메뉴 건너뛰기




Volumn 136, Issue 4, 2009, Pages 701-718

The Spliceosome: Design Principles of a Dynamic RNP Machine

Author keywords

[No Author keywords available]

Indexed keywords

CIS ACTING ELEMENT; ENZYME; MESSENGER RNA; MESSENGER RNA PRECURSOR; PROTEIN; PROTEIN SUBUNIT; RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; TELOMERASE;

EID: 60349104299     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2009.02.009     Document Type: Review
Times cited : (2038)

References (138)
  • 1
    • 57149111020 scopus 로고    scopus 로고
    • Is the spliceosome a ribonucleoprotein enzyme?
    • Abelson J. Is the spliceosome a ribonucleoprotein enzyme?. Nat. Struct. Mol. Biol. 15 (2008) 1235-1237
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1235-1237
    • Abelson, J.1
  • 2
    • 0031741144 scopus 로고    scopus 로고
    • The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein
    • Achsel T., Ahrens K., Brahms H., Teigelkamp S., and Lührmann R. The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein. Mol. Cell. Biol. 18 (1998) 6756-6766
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6756-6766
    • Achsel, T.1    Ahrens, K.2    Brahms, H.3    Teigelkamp, S.4    Lührmann, R.5
  • 3
    • 0033569743 scopus 로고    scopus 로고
    • A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′- end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro
    • Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., and Lührmann R. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′- end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J. 18 (1999) 5789-5802
    • (1999) EMBO J. , vol.18 , pp. 5789-5802
    • Achsel, T.1    Brahms, H.2    Kastner, B.3    Bachi, A.4    Wilm, M.5    Lührmann, R.6
  • 4
    • 0034405427 scopus 로고    scopus 로고
    • Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry
    • Ajuh P., Kuster B., Panov K., Zomerdijk J.C., Mann M., and Lamond A.I. Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry. EMBO J. 19 (2000) 6569-6581
    • (2000) EMBO J. , vol.19 , pp. 6569-6581
    • Ajuh, P.1    Kuster, B.2    Panov, K.3    Zomerdijk, J.C.4    Mann, M.5    Lamond, A.I.6
  • 5
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • Alber F., Forster F., Korkin D., Topf M., and Sali A. Integrating diverse data for structure determination of macromolecular assemblies. Annu. Rev. Biochem. 77 (2008) 443-477
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 443-477
    • Alber, F.1    Forster, F.2    Korkin, D.3    Topf, M.4    Sali, A.5
  • 6
    • 0030671163 scopus 로고    scopus 로고
    • Prp43: An RNA helicase-like factor involved in spliceosome disassembly
    • Arenas J.E., and Abelson J.N. Prp43: An RNA helicase-like factor involved in spliceosome disassembly. Proc. Natl. Acad. Sci. USA 94 (1997) 11798-11802
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 7
    • 0036747295 scopus 로고    scopus 로고
    • The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome
    • Bartels C., Klatt C., Lührmann R., and Fabrizio P. The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome. EMBO Rep. 3 (2002) 875-880
    • (2002) EMBO Rep. , vol.3 , pp. 875-880
    • Bartels, C.1    Klatt, C.2    Lührmann, R.3    Fabrizio, P.4
  • 9
    • 31044444461 scopus 로고    scopus 로고
    • Ubiquitin binding by a variant Jab1/MPN domain in the essential pre-mRNA splicing factor Prp8p
    • Bellare P., Kutach A.K., Rines A.K., Guthrie C., and Sontheimer E.J. Ubiquitin binding by a variant Jab1/MPN domain in the essential pre-mRNA splicing factor Prp8p. RNA 12 (2006) 292-302
    • (2006) RNA , vol.12 , pp. 292-302
    • Bellare, P.1    Kutach, A.K.2    Rines, A.K.3    Guthrie, C.4    Sontheimer, E.J.5
  • 11
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget S.M. Exon recognition in vertebrate splicing. J. Biol. Chem. 270 (1995) 2411-2414
    • (1995) J. Biol. Chem. , vol.270 , pp. 2411-2414
    • Berget, S.M.1
  • 12
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer M., and Rodnina M.V. The ribosomal peptidyl transferase. Mol. Cell 26 (2007) 311-321
    • (2007) Mol. Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 13
    • 42249093677 scopus 로고    scopus 로고
    • Isolation of an active step I spliceosome and composition of its RNP core
    • Bessonov S., Anokhina M., Will C.L., Urlaub H., and Lührmann R. Isolation of an active step I spliceosome and composition of its RNP core. Nature 452 (2008) 846-850
    • (2008) Nature , vol.452 , pp. 846-850
    • Bessonov, S.1    Anokhina, M.2    Will, C.L.3    Urlaub, H.4    Lührmann, R.5
  • 14
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black D.L. Mechanisms of alternative pre-messenger RNA splicing. Annu. Rev. Biochem. 72 (2003) 291-336
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 291-336
    • Black, D.L.1
  • 15
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: new insights from global analyses
    • Blencowe B.J. Alternative splicing: new insights from global analyses. Cell 126 (2006) 37-47
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 16
    • 53149145051 scopus 로고    scopus 로고
    • RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition
    • Bonnal S., Martinez C., Forch P., Bachi A., Wilm M., and Valcarcel J. RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition. Mol. Cell 32 (2008) 81-95
    • (2008) Mol. Cell , vol.32 , pp. 81-95
    • Bonnal, S.1    Martinez, C.2    Forch, P.3    Bachi, A.4    Wilm, M.5    Valcarcel, J.6
  • 17
    • 0037200062 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1
    • Boudrez A., Beullens M., Waelkens E., Stalmans W., and Bollen M. Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1. J. Biol. Chem. 277 (2002) 31834-31841
    • (2002) J. Biol. Chem. , vol.277 , pp. 31834-31841
    • Boudrez, A.1    Beullens, M.2    Waelkens, E.3    Stalmans, W.4    Bollen, M.5
  • 18
    • 57749186870 scopus 로고    scopus 로고
    • Spliceosomal cleavage generates the 3′ end of telomerase RNA
    • Box J.A., Bunch J.T., Tang W., and Baumann P. Spliceosomal cleavage generates the 3′ end of telomerase RNA. Nature 456 (2008) 910-914
    • (2008) Nature , vol.456 , pp. 910-914
    • Box, J.A.1    Bunch, J.T.2    Tang, W.3    Baumann, P.4
  • 19
    • 0036948420 scopus 로고    scopus 로고
    • Allosteric cascade of spliceosome activation
    • Brow D.A. 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
  • 20
    • 0001468848 scopus 로고    scopus 로고
    • Splicing of precursors to mRNAs by the spliceosomes
    • Gesteland R.F., Cech T.R., and Atkins J.F. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Burge C.B., Tuschl T., and Sharp P.A. Splicing of precursors to mRNAs by the spliceosomes. In: Gesteland R.F., Cech T.R., and Atkins J.F. (Eds). The RNA world. Second Edition (1999), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 525-560
    • (1999) The RNA world. Second Edition , pp. 525-560
    • Burge, C.B.1    Tuschl, T.2    Sharp, P.A.3
  • 21
    • 0025233806 scopus 로고
    • A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing
    • Burgess S., Couto J.R., and Guthrie C. A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing. Cell 60 (1990) 705-717
    • (1990) Cell , vol.60 , pp. 705-717
    • Burgess, S.1    Couto, J.R.2    Guthrie, C.3
  • 22
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres J.F., Stamm S., Helfman D.M., and Krainer A.R. Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265 (1994) 1706-1709
    • (1994) Science , vol.265 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 23
    • 0036207384 scopus 로고    scopus 로고
    • Listening to silence and understanding nonsense: exonic mutations that affect splicing
    • Cartegni L., Chew S.L., and Krainer A.R. Listening to silence and understanding nonsense: exonic mutations that affect splicing. Nat. Rev. Genet. 3 (2002) 285-298
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 285-298
    • Cartegni, L.1    Chew, S.L.2    Krainer, A.R.3
  • 24
    • 33747488951 scopus 로고    scopus 로고
    • The SF3b155 N-terminal domain is a scaffold important for splicing
    • Cass D.M., and Berglund J.A. The SF3b155 N-terminal domain is a scaffold important for splicing. Biochemistry 45 (2006) 10092-10101
    • (2006) Biochemistry , vol.45 , pp. 10092-10101
    • Cass, D.M.1    Berglund, J.A.2
  • 25
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan S.P., Kao D.I., Tsai W.Y., and Cheng S.C. The Prp19p-associated complex in spliceosome activation. Science 302 (2003) 279-282
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.P.1    Kao, D.I.2    Tsai, W.Y.3    Cheng, S.C.4
  • 27
    • 0033545859 scopus 로고    scopus 로고
    • Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing
    • Chen H.R., Tsao T.Y., Chen C.H., Tsai W.Y., Her L.S., Hsu M.M., and Cheng S.C. Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing. Proc. Natl. Acad. Sci. USA 96 (1999) 5406-5411
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5406-5411
    • Chen, H.R.1    Tsao, T.Y.2    Chen, C.H.3    Tsai, W.Y.4    Her, L.S.5    Hsu, M.M.6    Cheng, S.C.7
  • 28
    • 0037012922 scopus 로고    scopus 로고
    • Genomewide analysis of mRNA processing in yeast using splicing-specific microarrays
    • Clark T.A., Sugnet C.W., and Ares Jr. M. Genomewide analysis of mRNA processing in yeast using splicing-specific microarrays. Science 296 (2002) 907-910
    • (2002) Science , vol.296 , pp. 907-910
    • Clark, T.A.1    Sugnet, C.W.2    Ares Jr., M.3
  • 29
    • 38049077956 scopus 로고    scopus 로고
    • Visualizing the splicing of single pre-mRNA molecules in whole cell extract
    • Crawford D.J., Hoskins A.A., Friedman L.J., Gelles J., and Moore M.J. Visualizing the splicing of single pre-mRNA molecules in whole cell extract. RNA 14 (2008) 170-179
    • (2008) RNA , vol.14 , pp. 170-179
    • Crawford, D.J.1    Hoskins, A.A.2    Friedman, L.J.3    Gelles, J.4    Moore, M.J.5
  • 30
    • 33745860086 scopus 로고    scopus 로고
    • Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions
    • Deckert J., Hartmuth K., Boehringer D., Behzadnia N., Will C.L., Kastner B., Stark H., Urlaub H., and Lührmann R. Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions. Mol. Cell. Biol. 26 (2006) 5528-5543
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5528-5543
    • Deckert, J.1    Hartmuth, K.2    Boehringer, D.3    Behzadnia, N.4    Will, C.L.5    Kastner, B.6    Stark, H.7    Urlaub, H.8    Lührmann, R.9
  • 31
    • 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
    • Donmez G., Hartmuth K., Kastner B., Will C.L., and Lührmann R. The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes. Mol. Cell 25 (2007) 399-411
    • (2007) Mol. Cell , vol.25 , pp. 399-411
    • Donmez, G.1    Hartmuth, K.2    Kastner, B.3    Will, C.L.4    Lührmann, R.5
  • 32
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 34
    • 0030976931 scopus 로고    scopus 로고
    • An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2
    • Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., and Lührmann R. An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2. EMBO J. 16 (1997) 4092-4106
    • (1997) EMBO J. , vol.16 , pp. 4092-4106
    • Fabrizio, P.1    Laggerbauer, B.2    Lauber, J.3    Lane, W.S.4    Lührmann, R.5
  • 35
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., and Agrawal R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 406 (2000) 318-322
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 36
    • 0038670209 scopus 로고    scopus 로고
    • Molecular architecture of the multiprotein splicing factor SF3b
    • Golas M.M., Sander B., Will C.L., Lührmann R., and Stark H. Molecular architecture of the multiprotein splicing factor SF3b. Science 300 (2003) 980-984
    • (2003) Science , vol.300 , pp. 980-984
    • Golas, M.M.1    Sander, B.2    Will, C.L.3    Lührmann, R.4    Stark, H.5
  • 37
    • 0030044836 scopus 로고    scopus 로고
    • Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A
    • Gozani O., Feld R., and Reed R. Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A. Genes Dev. 10 (1996) 233-243
    • (1996) Genes Dev. , vol.10 , pp. 233-243
    • Gozani, O.1    Feld, R.2    Reed, R.3
  • 38
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site
    • Gozani O., Potashkin J., and Reed R. A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. Mol. Cell. Biol. 18 (1998) 4752-4760
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 39
    • 17844395704 scopus 로고    scopus 로고
    • Prp8 protein: at the heart of the spliceosome
    • Grainger R.J., and Beggs J.D. Prp8 protein: at the heart of the spliceosome. RNA 11 (2005) 533-557
    • (2005) RNA , vol.11 , pp. 533-557
    • Grainger, R.J.1    Beggs, J.D.2
  • 40
    • 0035252410 scopus 로고    scopus 로고
    • Alternative splicing: increasing diversity in the proteomic world
    • Graveley B.R. Alternative splicing: increasing diversity in the proteomic world. Trends Genet. 17 (2001) 100-107
    • (2001) Trends Genet. , vol.17 , pp. 100-107
    • Graveley, B.R.1
  • 42
    • 39149083341 scopus 로고    scopus 로고
    • Control of pre-mRNA splicing by the general splicing factors PUF60 and U2AF65
    • 10.1371/journal.pone.0000538
    • Hastings M.L., Allemand E., Duelli D.M., Myers M.P., and Krainer A.R. Control of pre-mRNA splicing by the general splicing factors PUF60 and U2AF65. PLoS ONE 2 (2007) e538 10.1371/journal.pone.0000538
    • (2007) PLoS ONE , vol.2
    • Hastings, M.L.1    Allemand, E.2    Duelli, D.M.3    Myers, M.P.4    Krainer, A.R.5
  • 43
    • 58149475699 scopus 로고    scopus 로고
    • Conservation of the protein composition and electron microscopy structure of Drosophila melanogaster and human spliceosomal complexes
    • Herold N., Will C.L., Wolf E., Kastner B., Urlaub H., and Lührmann R. Conservation of the protein composition and electron microscopy structure of Drosophila melanogaster and human spliceosomal complexes. Mol. Cell. Biol. 29 (2009) 281-301
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 281-301
    • Herold, N.1    Will, C.L.2    Wolf, E.3    Kastner, B.4    Urlaub, H.5    Lührmann, R.6
  • 44
    • 2442661481 scopus 로고    scopus 로고
    • Multiple functions for the invariant AGC triad of U6 snRNA
    • Hilliker A.K., and Staley J.P. Multiple functions for the invariant AGC triad of U6 snRNA. RNA 10 (2004) 921-928
    • (2004) RNA , vol.10 , pp. 921-928
    • Hilliker, A.K.1    Staley, J.P.2
  • 45
    • 37549029268 scopus 로고    scopus 로고
    • Structure-function relationships in RNA and RNP enzymes: recent advances
    • Hoogstraten C.G., and Sumita M. Structure-function relationships in RNA and RNP enzymes: recent advances. Biopolymers 87 (2007) 317-328
    • (2007) Biopolymers , vol.87 , pp. 317-328
    • Hoogstraten, C.G.1    Sumita, M.2
  • 46
    • 0036470544 scopus 로고    scopus 로고
    • A cyclophilin functions in pre-mRNA splicing
    • Horowitz D.S., Lee E.J., Mabon S.A., and Misteli T. A cyclophilin functions in pre-mRNA splicing. EMBO J. 21 (2002) 470-480
    • (2002) EMBO J. , vol.21 , pp. 470-480
    • Horowitz, D.S.1    Lee, E.J.2    Mabon, S.A.3    Misteli, T.4
  • 47
    • 33749515475 scopus 로고    scopus 로고
    • An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition
    • House A.E., and Lynch K.W. An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition. Nat. Struct. Mol. Biol. 13 (2006) 937-944
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 937-944
    • House, A.E.1    Lynch, K.W.2
  • 48
    • 0035256812 scopus 로고    scopus 로고
    • The 100-kda U5 snRNP protein (hPrp28p) contacts the 5′ splice site through its ATPase site
    • Ismaili N., Sha M., Gustafson E.H., and Konarska M.M. The 100-kda U5 snRNP protein (hPrp28p) contacts the 5′ splice site through its ATPase site. RNA 7 (2001) 182-193
    • (2001) RNA , vol.7 , pp. 182-193
    • Ismaili, N.1    Sha, M.2    Gustafson, E.H.3    Konarska, M.M.4
  • 49
    • 33745618668 scopus 로고    scopus 로고
    • A simple principle to explain the evolution of pre-mRNA splicing
    • Izquierdo J.M., and Valcarcel J. A simple principle to explain the evolution of pre-mRNA splicing. Genes Dev. 20 (2006) 1679-1684
    • (2006) Genes Dev. , vol.20 , pp. 1679-1684
    • Izquierdo, J.M.1    Valcarcel, J.2
  • 50
    • 37249014572 scopus 로고    scopus 로고
    • Searching for a wrench to throw into the splicing machine
    • Jurica M.S. Searching for a wrench to throw into the splicing machine. Nat. Chem. Biol. 4 (2008) 3-6
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 3-6
    • Jurica, M.S.1
  • 51
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: awash in a sea of proteins
    • Jurica M.S., and Moore M.J. Pre-mRNA splicing: awash in a sea of proteins. Mol. Cell 12 (2003) 5-14
    • (2003) Mol. Cell , vol.12 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 52
    • 0036242097 scopus 로고    scopus 로고
    • Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis
    • Jurica M.S., Licklider L.J., Gygi S.R., Grigorieff N., and Moore M.J. Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA 8 (2002) 426-439
    • (2002) RNA , vol.8 , pp. 426-439
    • Jurica, M.S.1    Licklider, L.J.2    Gygi, S.R.3    Grigorieff, N.4    Moore, M.J.5
  • 53
    • 0036315512 scopus 로고    scopus 로고
    • Early organization of pre-mRNA during spliceosome assembly
    • Kent O.A., and MacMillan A.M. Early organization of pre-mRNA during spliceosome assembly. Nat. Struct. Biol. 9 (2002) 576-581
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 576-581
    • Kent, O.A.1    MacMillan, A.M.2
  • 54
    • 0029965552 scopus 로고    scopus 로고
    • Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing
    • Kim S.H., and Lin R.J. Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing. Mol. Cell. Biol. 16 (1996) 6810-6819
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6810-6819
    • Kim, S.H.1    Lin, R.J.2
  • 55
    • 25844443478 scopus 로고    scopus 로고
    • Insights into the mechanisms of splicing: more lessons from the ribosome
    • Konarska M.M., and Query C.C. Insights into the mechanisms of splicing: more lessons from the ribosome. Genes Dev. 19 (2005) 2255-2260
    • (2005) Genes Dev. , vol.19 , pp. 2255-2260
    • Konarska, M.M.1    Query, C.C.2
  • 56
    • 32444443532 scopus 로고    scopus 로고
    • Repositioning of the reaction intermediate within the catalytic center of the spliceosome
    • Konarska M.M., Vilardell J., and Query C.C. Repositioning of the reaction intermediate within the catalytic center of the spliceosome. Mol. Cell 21 (2006) 543-553
    • (2006) Mol. Cell , vol.21 , pp. 543-553
    • Konarska, M.M.1    Vilardell, J.2    Query, C.C.3
  • 58
    • 56849100744 scopus 로고    scopus 로고
    • A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding yeast
    • Kress T.L., Krogan N.J., and Guthrie C. A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding yeast. Mol. Cell 32 (2008) 727-734
    • (2008) Mol. Cell , vol.32 , pp. 727-734
    • Kress, T.L.1    Krogan, N.J.2    Guthrie, C.3
  • 59
    • 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 Lührmann R. Stalling of spliceosome assembly at distinct stages by small-molecule inhibitors of protein acetylation and deacetylation. RNA 15 (2009) 153-175
    • (2009) RNA , vol.15 , pp. 153-175
    • Kuhn, A.N.1    van Santen, M.A.2    Schwienhorst, A.3    Urlaub, H.4    Lührmann, R.5
  • 60
    • 0037013146 scopus 로고    scopus 로고
    • Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45
    • Lallena M.J., Chalmers K.J., Llamazares S., Lamond A.I., and Valcarcel J. Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45. Cell 109 (2002) 285-296
    • (2002) Cell , vol.109 , pp. 285-296
    • Lallena, M.J.1    Chalmers, K.J.2    Llamazares, S.3    Lamond, A.I.4    Valcarcel, J.5
  • 61
    • 33745613530 scopus 로고    scopus 로고
    • The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP
    • Liu S., Rauhut R., Vornlocher H.P., and Lührmann R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA 12 (2006) 1418-1430
    • (2006) RNA , vol.12 , pp. 1418-1430
    • Liu, S.1    Rauhut, R.2    Vornlocher, H.P.3    Lührmann, R.4
  • 63
    • 0036315396 scopus 로고    scopus 로고
    • p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5′ splice site duplex
    • Liu Z.R. p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5′ splice site duplex. Mol. Cell. Biol. 22 (2002) 5443-5450
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5443-5450
    • Liu, Z.R.1
  • 64
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
    • Lu K.P., and Zhou X.Z. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease. Nat. Rev. Mol. Cell Biol. 8 (2007) 904-916
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 65
    • 24744460822 scopus 로고    scopus 로고
    • Extending the size of protein-RNA complexes studied by nuclear magnetic resonance spectroscopy
    • Mackereth C.D., Simon B., and Sattler M. Extending the size of protein-RNA complexes studied by nuclear magnetic resonance spectroscopy. ChemBioChem 6 (2005) 1578-1584
    • (2005) ChemBioChem , vol.6 , pp. 1578-1584
    • Mackereth, C.D.1    Simon, B.2    Sattler, M.3
  • 66
    • 0026486883 scopus 로고
    • A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome
    • Madhani H.D., and Guthrie C. A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome. Cell 71 (1992) 803-817
    • (1992) Cell , vol.71 , pp. 803-817
    • Madhani, H.D.1    Guthrie, C.2
  • 67
    • 58149231008 scopus 로고    scopus 로고
    • ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8
    • Maeder C., Kutach A.K., and Guthrie C. ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8. Nat. Struct. Mol. Biol. 16 (2009) 42-48
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 42-48
    • Maeder, C.1    Kutach, A.K.2    Guthrie, C.3
  • 68
    • 30344476997 scopus 로고    scopus 로고
    • Protein conformations, interactions, and H/D exchange
    • Maier C.S., and Deinzer M.L. Protein conformations, interactions, and H/D exchange. Methods Enzymol. 402 (2005) 312-360
    • (2005) Methods Enzymol. , vol.402 , pp. 312-360
    • Maier, C.S.1    Deinzer, M.L.2
  • 69
    • 0037073946 scopus 로고    scopus 로고
    • Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome
    • Makarov E.M., Makarova O.V., Urlaub H., Gentzel M., Will C.L., Wilm M., and Lührmann R. Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome. Science 298 (2002) 2205-2208
    • (2002) Science , vol.298 , pp. 2205-2208
    • Makarov, E.M.1    Makarova, O.V.2    Urlaub, H.3    Gentzel, M.4    Will, C.L.5    Wilm, M.6    Lührmann, R.7
  • 70
    • 3242737496 scopus 로고    scopus 로고
    • A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing
    • Makarova O.V., Makarov E.M., Urlaub H., Will C.L., Gentzel M., Wilm M., and Lührmann R. A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing. EMBO J. 23 (2004) 2381-2391
    • (2004) EMBO J. , vol.23 , pp. 2381-2391
    • Makarova, O.V.1    Makarov, E.M.2    Urlaub, H.3    Will, C.L.4    Gentzel, M.5    Wilm, M.6    Lührmann, R.7
  • 71
    • 0037041395 scopus 로고    scopus 로고
    • An extensive network of coupling among gene expression machines
    • Maniatis T., and Reed R. An extensive network of coupling among gene expression machines. Nature 416 (2002) 499-506
    • (2002) Nature , vol.416 , pp. 499-506
    • Maniatis, T.1    Reed, R.2
  • 72
    • 43249109907 scopus 로고    scopus 로고
    • Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome
    • Mathew R., Hartmuth K., Mohlmann S., Urlaub H., Ficner R., and Lührmann R. Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome. Nat. Struct. Mol. Biol. 15 (2008) 435-443
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 435-443
    • Mathew, R.1    Hartmuth, K.2    Mohlmann, S.3    Urlaub, H.4    Ficner, R.5    Lührmann, R.6
  • 73
    • 33744937919 scopus 로고    scopus 로고
    • Exon ligation is proofread by the DExD/H-box ATPase Prp22p
    • Mayas R.M., Maita H., and Staley J.P. Exon ligation is proofread by the DExD/H-box ATPase Prp22p. Nat. Struct. Mol. Biol. 13 (2006) 482-490
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 482-490
    • Mayas, R.M.1    Maita, H.2    Staley, J.P.3
  • 74
    • 0033517098 scopus 로고    scopus 로고
    • Characterization of Sm-like proteins in yeast and their association with U6 snRNA
    • Mayes A.E., Verdone L., Legrain P., and Beggs J.D. Characterization of Sm-like proteins in yeast and their association with U6 snRNA. EMBO J. 18 (1999) 4321-4331
    • (1999) EMBO J. , vol.18 , pp. 4321-4331
    • Mayes, A.E.1    Verdone, L.2    Legrain, P.3    Beggs, J.D.4
  • 75
    • 34250860714 scopus 로고    scopus 로고
    • Enzymes catalyzing protein folding and their cellular functions
    • Nagradova N. Enzymes catalyzing protein folding and their cellular functions. Curr. Protein Pept. Sci. 8 (2007) 273-282
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 273-282
    • Nagradova, N.1
  • 76
    • 0002340095 scopus 로고    scopus 로고
    • RNA-RNA interactions in nuclear pre-mRNA splicing
    • Simons R.W., and Grunberg-Manago M. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Nilsen T.W. RNA-RNA interactions in nuclear pre-mRNA splicing. In: Simons R.W., and Grunberg-Manago M. (Eds). RNA structure and function (1998), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 279-308
    • (1998) RNA structure and function , pp. 279-308
    • Nilsen, T.W.1
  • 77
    • 23644432376 scopus 로고    scopus 로고
    • The splicing machinery is a genetic modifier of disease severity
    • Nissim-Rafinia M., and Kerem B. The splicing machinery is a genetic modifier of disease severity. Trends Genet. 21 (2005) 480-483
    • (2005) Trends Genet. , vol.21 , pp. 480-483
    • Nissim-Rafinia, M.1    Kerem, B.2
  • 78
    • 0033229873 scopus 로고    scopus 로고
    • Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5′ stem-loop of U4 snRNA
    • Nottrott S., Hartmuth K., Fabrizio P., Urlaub H., Vidovic I., Ficner R., and Lührmann R. Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5′ stem-loop of U4 snRNA. EMBO J. 18 (1999) 6119-6133
    • (1999) EMBO J. , vol.18 , pp. 6119-6133
    • Nottrott, S.1    Hartmuth, K.2    Fabrizio, P.3    Urlaub, H.4    Vidovic, I.5    Ficner, R.6    Lührmann, R.7
  • 80
    • 0036118353 scopus 로고    scopus 로고
    • Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs
    • Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., and Gould K.L. Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. Mol. Cell. Biol. 22 (2002) 2011-2024
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2011-2024
    • Ohi, M.D.1    Link, A.J.2    Ren, L.3    Jennings, J.L.4    McDonald, W.H.5    Gould, K.L.6
  • 82
    • 0345169036 scopus 로고    scopus 로고
    • Splicing double:Insights from the second spliceosome
    • Patel A.A., and Steitz J.A. Splicing double:Insights from the second spliceosome. Nat. Rev. Mol. Cell Biol. 4 (2003) 960-970
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 960-970
    • Patel, A.A.1    Steitz, J.A.2
  • 83
    • 33847053558 scopus 로고    scopus 로고
    • Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa
    • Pena V., Liu S., Bujnicki J.M., Lührmann R., and Wahl M.C. Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa. Mol. Cell 25 (2007) 615-624
    • (2007) Mol. Cell , vol.25 , pp. 615-624
    • Pena, V.1    Liu, S.2    Bujnicki, J.M.3    Lührmann, R.4    Wahl, M.C.5
  • 84
    • 55549143970 scopus 로고    scopus 로고
    • Structure and function of an RNase H domain at the heart of the spliceosome
    • Pena V., Rozov A., Fabrizio P., Lührmann R., and Wahl M.C. Structure and function of an RNase H domain at the heart of the spliceosome. EMBO J. 27 (2008) 2929-2940
    • (2008) EMBO J. , vol.27 , pp. 2929-2940
    • Pena, V.1    Rozov, A.2    Fabrizio, P.3    Lührmann, R.4    Wahl, M.C.5
  • 85
    • 34247255773 scopus 로고    scopus 로고
    • Transcript specificity in yeast pre-mRNA splicing revealed by mutations in core spliceosomal components
    • 10.1371/journal.pbio.0050090
    • Pleiss J.A., Whitworth G.B., Bergkessel M., and Guthrie C. Transcript specificity in yeast pre-mRNA splicing revealed by mutations in core spliceosomal components. PLoS Biol. 5 (2007) e90 10.1371/journal.pbio.0050090
    • (2007) PLoS Biol. , vol.5
    • Pleiss, J.A.1    Whitworth, G.B.2    Bergkessel, M.3    Guthrie, C.4
  • 86
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle A.M. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. Biomol. Struct. 37 (2008) 317-336
    • (2008) Annu. Rev. Biophys. Biomol. Struct. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 87
    • 2342522014 scopus 로고    scopus 로고
    • Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants
    • Query C.C., and Konarska M.M. Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants. Mol. Cell 14 (2004) 343-354
    • (2004) Mol. Cell , vol.14 , pp. 343-354
    • Query, C.C.1    Konarska, M.M.2
  • 88
    • 0037224514 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J., Ryder U., Lamond A.I., and Mann M. Large-scale proteomic analysis of the human spliceosome. Genome Res. 12 (2002) 1231-1245
    • (2002) Genome Res. , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 89
    • 0037823485 scopus 로고    scopus 로고
    • Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide
    • Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Lührmann R., and Ficner R. Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J. Mol. Biol. 331 (2003) 45-56
    • (2003) J. Mol. Biol. , vol.331 , pp. 45-56
    • Reidt, U.1    Wahl, M.C.2    Fasshauer, D.3    Horowitz, D.S.4    Lührmann, R.5    Ficner, R.6
  • 90
    • 0029827836 scopus 로고    scopus 로고
    • The canonical GU dinucleotide at the 5′ splice site is recognized by p220 of the U5 snRNP within the spliceosome
    • Reyes J.L., Kois P., Konforti B.B., and Konarska M.M. The canonical GU dinucleotide at the 5′ splice site is recognized by p220 of the U5 snRNP within the spliceosome. RNA 2 (1996) 213-225
    • (1996) RNA , vol.2 , pp. 213-225
    • Reyes, J.L.1    Kois, P.2    Konforti, B.B.3    Konarska, M.M.4
  • 91
    • 33745755054 scopus 로고    scopus 로고
    • Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes
    • Rhode B.M., Hartmuth K., Westhof E., and Lührmann R. Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes. EMBO J. 25 (2006) 2475-2486
    • (2006) EMBO J. , vol.25 , pp. 2475-2486
    • Rhode, B.M.1    Hartmuth, K.2    Westhof, E.3    Lührmann, R.4
  • 93
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina M.V., Savelsbergh A., Katunin V.I., and Wintermeyer W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385 (1997) 37-41
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 94
    • 0029312195 scopus 로고
    • The final stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promote step 1 of splicing
    • Roy J., Kim K., Maddock J.R., Anthony J.G., and Woolford Jr. J.L. The final stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promote step 1 of splicing. RNA 1 (1995) 375-390
    • (1995) RNA , vol.1 , pp. 375-390
    • Roy, J.1    Kim, K.2    Maddock, J.R.3    Anthony, J.G.4    Woolford Jr., J.L.5
  • 96
    • 44949117567 scopus 로고    scopus 로고
    • A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release
    • Schwer B. A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release. Mol. Cell 30 (2008) 743-754
    • (2008) Mol. Cell , vol.30 , pp. 743-754
    • Schwer, B.1
  • 97
    • 0027065506 scopus 로고
    • A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis
    • Schwer B., and Guthrie C. A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis. EMBO J. 11 (1992) 5033-5039
    • (1992) EMBO J. , vol.11 , pp. 5033-5039
    • Schwer, B.1    Guthrie, C.2
  • 99
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T., Nureki O., Nakamura A., Kobayashi S., and Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125 (2006) 287-300
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 100
    • 38849187162 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
    • Sharma S., Kohlstaedt L.A., Damianov A., Rio D.C., and Black D.L. Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nat. Struct. Mol. Biol. 15 (2008) 183-191
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 183-191
    • Sharma, S.1    Kohlstaedt, L.A.2    Damianov, A.3    Rio, D.C.4    Black, D.L.5
  • 101
    • 33748415171 scopus 로고    scopus 로고
    • PP1/PP2A phosphatases are required for the second step of Pre-mRNA splicing and target specific snRNP proteins
    • Shi Y., Reddy B., and Manley J.L. PP1/PP2A phosphatases are required for the second step of Pre-mRNA splicing and target specific snRNP proteins. Mol. Cell 23 (2006) 819-829
    • (2006) Mol. Cell , vol.23 , pp. 819-829
    • Shi, Y.1    Reddy, B.2    Manley, J.L.3
  • 102
    • 38649126163 scopus 로고    scopus 로고
    • Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit
    • Simonovic M., and Steitz T.A. Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit. Proc. Natl. Acad. Sci. USA 105 (2008) 500-505
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 500-505
    • Simonovic, M.1    Steitz, T.A.2
  • 103
    • 26944489645 scopus 로고    scopus 로고
    • Building specificity with nonspecific RNA-binding proteins
    • Singh R., and Valcarcel J. Building specificity with nonspecific RNA-binding proteins. Nat. Struct. Mol. Biol. 12 (2005) 645-653
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 645-653
    • Singh, R.1    Valcarcel, J.2
  • 104
    • 33746441457 scopus 로고    scopus 로고
    • The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase
    • Small E.C., Leggett S.R., Winans A.A., and Staley J.P. The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase. Mol. Cell 23 (2006) 389-399
    • (2006) Mol. Cell , vol.23 , pp. 389-399
    • Small, E.C.1    Leggett, S.R.2    Winans, A.A.3    Staley, J.P.4
  • 105
    • 0034256020 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing: the logic of combinatorial control
    • Smith C.W., and Valcarcel J. Alternative pre-mRNA splicing: the logic of combinatorial control. Trends Biochem. Sci. 25 (2000) 381-388
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 381-388
    • Smith, C.W.1    Valcarcel, J.2
  • 106
    • 44949246374 scopus 로고    scopus 로고
    • "Nought may endure but mutability": spliceosome dynamics and the regulation of splicing
    • Smith D.J., Query C.C., and Konarska M.M. "Nought may endure but mutability": spliceosome dynamics and the regulation of splicing. Mol. Cell 30 (2008) 657-666
    • (2008) Mol. Cell , vol.30 , pp. 657-666
    • Smith, D.J.1    Query, C.C.2    Konarska, M.M.3
  • 107
    • 0030833215 scopus 로고    scopus 로고
    • Metal ion catalysis during splicing of premessenger RNA
    • Sontheimer E.J., Sun S., and Piccirilli J.A. Metal ion catalysis during splicing of premessenger RNA. Nature 388 (1997) 801-805
    • (1997) Nature , vol.388 , pp. 801-805
    • Sontheimer, E.J.1    Sun, S.2    Piccirilli, J.A.3
  • 108
    • 33344463111 scopus 로고    scopus 로고
    • Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing
    • Spadaccini R., Reidt U., Dybkov O., Will C., Frank R., Stier G., Corsini L., Wahl M.C., Lührmann R., and Sattler M. Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing. RNA 12 (2006) 410-425
    • (2006) RNA , vol.12 , pp. 410-425
    • Spadaccini, R.1    Reidt, U.2    Dybkov, O.3    Will, C.4    Frank, R.5    Stier, G.6    Corsini, L.7    Wahl, M.C.8    Lührmann, R.9    Sattler, M.10
  • 109
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley J.P., and Guthrie C. 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
  • 111
  • 112
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz T.A. A structural understanding of the dynamic ribosome machine. Nat. Rev. Mol. Cell Biol. 9 (2008) 242-253
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 114
    • 0028917214 scopus 로고
    • A novel U2-U6 snRNA structure is necessary for mammalian mRNA splicing
    • Sun J.S., and Manley J.L. A novel U2-U6 snRNA structure is necessary for mammalian mRNA splicing. Genes Dev. 9 (1995) 843-854
    • (1995) Genes Dev. , vol.9 , pp. 843-854
    • Sun, J.S.1    Manley, J.L.2
  • 115
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamoto K., and Chance M.R. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 251-276
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 116
    • 2342540912 scopus 로고    scopus 로고
    • The ever-increasing complexities of the exon junction complex
    • Tange T.O., Nott A., and Moore M.J. The ever-increasing complexities of the exon junction complex. Curr. Opin. Cell Biol. 16 (2004) 279-284
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 279-284
    • Tange, T.O.1    Nott, A.2    Moore, M.J.3
  • 117
    • 58149096435 scopus 로고    scopus 로고
    • Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155)
    • Tanuma N., Kim S.E., Beullens M., Tsubaki Y., Mitsuhashi S., Nomura M., Kawamura T., Isono K., Koseki H., Sato M., et al. Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155). J. Biol. Chem. 283 (2008) 35805-35814
    • (2008) J. Biol. Chem. , vol.283 , pp. 35805-35814
    • Tanuma, N.1    Kim, S.E.2    Beullens, M.3    Tsubaki, Y.4    Mitsuhashi, S.5    Nomura, M.6    Kawamura, T.7    Isono, K.8    Koseki, H.9    Sato, M.10
  • 118
    • 41749109563 scopus 로고    scopus 로고
    • Crystal structure of a self-spliced group II intron
    • Toor N., Keating K.S., Taylor S.D., and Pyle A.M. Crystal structure of a self-spliced group II intron. Science 320 (2008) 77-82
    • (2008) Science , vol.320 , pp. 77-82
    • Toor, N.1    Keating, K.S.2    Taylor, S.D.3    Pyle, A.M.4
  • 119
    • 29144515824 scopus 로고    scopus 로고
    • Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2
    • Tsai R.T., Fu R.H., Yeh F.L., Tseng C.K., Lin Y.C., Huang Y.H., and Cheng S.C. Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2. Genes Dev. 19 (2005) 2991-3003
    • (2005) Genes Dev. , vol.19 , pp. 2991-3003
    • Tsai, R.T.1    Fu, R.H.2    Yeh, F.L.3    Tseng, C.K.4    Lin, Y.C.5    Huang, Y.H.6    Cheng, S.C.7
  • 120
    • 46449086933 scopus 로고    scopus 로고
    • Both catalytic steps of nuclear pre-mRNA splicing are reversible
    • Tseng C.K., and Cheng S.C. Both catalytic steps of nuclear pre-mRNA splicing are reversible. Science 320 (2008) 1782-1784
    • (2008) Science , vol.320 , pp. 1782-1784
    • Tseng, C.K.1    Cheng, S.C.2
  • 121
    • 0029397324 scopus 로고
    • The second catalytic step of pre-mRNA splicing
    • Umen J.G., and Guthrie C. The second catalytic step of pre-mRNA splicing. RNA 1 (1995) 869-885
    • (1995) RNA , vol.1 , pp. 869-885
    • Umen, J.G.1    Guthrie, C.2
  • 122
    • 0035909314 scopus 로고    scopus 로고
    • Splicing-related catalysis by protein-free snRNAs
    • Valadkhan S., and Manley J.L. Splicing-related catalysis by protein-free snRNAs. Nature 413 (2001) 701-707
    • (2001) Nature , vol.413 , pp. 701-707
    • Valadkhan, S.1    Manley, J.L.2
  • 123
    • 0030595187 scopus 로고    scopus 로고
    • Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA
    • Valcarcel J., Gaur R.K., Singh R., and Green M.R. Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA. Science 273 (1996) 1706-1709
    • (1996) Science , vol.273 , pp. 1706-1709
    • Valcarcel, J.1    Gaur, R.K.2    Singh, R.3    Green, M.R.4
  • 124
    • 0032523934 scopus 로고    scopus 로고
    • Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis
    • Wang C., Chua K., Seghezzi W., Lees E., Gozani O., and Reed R. Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis. Genes Dev. 12 (1998) 1409-1414
    • (1998) Genes Dev. , vol.12 , pp. 1409-1414
    • Wang, C.1    Chua, K.2    Seghezzi, W.3    Lees, E.4    Gozani, O.5    Reed, R.6
  • 125
    • 34548758543 scopus 로고    scopus 로고
    • Splicing in disease: disruption of the splicing code and the decoding machinery
    • Wang G.S., and Cooper T.A. Splicing in disease: disruption of the splicing code and the decoding machinery. Nat. Rev. Genet. 8 (2007) 749-761
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 749-761
    • Wang, G.S.1    Cooper, T.A.2
  • 126
    • 0027394389 scopus 로고
    • mRNA splicing and autocatalytic introns: distant cousins or the products of chemical determinism?
    • Weiner A.M. mRNA splicing and autocatalytic introns: distant cousins or the products of chemical determinism?. Cell 72 (1993) 161-164
    • (1993) Cell , vol.72 , pp. 161-164
    • Weiner, A.M.1
  • 127
    • 33645213731 scopus 로고    scopus 로고
    • Spliceosome structure and function
    • Gesteland R.F., Cech T.R., and Atkins J.F. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Will C.L., and Lührmann R. Spliceosome structure and function. In: Gesteland R.F., Cech T.R., and Atkins J.F. (Eds). The RNA world. Third Edition (2006), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 369-400
    • (2006) The RNA world. Third Edition , pp. 369-400
    • Will, C.L.1    Lührmann, R.2
  • 129
    • 0032488946 scopus 로고    scopus 로고
    • Molecular movement inside the translational engine
    • Wilson K.S., and Noller H.F. Molecular movement inside the translational engine. Cell 92 (1998) 337-349
    • (1998) Cell , vol.92 , pp. 337-349
    • Wilson, K.S.1    Noller, H.F.2
  • 131
    • 33745633573 scopus 로고    scopus 로고
    • Rapid peptide bond formation on isolated 50S ribosomal subunits
    • Wohlgemuth I., Beringer M., and Rodnina M.V. Rapid peptide bond formation on isolated 50S ribosomal subunits. EMBO Rep. 7 (2006) 699-703
    • (2006) EMBO Rep. , vol.7 , pp. 699-703
    • Wohlgemuth, I.1    Beringer, M.2    Rodnina, M.V.3
  • 132
    • 36749080450 scopus 로고    scopus 로고
    • Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly
    • Xu Y.Z., and Query C.C. Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly. Mol. Cell 28 (2007) 838-849
    • (2007) Mol. Cell , vol.28 , pp. 838-849
    • Xu, Y.Z.1    Query, C.C.2
  • 133
    • 52949131890 scopus 로고    scopus 로고
    • Crystal structure of the beta-finger domain of Prp8 reveals analogy to ribosomal proteins
    • Yang K., Zhang L., Xu T., Heroux A., and Zhao R. Crystal structure of the beta-finger domain of Prp8 reveals analogy to ribosomal proteins. Proc. Natl. Acad. Sci. USA 105 (2008) 13817-13822
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13817-13822
    • Yang, K.1    Zhang, L.2    Xu, T.3    Heroux, A.4    Zhao, R.5
  • 134
    • 0034649666 scopus 로고    scopus 로고
    • Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome
    • Yean S.L., Wuenschell G., Termini J., and Lin R.J. Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome. Nature 408 (2000) 881-884
    • (2000) Nature , vol.408 , pp. 881-884
    • Yean, S.L.1    Wuenschell, G.2    Termini, J.3    Lin, R.J.4
  • 136
    • 34249790589 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of splicing factor Prp8 carrying retinitis pigmentosa mutants
    • Zhang L., Shen J., Guarnieri M.T., Heroux A., Yang K., and Zhao R. Crystal structure of the C-terminal domain of splicing factor Prp8 carrying retinitis pigmentosa mutants. Protein Sci. 16 (2007) 1024-1031
    • (2007) Protein Sci. , vol.16 , pp. 1024-1031
    • Zhang, L.1    Shen, J.2    Guarnieri, M.T.3    Heroux, A.4    Yang, K.5    Zhao, R.6
  • 137
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou Z., Licklider L.J., Gygi S.P., and Reed R. Comprehensive proteomic analysis of the human spliceosome. Nature 419 (2002) 182-185
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 138
    • 0035691667 scopus 로고    scopus 로고
    • Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
    • Zhu J., Mayeda A., and Krainer A.R. Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol. Cell 8 (2001) 1351-1361
    • (2001) Mol. Cell , vol.8 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.