메뉴 건너뛰기




Volumn 140, Issue 4, 1998, Pages 737-750

SRPK2: A differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BIOLOGICAL FACTOR; MESSENGER RNA PRECURSOR; PROTEIN; PROTEIN KINASE; SERINE;

EID: 0032559642     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.4.737     Document Type: Article
Times cited : (273)

References (61)
  • 1
    • 0030910308 scopus 로고    scopus 로고
    • FBP WW domains and the ABL SH3 domains bind to a specific class of proline-rich ligands
    • Bedford, M.T., D.C. Chan, and P. Leder. 1997. FBP WW domains and the ABL SH3 domains bind to a specific class of proline-rich ligands. EMBO (Eur. Mol. Biol. Organ.) J. 16:2376-2383.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 2376-2383
    • Bedford, M.T.1    Chan, D.C.2    Leder, P.3
  • 2
    • 0026011116 scopus 로고
    • A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators
    • Ben-David, Y., K Letwin, L. Tamock, A. Bernstein, and T. Pawson. 1991. A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators. EMBO (Eur. Mol. Biol. Organ.) J. 10:317-325.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 317-325
    • Ben-David, Y.1    Letwin, K.2    Tamock, L.3    Bernstein, A.4    Pawson, T.5
  • 3
    • 0028034042 scopus 로고
    • Association of nuclear matrix antigens with exon-containing splicing complexes
    • Blencowe, B.J., J.A. Nickerson, R. Issner, S. Penman, and P.A. Sharp. 1994. Association of nuclear matrix antigens with exon-containing splicing complexes. J. Cell Biol. 127:593-607.
    • (1994) J. Cell Biol. , vol.127 , pp. 593-607
    • Blencowe, B.J.1    Nickerson, J.A.2    Issner, R.3    Penman, S.4    Sharp, P.A.5
  • 5
    • 0027501327 scopus 로고
    • Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains
    • Caceres, J.F., and A.R. Krainer. 1993. Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains. EMBO (Eur. Mol. Biol. Organ.) J. 12:4715-4726.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 4715-4726
    • Caceres, J.F.1    Krainer, A.R.2
  • 6
    • 0027998643 scopus 로고
    • Protein phosphatase 1 can modulate alternative 5′ splice site selection in a HeLa splicing extract
    • Cardinali, B., P.T. Cohen, and A.I. Lamond. 1994. Protein phosphatase 1 can modulate alternative 5′ splice site selection in a HeLa splicing extract. FEBS Lett. 35:276-280.
    • (1994) FEBS Lett. , vol.35 , pp. 276-280
    • Cardinali, B.1    Cohen, P.T.2    Lamond, A.I.3
  • 7
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan, D.C., M.T. Bedford, and P. Leder. 1996. Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO (Eur. Mol. Biol. Organ.) J. 15:1045-1054.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 8
    • 0029099161 scopus 로고
    • The WW of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
    • Chen, H.I., and M. Sudol. 1995. The WW of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA. 92:7819-7823.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7819-7823
    • Chen, H.I.1    Sudol, M.2
  • 10
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/Sty protein kinases show distinct substrate specifities for serine/arginine-rich splicine factors
    • Colwill, K., L.L. Feng, J.M. Yeakaly, G.D. Gish, J.F. Caceres, T. Pawson, and X-D. Fu. 1996b. SRPK1 and Clk/Sty protein kinases show distinct substrate specifities for serine/arginine-rich splicine factors. J. Biol. Chem. 271:24569-24575.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24569-24575
    • Colwill, K.1    Feng, L.L.2    Yeakaly, J.M.3    Gish, G.D.4    Caceres, J.F.5    Pawson, T.6    Fu, X.-D.7
  • 12
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck, J.A., G.G. Maul, W.H. Miller, J.D. Chen, A. Kakizuka, and R.M. Evans. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell. 76:333-343.
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 13
    • 0029372979 scopus 로고
    • The superfamily of arginine-serine-ricn splicing factors
    • Fu, X-D. 1995. The superfamily of arginine-serine-ricn splicing factors. RNA. 1:663-680.
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.-D.1
  • 14
    • 0025115231 scopus 로고
    • Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus
    • Fu, X-D., and T. Maniatis. 1990. Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus. Nature. 343:437-441.
    • (1990) Nature , vol.343 , pp. 437-441
    • Fu, X.-D.1    Maniatis, T.2
  • 15
    • 0026437581 scopus 로고
    • General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection
    • Fu, X-D., A. Mayeda, T. Maniatis, and A.R. Krainer. 1992. General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection. Proc. Natl. Acad. Sci. USA. 89:11224-11228.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11224-11228
    • Fu, X.-D.1    Mayeda, A.2    Maniatis, T.3    Krainer, A.R.4
  • 16
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA. 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 17
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui, J-F., W.S. Lane, and X-D. Fu. 1994a. A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature. 369:678-682.
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.-F.1    Lane, W.S.2    Fu, X.-D.3
  • 18
    • 0027962510 scopus 로고
    • Purification and characterization of a kinase specific for the serine- and arginine-rich premRNA splicing factors
    • Gui, J-F., H. Tronchere, S.D. Chandler, and X-D. Fu. 1994b. Purification and characterization of a kinase specific for the serine- and arginine-rich premRNA splicing factors. Proc. Natl. Acad. Sci. USA. 91:10824-10828.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10824-10828
    • Gui, J.-F.1    Tronchere, H.2    Chandler, S.D.3    Fu, X.-D.4
  • 19
    • 0027938872 scopus 로고
    • Characterization by cDNa cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases
    • Hanes, J., H. von der Kammer, J. Klaudiny, and K.H. Scheit. 1994. Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases. J. Mol. Biol. 244:665-672.
    • (1994) J. Mol. Biol. , vol.244 , pp. 665-672
    • Hanes, J.1    Von Der Kammer, H.2    Klaudiny, J.3    Scheit, K.H.4
  • 20
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary and classification of family members
    • Hanks, S.K., and A.M. Quinn. 1991. Protein kinase catalytic domain sequence database: identification of conserved features of primary and classification of family members. Methods Enzymol. 200:38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 22
    • 0029952583 scopus 로고    scopus 로고
    • Intron-dependent recruitment of pre-mRNA splicing factors to sites of transcription
    • Huang, S., and D.L. Spector. 1996. Intron-dependent recruitment of pre-mRNA splicing factors to sites of transcription. J. Cell Biol 133:719-732.
    • (1996) J. Cell Biol , vol.133 , pp. 719-732
    • Huang, S.1    Spector, D.L.2
  • 23
    • 0027478001 scopus 로고
    • In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism
    • Jimenez-Garcia, L.F., and D.L. Spector. 1993. In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism. Cell. 73:47-59.
    • (1993) Cell , vol.73 , pp. 47-59
    • Jimenez-Garcia, L.F.1    Spector, D.L.2
  • 24
    • 0025756794 scopus 로고
    • Molecular cloning of a novel human cdc2/CDC28-like protein kinase
    • Johnson, K.W., and K.A. Smith. 1991. Molecular cloning of a novel human cdc2/CDC28-like protein kinase. J. Biol. Chem. 266:3402-3407.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3402-3407
    • Johnson, K.W.1    Smith, K.A.2
  • 25
    • 0027445241 scopus 로고
    • The conserved pre-mRNA splicing factor U2AF from Drosophila: Requirement for viability
    • Kanaar, R., S.E. Roche, E.L. Beall, M.R. Green, and D.C. Rio. 1993. The conserved pre-mRNA splicing factor U2AF from Drosophila: requirement for viability. Science. 262:569-573.
    • (1993) Science , vol.262 , pp. 569-573
    • Kanaar, R.1    Roche, S.E.2    Beall, E.L.3    Green, M.R.4    Rio, D.C.5
  • 26
    • 0030027483 scopus 로고    scopus 로고
    • Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle
    • Kao, H.Y., and P.G. Siliciano. 1996. Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle. Mol. Cell. Biol. 16:960-967.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 960-967
    • Kao, H.Y.1    Siliciano, P.G.2
  • 28
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Krämer, A. 1996. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65:367-409.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Krämer, A.1
  • 29
    • 0029028584 scopus 로고
    • Evidence for a NIMA-like mitotic pathway in vertebrate cells
    • Lu, K.P., and T. Hunter. 1995. Evidence for a NIMA-like mitotic pathway in vertebrate cells. Cell 81:413-424.
    • (1995) Cell , vol.81 , pp. 413-424
    • K.p, L.1    Hunter, T.2
  • 30
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K.P., S.D. Hanes, and T. Hunter. 1996. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 31
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias, M.J., M. Hyvonen, E. Baraldi, J. Schultz, M. Sudol, M. Saraste, and H. Oschkinat. 1996. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382:646-649.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 32
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley, J.L., and R. Tacke. 1996. SR proteins and splicing control. Genes Dev. 10:1569-1579.
    • (1996) Genes Dev. , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 33
    • 0026731973 scopus 로고
    • Ser/Thr-specific protein phosphophatases are required for both catalytic steps pre-mRNA splicing
    • Mermoud, J.E., P.T. Cohen, and A.I. Lamond. 1992. Ser/Thr-specific protein phosphophatases are required for both catalytic steps pre-mRNA splicing. Nucleic Acids Res. 20:5263-5269.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5263-5269
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.I.3
  • 34
    • 0028043718 scopus 로고
    • Regulation of mammalian splicesome assembly by a protein phosphorylation mechanism
    • Mermoud, J.E., P.T. Cohen, and A.E. Lamond. 1994. Regulation of mammalian splicesome assembly by a protein phosphorylation mechanism. EMBO (Eur. Mol. Biol. Organ.) J. 13:5679-5688.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 5679-5688
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.E.3
  • 35
    • 0029798802 scopus 로고    scopus 로고
    • Serine/threonine phosphatase I modulates the subnuclear distribution of pre-mRNA splicing factors
    • Misteli, T., and D.L. Spector. 1996. Serine/threonine phosphatase I modulates the subnuclear distribution of pre-mRNA splicing factors. Mol. Biol. Cell. 7:1559-1572.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1559-1572
    • Misteli, T.1    Spector, D.L.2
  • 36
    • 1842376906 scopus 로고    scopus 로고
    • The dynamics of a pre-mRNa splicing factor in living cells
    • Misteli, T., J.F. Caceres, and D.L. Spector. 1997. The dynamics of a pre-mRNA splicing factor in living cells. Nature. 387:523-527.
    • (1997) Nature , vol.387 , pp. 523-527
    • Misteli, T.1    Caceres, J.F.2    Spector, D.L.3
  • 37
    • 0027492990 scopus 로고
    • U2AF homolog required for splicing in vivo
    • Potashkin, J., K. Naik, and K. Wentz-Hunter. 1993. U2AF homolog required for splicing in vivo. Science. 262:573-575.
    • (1993) Science , vol.262 , pp. 573-575
    • Potashkin, J.1    Naik, K.2    Wentz-Hunter, K.3
  • 38
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren, R., B.J. Mayer, P. Cicchetti, and D. Baltimore. 1993. Identification of a ten-amino acid proline-rich SH3 binding site. Science. 259:1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 39
    • 0029814786 scopus 로고
    • Mutations in the small subunit of the Drosophila U2AF splicing factor cause lethality and developmental defects
    • Rudner, D.Z., R. Kanaar, K.S. Breger, and D.C. Rio. 1993. Mutations in the small subunit of the Drosophila U2AF splicing factor cause lethality and developmental defects. Proc. Natl. Acad Sci. USA. 93:10333-10337.
    • (1993) Proc. Natl. Acad Sci. USA , vol.93 , pp. 10333-10337
    • Rudner, D.Z.1    Kanaar, R.2    Breger, K.S.3    Rio, D.C.4
  • 40
    • 0025737866 scopus 로고
    • Cloning of a yeast U1 snRNP 70K protein homologue: Functional conservation of an RNA-binding domain between humans and yeast
    • Smith, V., and B.C. Barrell. 1991. Cloning of a yeast U1 snRNP 70K protein homologue: functional conservation of an RNA-binding domain between humans and yeast. EMBO (Eur. Mol. Biol. Organ.) J. 10:2627-2634.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 2627-2634
    • Smith, V.1    Barrell, B.C.2
  • 42
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for the substrate specifities of protein ser/thr kinases: Primary sequence preference of casein kinase I and II, NIMA, phosphorytase kinase, calmodulin-dependent kinase II, CDK5 and Erk1
    • Songyang, Z., K.P. Lu, Y.T. Kwon, L.H. Tsai, O. Filhol, C. Cochet, D.A. Brickey, T.R. Soderling, C. Bartleson, D.J. Graves, et al. 1996. A structural basis for the substrate specifities of protein ser/thr kinases: primary sequence preference of casein kinase I and II, NIMA, phosphorytase kinase, calmodulin-dependent kinase II, CDK5 and Erk1. Mol. Cell. Biol. 16:6486-6493.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 43
    • 0027135889 scopus 로고
    • Macromolecular domains within the cell nucleus
    • Spector, D.L. 1993. Macromolecular domains within the cell nucleus. Annu. Rev. Cell. Biol. 9:265-315.
    • (1993) Annu. Rev. Cell. Biol. , vol.9 , pp. 265-315
    • Spector, D.L.1
  • 44
    • 0027407640 scopus 로고
    • Autoactivation of catalytic (C alpha) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197
    • Steinberg, R.A., R.D. Cauthron, M.M. Symcox, and H. Shuntoh. 1993. Autoactivation of catalytic (C alpha) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197. Mol. Cell Biol. 13:2332-2341.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2332-2341
    • Steinberg, R.A.1    Cauthron, R.D.2    Symcox, M.M.3    Shuntoh, H.4
  • 46
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol, M. 1996a. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65:113-132.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 113-132
    • Sudol, M.1
  • 47
    • 0029991867 scopus 로고    scopus 로고
    • The WW module competes with the SH3 domain?
    • Sudol, M. 1996b. The WW module competes with the SH3 domain? Trends Biochem. Sci. 21:161-163.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 161-163
    • Sudol, M.1
  • 48
    • 0029146950 scopus 로고
    • Characterization of a novel protein-binding module-the WW domain
    • Sudol, M., H.I. Chen, C. Bougeret, A. Einbond, and P. Bork. 1995. Characterization of a novel protein-binding module-the WW domain. FEBS Lett. 369: 67-71.
    • (1995) FEBS Lett. , vol.369 , pp. 67-71
    • Sudol, M.1    Chen, H.I.2    Bougeret, C.3    Einbond, A.4    Bork, P.5
  • 49
    • 0031037690 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: Creation of an SRp40-specific splicing enhancer
    • Tacke, R., Y. Chen, and J.L. Manley. 1997. Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer. Proc. Natl. Acad. Sci. USA. 94:1148-1153.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 50
    • 0027529270 scopus 로고
    • A mitotic role for a novel fission yeast protein kinase dsk1 with cell cycle stage dependent phosphorylation and localization
    • Takeuchi, M., and M. Yanagida. 1993. A mitotic role for a novel fission yeast protein kinase dsk1 with cell cycle stage dependent phosphorylation and localization. Mol. Biol. Cell. 4:247-260.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 247-260
    • Takeuchi, M.1    Yanagida, M.2
  • 51
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor, S.S., and E. Radizo-Andzelm. 1994. Three protein kinase structures define a common motif. Structure. 2:345-355.
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radizo-Andzelm, E.2
  • 53
    • 0039769985 scopus 로고    scopus 로고
    • A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre- MRNA
    • Tronchere, H., J. Wang, and X-D. Fu. 1997. A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA. Nature. 388:397-400.
    • (1997) Nature , vol.388 , pp. 397-400
    • Tronchere, H.1    Wang, J.2    Fu, X.-D.3
  • 54
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell. 61:203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 55
    • 0030218143 scopus 로고    scopus 로고
    • The SR protein family: Pleiotropic functions in pre-mRNA splicing
    • Valcárcel, J., and M.R. Green. 1996. The SR protein family: pleiotropic functions in pre-mRNA splicing. Trends Biochem. Sci. 21:296-301.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 296-301
    • Valcárcel, J.1    Green, M.R.2
  • 56
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S.H., and J.L. Manley. 1997. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 11:334-344.
    • (1997) Genes Dev. , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 57
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of pre-mRNa splicing factors
    • Zahler, A.M., W.S. Lane, J.A. Stolk, and M.B. Roth. 1992. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev. 6:837-847.
    • (1992) Genes Dev. , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 58
    • 0027160003 scopus 로고
    • Distinct functions of SR proteins in alternative pre-mRNA splicing
    • Zahler, A.M., K.M. Neugebauer, W.S. Lane, and M.B. Roth. 1993. Distinct functions of SR proteins in alternative pre-mRNA splicing. Science. 260: 219-222.
    • (1993) Science , vol.260 , pp. 219-222
    • Zahler, A.M.1    Neugebauer, K.M.2    Lane, W.S.3    Roth, M.B.4
  • 59
    • 0026569967 scopus 로고
    • Cloning and domain stucture of the mammalian splicing factor U2AF
    • Zamore, P.D., J.G. Patton, and M.R. Green. 1992. Cloning and domain stucture of the mammalian splicing factor U2AF. Nature. 355:609-614.
    • (1992) Nature , vol.355 , pp. 609-614
    • Zamore, P.D.1    Patton, J.G.2    Green, M.R.3
  • 60
    • 0026649523 scopus 로고
    • Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit
    • Zhang, M., P.D. Zamore, M. Carmo-Fonseca, A.I. Lamond, and M.R. Green, 1992. Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit. Proc. Natl. Acad. Sci. USA. 89: 8769-8773.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8769-8773
    • Zhang, M.1    Zamore, P.D.2    Carmo-Fonseca, M.3    Lamond, A.I.4    Green, M.R.5
  • 61
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • Zheng, J., D.R. Knighton, H.H. Xuong, S.S. Taylor, J.M. Sowadski, and L.F. Ten Eyck. 1993. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Sci. 2:1559-1573.
    • (1993) Protein Sci. , vol.2 , pp. 1559-1573
    • Zheng, J.1    Knighton, D.R.2    Xuong, H.H.3    Taylor, S.S.4    Sowadski, J.M.5    Ten Eyck, L.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.