메뉴 건너뛰기




Volumn 32, Issue 24, 2012, Pages 5056-5066

The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN BRR2; PRP2 PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 84871880170     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01109-12     Document Type: Article
Times cited : (47)

References (58)
  • 1
    • 0029146556 scopus 로고
    • SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing
    • Ansari A, Schwer B. 1995. SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing. EMBO J. 14:4001-4009.
    • (1995) EMBO J. , vol.14 , pp. 4001-4009
    • Ansari, A.1    Schwer, B.2
  • 2
    • 0036948420 scopus 로고    scopus 로고
    • Allosteric cascade of spliceosome activation
    • Brow DA. 2002. Allosteric cascade of spliceosome activation. Annu. Rev. Genet. 36:333-360.
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 333-360
    • Brow, D.A.1
  • 3
    • 24744465409 scopus 로고    scopus 로고
    • The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceosome activation
    • Chan S-P, Cheng S-C. 2005. The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceosome activation. J. Biol. Chem. 280:31190-31199.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31190-31199
    • Chan, S.-P.1    Cheng, S.-C.2
  • 4
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan S-P, Kao D-I, Tsai W-Y, Cheng S-C. 2003. The Prp19p-associated complex in spliceosome activation. Science 302:279-282.
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.-P.1    Kao, D.-I.2    Tsai, W.-Y.3    Cheng, S.-C.4
  • 5
    • 84863680893 scopus 로고    scopus 로고
    • Functional roles of protein splicing factors
    • Chen H-C, Cheng S-C. 2012. Functional roles of protein splicing factors. Biosci. Rep. 32:345-359.
    • (2012) Biosci. Rep. , vol.32 , pp. 345-359
    • Chen, H.-C.1    Cheng, S.-C.2
  • 6
    • 0028339804 scopus 로고
    • Formation of the yeast splicing complex A1 and association of the splicing factor PRP19 with the pre-mRNA are independent of the 3= region of the intron
    • Cheng S-C. 1994. Formation of the yeast splicing complex A1 and association of the splicing factor PRP19 with the pre-mRNA are independent of the 3= region of the intron. Nucleic Acids Res. 22:1548-1554.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1548-1554
    • Cheng, S.-c.1
  • 7
    • 0023449728 scopus 로고
    • Spliceosome assembly in yeast
    • Cheng S-C, Abelson J. 1987. Spliceosome assembly in yeast. Genes Dev. 1:1014-1027.
    • (1987) Genes Dev. , vol.1 , pp. 1014-1027
    • Cheng, S.-C.1    Abelson, J.2
  • 9
    • 70350532246 scopus 로고    scopus 로고
    • Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction
    • Chiu Y-F, et al. 2009. Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction. Mol. Cell. Biol. 29:5671-5678.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5671-5678
    • Chiu, Y.-F.1
  • 10
    • 0026088747 scopus 로고
    • Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes
    • Company M, Arenas J, Abelson J. 1991. Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349:487-493.
    • (1991) Nature , vol.349 , pp. 487-493
    • Company, M.1    Arenas, J.2    Abelson, J.3
  • 11
    • 84861984263 scopus 로고    scopus 로고
    • Structure, function and regulation of spliceosomal RNA helicases
    • Cordin O, Hahn D, Beggs JD. 2012. Structure, function and regulation of spliceosomal RNA helicases. Curr. Opin. Cell Biol. 24:431-438.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 431-438
    • Cordin, O.1    Hahn, D.2    Beggs, J.D.3
  • 12
    • 0032880119 scopus 로고    scopus 로고
    • Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155
    • Das BK, et al. 1999. Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol. Cell. Biol. 19: 6796-6802.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6796-6802
    • Das, B.K.1
  • 13
    • 0033864702 scopus 로고    scopus 로고
    • Dominant negative mutants of the yeast splicing factor Prp2 map to a putative cleft region in the helicase domain of DExD/H-box proteins
    • Edwalds-Gilbert G, et al. 2000. Dominant negative mutants of the yeast splicing factor Prp2 map to a putative cleft region in the helicase domain of DExD/H-box proteins. RNA 6:1106-1119.
    • (2000) RNA , vol.6 , pp. 1106-1119
    • Edwalds-gilbert, G.1
  • 14
    • 1642540281 scopus 로고    scopus 로고
    • Definition of a spliceosome interaction domain in yeast Prp2 ATPase
    • Edwalds-Gilbert G, Kim D-H, Lin R-J. 2004. Definition of a spliceosome interaction domain in yeast Prp2 ATPase. RNA 10:210-220.
    • (2004) RNA , vol.10 , pp. 210-220
    • Edwalds-gilbert, G.1    Kim, D.-H.2    Lin, R.-J.3
  • 15
    • 0026440183 scopus 로고
    • An essential splicing factor, SLU7, mediates 3= splice site choice in yeast
    • Frank D, Guthrie C. 1992. An essential splicing factor, SLU7, mediates 3= splice site choice in yeast. Genes Dev. 6:2112-2124.
    • (1992) Genes Dev. , vol.6 , pp. 2112-2124
    • Frank, D.1    Guthrie, C.2
  • 16
    • 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, Reed R. 1996. 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: 233-243.
    • (1996) Genes Dev. , vol.10 , pp. 233-243
    • Gozani, O.1    Feld, R.2    Reed, R.3
  • 17
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF SAP155 interactions in recruiting U2 snRNP to the branch site
    • Gozani O, Potashkin J, Reed R. 1998. A potential role for U2AF SAP155 interactions in recruiting U2 snRNP to the branch site. Mol. Cell. Biol. 18:4752-4760.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 18
    • 0027404721 scopus 로고
    • Stages in the second reaction of premRNAsplicing: the final step is ATP independent
    • Horowitz DS, Abelson J. 1993. Stages in the second reaction of premRNAsplicing: the final step is ATP independent. Genes Dev. 7:320-329.
    • (1993) Genes Dev. , vol.7 , pp. 320-329
    • Horowitz, D.S.1    Abelson, J.2
  • 19
    • 33749130843 scopus 로고    scopus 로고
    • Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases
    • Jankowsky E, Bowers H. 2006. Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases. Nucleic Acids Res. 34:4181-4188.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4181-4188
    • Jankowsky, E.1    Bowers, H.2
  • 20
  • 21
    • 0027533005 scopus 로고
    • Pre-mRNA splicing within an assembled yeast spliceosome requires an RNA-dependent ATPase and ATP hydrolysis
    • im S-H, Lin R-J. 1993. Pre-mRNA splicing within an assembled yeast spliceosome requires an RNA-dependent ATPase and ATP hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 90:888-892.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 888-892
    • Kim, S.-H.1    Lin, R.-J.2
  • 22
    • 0026535919 scopus 로고
    • The purified yeast premRNA splicing factor PRP2 is an RNA-dependent NTPase
    • Kim S-H, Smith J, Claude A, Lin R-J. 1992. The purified yeast premRNA splicing factor PRP2 is an RNA-dependent NTPase. EMBO J. 11: 2319-2326.
    • (1992) EMBO J. , vol.11 , pp. 2319-2326
    • Kim, S.-H.1    Smith, J.2    Claude, A.3    Lin, R.-J.4
  • 23
    • 21044449402 scopus 로고    scopus 로고
    • Structure-function analysis of the U2 snRNPassociated splicing factor SF3a
    • Krämer A, et al. 2005. Structure-function analysis of the U2 snRNPassociated splicing factor SF3a. Biochem. Soc. Trans. 33:439-442.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 439-442
    • Krämer, A.1
  • 24
    • 0033612569 scopus 로고    scopus 로고
    • Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP
    • Krämer A, Gruter P, Groning K, Kastner B. 1999. Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP. J. Cell Biol. 145:1355-1368.
    • (1999) J. Cell Biol. , vol.145 , pp. 1355-1368
    • Krämer, A.1    Gruter, P.2    Groning, K.3    Kastner, B.4
  • 25
    • 77149180424 scopus 로고    scopus 로고
    • Release of SF3 from the intron branch point activates the first step of pre-mRNA splicing
    • Lardelli RM, Thompson JX, Yates JR III, Stevens SW. 2010. Release of SF3 from the intron branch point activates the first step of pre-mRNA splicing. RNA 16:516-528.
    • (2010) RNA , vol.16 , pp. 516-528
    • Lardelli, R.M.1    Thompson, J.X.2    Yates, J.R.3    Stevens, S.W.4
  • 26
    • 0023296411 scopus 로고
    • Splicing of yeast nuclear pre-mRNA in vitro requires a functional 40S spliceosome and several extrinsic factors
    • Lin R-J, Lustig AJ, Abelson J. 1987. Splicing of yeast nuclear pre-mRNA in vitro requires a functional 40S spliceosome and several extrinsic factors. Genes Dev. 1:7-18.
    • (1987) Genes Dev. , vol.1 , pp. 7-18
    • Lin, R.-J.1    Lustig, A.J.2    Abelson, J.3
  • 27
    • 79960724199 scopus 로고    scopus 로고
    • From unwinding to clamping-the DEAD box RNA helicase family
    • Linder P, Jankowsky E. 2011. From unwinding to clamping-the DEAD box RNA helicase family. Nat. Rev. Mol. Cell Biol. 12:505-516.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 505-516
    • Linder, P.1    Jankowsky, E.2
  • 28
    • 34547155595 scopus 로고    scopus 로고
    • A novel splicing factor Yju2 is associated with NTC and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing
    • Liu Y-C, Chen H-C, Wu N-Y, Cheng S-C. 2007. A novel splicing factor Yju2 is associated with NTC and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing. Mol. Cell. Biol. 27:5403-5413.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5403-5413
    • Liu, Y.-C.1    Chen, H.-C.2    Wu, N.-Y.3    Cheng, S.-C.4
  • 29
    • 40649103688 scopus 로고    scopus 로고
    • Identification of RNA binding proteins by UV cross-linking
    • Unit 27.2
    • Luo MJ, Reed R. 2003. Identification of RNA binding proteins by UV cross-linking. Curr. Protoc. Mol. Biol. 27:Unit 27.2.
    • (2003) Curr. Protoc. Mol. Biol. , vol.27
    • Luo, M.J.1    Reed, R.2
  • 30
    • 0026486883 scopus 로고
    • A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome
    • Madhani HD, Guthrie C. 1992. A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome. Cell 71:803-818.
    • (1992) Cell , vol.71 , pp. 803-818
    • Madhani, H.D.1    Guthrie, C.2
  • 31
    • 0026486884 scopus 로고
    • Mutational analysis of the yeast U2 snRNA suggests a structural similarity to the catalytic core of group I introns
    • McPheeters DS, Abelson J. 1992. Mutational analysis of the yeast U2 snRNA suggests a structural similarity to the catalytic core of group I introns. Cell 71:819-832.
    • (1992) Cell , vol.71 , pp. 819-832
    • Mcpheeters, D.S.1    Abelson, J.2
  • 32
    • 0037980050 scopus 로고    scopus 로고
    • Spatial organization of protein-RNA interactions in the branch site-3= splice site region during premRNA splicing in yeast
    • McPheeters DS, Muhlenkamp P. 2003. Spatial organization of protein-RNA interactions in the branch site-3= splice site region during premRNA splicing in yeast. Mol. Cell. Biol. 23:4174-4186.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4174-4186
    • Mcpheeters, D.S.1    Muhlenkamp, P.2
  • 33
    • 3843051369 scopus 로고    scopus 로고
    • RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2.
    • Nandakumar J, Ho CK, Lima CD, Shuman S. 2004. RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2. J. Biol. Chem. 279:31337-31347.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31337-31347
    • Nandakumar, J.1    Ho, C.K.2    Lima, C.D.3    Shuman, S.4
  • 34
    • 84861394737 scopus 로고    scopus 로고
    • Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS
    • Ohrt T, et al. 2012. Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS. RNA 18:1244-1256.
    • (2012) RNA , vol.18 , pp. 1244-1256
    • Ohrt, T.1
  • 35
    • 0027955630 scopus 로고
    • A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes
    • Plumpton M, McGarvey M, Beggs JD. 1994. A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes. EMBO J. 13:879-887.
    • (1994) EMBO J. , vol.13 , pp. 879-887
    • Plumpton, M.1    Mcgarvey, M.2    Beggs, J.D.3
  • 36
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. 2008. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. 37:317-336.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 37
    • 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 JR, Anthony JG, Woolford JJL. 1995. The final stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promote step 1 of splicing. RNA 1:375-390.
    • (1995) RNA , vol.1 , pp. 375-390
    • Roy, J.1    Kim, K.2    Maddock, J.R.3    Anthony, J.G.4    Woolford, J.J.L.5
  • 38
    • 0022343426 scopus 로고
    • Cleavage of 5= splice site and lariat formation are independent of 3= splice site in yeast mRNA splicing
    • Rymond BC, Rosbash M. 1985. Cleavage of 5= splice site and lariat formation are independent of 3= splice site in yeast mRNA splicing. Nature 317:735-737.
    • (1985) Nature , vol.317 , pp. 735-737
    • Rymond, B.C.1    Rosbash, M.2
  • 39
    • 0023338718 scopus 로고
    • A novel role for the 3= region of introns in pre-mRNA splicing of Saccharomyces cerevisiae
    • Rymond BC, Torrey DD, Rosbash M. 1987. A novel role for the 3= region of introns in pre-mRNA splicing of Saccharomyces cerevisiae. Genes Dev. 1:238-246.
    • (1987) Genes Dev. , vol.1 , pp. 238-246
    • Rymond, B.C.1    Torrey, D.D.2    Rosbash, M.3
  • 40
    • 0026524532 scopus 로고
    • Association of U6 snRNA with the 5=-splice site region of pre-mRNA in the spliceosome
    • Sawa H, Shimura Y. 1992. Association of U6 snRNA with the 5=-splice site region of pre-mRNA in the spliceosome. Genes Dev. 6:244-254.
    • (1992) Genes Dev. , vol.6 , pp. 244-254
    • Sawa, H.1    Shimura, Y.2
  • 41
    • 44949117567 scopus 로고    scopus 로고
    • A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release
    • Schwer B. 2008. A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release. Mol. Cell 30:743-754.
    • (2008) Mol. Cell , vol.30 , pp. 743-754
    • Schwer, B.1
  • 42
    • 0032055765 scopus 로고    scopus 로고
    • Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing
    • Schwer B, Gross CH. 1998. Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. EMBO J. 17:2086-2094.
    • (1998) EMBO J. , vol.17 , pp. 2086-2094
    • Schwer, B.1    Gross, C.H.2
  • 43
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • Schwer B, Guthrie C. 1991. PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349:494-499.
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 44
    • 8644284892 scopus 로고    scopus 로고
    • Interaction between a G-patch protein and a spliceosome DEXD/H-box ATPase that is critical for splicing
    • Silverman EJ, et al. 2004. Interaction between a G-patch protein and a spliceosome DEXD/H-box ATPase that is critical for splicing. Mol. Cell. Biol. 24:10101-10110.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10101-10110
    • Silverman, E.J.1
  • 45
    • 0028465429 scopus 로고
    • Site-specific RNA crosslinking with 4-thiouridine
    • Sontheimer EJ. 1994. Site-specific RNA crosslinking with 4-thiouridine. Mol. Biol. Rep. 20:35-44.
    • (1994) Mol. Biol. Rep. , vol.20 , pp. 35-44
    • Sontheimer, E.J.1
  • 46
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley JP, Guthrie C. 1998. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92:315-326.
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 47
    • 0028365538 scopus 로고
    • Functional association of essential splicing factor( s) with PRP19 in a protein complex
    • Tarn W-Y, et al. 1994. Functional association of essential splicing factor( s) with PRP19 in a protein complex. EMBO J. 13:2421-2431.
    • (1994) EMBO J. , vol.13 , pp. 2421-2431
    • Tarn, W.-Y.1
  • 48
    • 0028158655 scopus 로고
    • The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA
    • Teigelkamp S, McGarvey M, Plumpton M, Beggs JD. 1994. The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA. EMBO J. 13:888-897.
    • (1994) EMBO J. , vol.13 , pp. 888-897
    • Teigelkamp, S.1    Mcgarvey, M.2    Plumpton, M.3    Beggs, J.D.4
  • 49
    • 36849009618 scopus 로고    scopus 로고
    • Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly
    • Tsai R-T, et al. 2007. Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly. Mol. Cell. Biol. 27:8027-8037.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8027-8037
    • Tsai, R.-T.1
  • 50
    • 78650446117 scopus 로고    scopus 로고
    • DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps
    • Tseng C-K, Liu H-L, Cheng S-C. 2011. DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps. RNA 17: 145-154.
    • (2011) RNA , vol.17 , pp. 145-154
    • Tseng, C.-K.1    Liu, H.-L.2    Cheng, S.-C.3
  • 51
    • 0035053295 scopus 로고    scopus 로고
    • Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae
    • van Nues RW, Beggs JD. 2001. Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae. Genetics 157:1451-1467.
    • (2001) Genetics , vol.157 , pp. 1451-1467
    • Nues, R.W.V.1    Beggs, J.D.2
  • 52
    • 0032525149 scopus 로고    scopus 로고
    • The DEAH-box protein PRP22 is an ATPase that mediates ATPdependent mRNA release from the spliceosome and unwinds RNA duplexes
    • Wagner JDO, Jankowsky E, Company M, Pyle AM, Abelson JN. 1998. The DEAH-box protein PRP22 is an ATPase that mediates ATPdependent mRNA release from the spliceosome and unwinds RNA duplexes. EMBO J. 17:2926-2937.
    • (1998) EMBO J. , vol.17 , pp. 2926-2937
    • Wagner, J.D.O.1    Jankowsky, E.2    Company, M.3    Pyle, A.M.4    Abelson, J.N.5
  • 53
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: design principles of a dynamic RNP machine
    • Wahl MC, Will CL, Lührmann RL. 2009. The spliceosome: design principles of a dynamic RNP machine. Cell 136:701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Lührmann, R.L.3
  • 54
    • 71449119694 scopus 로고    scopus 로고
    • Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components
    • Warkocki Z, et al. 2009. Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components. Nat. Struct. Mol. Biol. 16:1237-1243.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1237-1243
    • Warkocki, Z.1
  • 55
    • 0026670431 scopus 로고
    • Interactions of small nuclear RNA's with precursor messenger RNA during in vitro splicing
    • Wassarman DA, Steitz JA. 1992. Interactions of small nuclear RNA's with precursor messenger RNA during in vitro splicing. Science 257:1918-1925.
    • (1992) Science , vol.257 , pp. 1918-1925
    • Wassarman, D.A.1    Steitz, J.A.2
  • 56
    • 80455144530 scopus 로고    scopus 로고
    • Spliceosome structure and function
    • pii a003707. doi:10.1101/cshperspect.a003707
    • Will CL, Lührmann R. 2011. Spliceosome structure and function. Cold Spring Harb. Perspect. Biol. 3:pii a003707. doi:10.1101/cshperspect.a003707.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Will, C.L.1    Lührmann, R.2
  • 57
    • 0037119975 scopus 로고    scopus 로고
    • Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. E
    • Will CL, et al. 2002. Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 21:4978-4988.
    • (2002) MBO J. , vol.21 , pp. 4978-4988
    • Will, C.L.1
  • 58
    • 78751686704 scopus 로고    scopus 로고
    • Cwc22 is a novel splicing factor required for the function of Prp2 and for the spliceosome to escape from a futile pathway
    • Yeh T-C, et al. 2011. Cwc22 is a novel splicing factor required for the function of Prp2 and for the spliceosome to escape from a futile pathway. Mol. Cell. Biol. 31:43-53.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 43-53
    • Yeh, T.-C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.