, J.B. Kunz, G. Neu-Yilik, S. Breit, M.H. Viegas, and M.W. Hentze Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements Mol Cell 20 2005 65 75
    • (2005) Mol Cell , vol.20 , pp. 65-75
    • Gehring, N.H.1    Kunz, J.B.2    Neu-Yilik, G.3    Breit, S.4    Viegas, M.H.5    Hentze, M.W.6
  • 86
    • 34948854852 scopus 로고    scopus 로고
    • Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA
    • D. Matsuda, N. Hosoda, Y.K. Kim, and L.E. Maquat Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA Nat Struct Mol Biol 14 2007 974 979
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 974-979
    • Matsuda, D.1    Hosoda, N.2    Kim, Y.K.3    Maquat, L.E.4
  • 87
    • 77954948738 scopus 로고    scopus 로고
    • A potential role for initiator-tRNA in pre-mRNA splicing regulation
    • E. Kamhi, O. Raitskin, R. Sperling, and J. Sperling A potential role for initiator-tRNA in pre-mRNA splicing regulation Proc Natl Acad Sci U S A 107 2010 11319 11324
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11319-11324
    • Kamhi, E.1    Raitskin, O.2    Sperling, R.3    Sperling, J.4
  • 88
    • 57349162135 scopus 로고    scopus 로고
    • Nuclear surveillance of RNA polymerase II transcripts
    • J. Sperling, and R. Sperling Nuclear surveillance of RNA polymerase II transcripts RNA Biol 5 2008 220 224
    • (2008) RNA Biol , vol.5 , pp. 220-224
    • Sperling, J.1    Sperling, R.2
  • 90
    • 15844406352 scopus 로고    scopus 로고
    • Nonsense mutations inhibit RNA splicing in a cell-free system: Recognition of mutant codon is independent of protein synthesis
    • S. Aoufouchi, J. Yelamos, and C. Milstein Nonsense mutations inhibit RNA splicing in a cell-free system: recognition of mutant codon is independent of protein synthesis Cell 85 1996 415 422
    • (1996) Cell , vol.85 , pp. 415-422
    • Aoufouchi, S.1    Yelamos, J.2    Milstein, C.3
  • 91
    • 0033529631 scopus 로고    scopus 로고
    • A premature termination codon in either exon of minute virus of mice P4 promoter-generated pre-mRNA can inhibit nuclear splicing of the intervening intron in an open reading frame-dependent manner
    • A. Gersappe, L. Burger, and D.J. Pintel A premature termination codon in either exon of minute virus of mice P4 promoter-generated pre-mRNA can inhibit nuclear splicing of the intervening intron in an open reading frame-dependent manner J Biol Chem 274 1999 22452 22458
    • (1999) J Biol Chem , vol.274 , pp. 22452-22458
    • Gersappe, A.1    Burger, L.2    Pintel, D.J.3
  • 92
    • 81755161588 scopus 로고    scopus 로고
    • Cotranscriptional effect of a premature termination codon revealed by live-cell imaging
    • V. de Turris, P. Nicholson, R.Z. Orozco, R.H. Singer, and O. Mühlemann Cotranscriptional effect of a premature termination codon revealed by live-cell imaging RNA 17 2011 2094 2107
    • (2011) RNA , vol.17 , pp. 2094-2107
    • De Turris, V.1    Nicholson, P.2    Orozco, R.Z.3    Singer, R.H.4    Mühlemann, O.5
  • 93
    • 33749672830 scopus 로고    scopus 로고
    • Organization of core spliceosomal components U5 snRNA loop i and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy
    • B. Sander, M.M. Golas, E.M. Makarov, H. Brahms, B. Kastner, and R. Luhrmann Organization of core spliceosomal components U5 snRNA loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy Mol Cell 24 2006 267 278
    • (2006) Mol Cell , vol.24 , pp. 267-278
    • Sander, B.1    Golas, M.M.2    Makarov, E.M.3    Brahms, H.4    Kastner, B.5    Luhrmann, R.6
  • 95
    • 42449161413 scopus 로고    scopus 로고
    • The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact in the cell nucleus
    • L. Agranat, O. Raitskin, J. Sperling, and R. Sperling The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact in the cell nucleus Proc Natl Acad Sci U S A 105 2008 5028 5033
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5028-5033
    • Agranat, L.1    Raitskin, O.2    Sperling, J.3    Sperling, R.4
  • 96
    • 77953746618 scopus 로고    scopus 로고
    • A novel tissue-specific alternatively spliced form of the A-to-I RNA editing enzyme ADAR2
    • L. Agranat, J. Sperling, and R. Sperling A novel tissue-specific alternatively spliced form of the A-to-I RNA editing enzyme ADAR2 RNA Biol 7 2010 253 262
    • (2010) RNA Biol , vol.7 , pp. 253-262
    • Agranat, L.1    Sperling, J.2    Sperling, R.3
  • 98
    • 0022468756 scopus 로고
    • U1, U2 and U6 small nuclear ribonucleoprtoeins (snRNPs) are associated with large nuclear RNP particles containing transcripts of an amplified gene in vivo
    • R. Sperling, P. Spann, D. Offen, and J. Sperling U1, U2 and U6 small nuclear ribonucleoprtoeins (snRNPs) are associated with large nuclear RNP particles containing transcripts of an amplified gene in vivo Proc Natl Acad Sci U S A 83 1986 6721 6725
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 6721-6725
    • Sperling, R.1    Spann, P.2    Offen, D.3    Sperling, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.