메뉴 건너뛰기




Volumn 11, Issue 1, 2006, Pages 80-89

The identification and characterization of a testisspecific cDNA during spermatogenesis

Author keywords

Expression pattern; Spermatogenesis; Splicing factor

Indexed keywords

ARGININE; COMPLEMENTARY DNA; RNA BINDING PROTEIN; SPERMATOGENESIS RELATED SPLICING FACTOR, MOUSE;

EID: 33749389879     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-006-0008-4     Document Type: Article
Times cited : (1)

References (28)
  • 1
    • 0030030366 scopus 로고    scopus 로고
    • Patterns of transcriptional regulation in the mammalian testes
    • Kleen, K.C. Patterns of transcriptional regulation in the mammalian testes. Mol. Report Dev. 423 (1996) 268-281.
    • (1996) Mol. Report Dev. , vol.423 , pp. 268-281
    • Kleen, K.C.1
  • 2
    • 0036777902 scopus 로고    scopus 로고
    • Alternative splicing in the testes
    • Venables, J.P. Alternative splicing in the testes. Curr. Opin. Genet. Dev. 12 (2002) 615-619.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 615-619
    • Venables, J.P.1
  • 3
    • 0027424442 scopus 로고
    • Specific commitment of different pre-mRNA to splicing by single SR proteins
    • Fu, X.D. Specific commitment of different pre-mRNA to splicing by single SR proteins. Nature 365 (1993) 82-85.
    • (1993) Nature , vol.365 , pp. 82-85
    • Fu, X.D.1
  • 4
    • 12244290335 scopus 로고    scopus 로고
    • An early ancestor in the evolution of splicing: A Trypanosoma cruzi serine-arginin-rich protein (TcSR) is functional in cis-splicing
    • Portal, D. and Joaqúin, M. An early ancestor in the evolution of splicing: a Trypanosoma cruzi serine-arginin-rich protein (TcSR) is functional in cis-splicing. Mol. Biochem. Parasitol.127 (2003) 37-46.
    • (2003) Mol. Biochem. Parasitol. , vol.127 , pp. 37-46
    • Portal, D.1    Joaqúin, M.2
  • 5
    • 0033152209 scopus 로고    scopus 로고
    • Determinants of SR protein specificity
    • Roland, T. and James, L. Determinants of SR protein specificity. Curr. Opin. Cell Biol. 11 (1999) 358-362.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 358-362
    • Roland, T.1    James, L.2
  • 6
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Krämer, A. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65 (1996) 367-409.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Krämer, A.1
  • 7
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu, X.D. The superfamily of arginine/serine-rich splicing factors. RNA 1 (1995) 663-680.
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 8
    • 12244253959 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley, J.L. and Tacke, R. SR proteins and splicing control. Genes Dev. 9 (1996) 284-293.
    • (1996) Genes Dev. , vol.9 , pp. 284-293
    • Manley, J.L.1    Tacke, R.2
  • 9
    • 0030218143 scopus 로고    scopus 로고
    • The SR protein family: Pleiotropic functions in pre-mRNA splicing
    • Valcárcel, J. and Green, M.R. The SR protein family: pleiotropic functions in pre-mRNA splicing. Trends Biochem. Sci. 21 (1996) 296-301.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 296-301
    • Valcárcel, J.1    Green, M.R.2
  • 11
    • 0344407006 scopus 로고    scopus 로고
    • Proto-oncoprotein TLS/FUS is associated to the nuclear mitrix and complexed with splicing factors PTB, SRm160, and SR proteins
    • Meissner, M., Lopato, S., Gotzmann, J., Sauermann, G. and Barta, A. Proto-oncoprotein TLS/FUS is associated to the nuclear mitrix and complexed with splicing factors PTB, SRm160, and SR proteins. Exp. Cell Res. 283 (2003) 184-195.
    • (2003) Exp. Cell Res. , vol.283 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 12
    • 0034671932 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the absence of a SR protein SR domain
    • Zhu, J. and Krainer, A.R. Pre-mRNA splicing in the absence of a SR protein SR domain. Genes 14 (2000) 3166-3178.
    • (2000) Genes , vol.14 , pp. 3166-3178
    • Zhu, J.1    Krainer, A.R.2
  • 13
    • 0029859659 scopus 로고    scopus 로고
    • Targeted disruption of an essential vertebrate gene ASF/SF2 is required for cell viability
    • Wang, J., Takegaki, Y. and Manliy, J.L. Targeted disruption of an essential vertebrate gene ASF/SF2 is required for cell viability. Genes Dev. 10 (1996) 2588-2599.
    • (1996) Genes Dev. , vol.10 , pp. 2588-2599
    • Wang, J.1    Takegaki, Y.2    Manliy, J.L.3
  • 14
    • 1642303197 scopus 로고    scopus 로고
    • In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160
    • Stefan, W., Simion, C., Ivshina, M. and Nickerson, J.A. In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160. J. Cell Biol. 164 (2004) 843-850.
    • (2004) J. Cell Biol. , vol.164 , pp. 843-850
    • Stefan, W.1    Simion, C.2    Ivshina, M.3    Nickerson, J.A.4
  • 15
    • 0037452886 scopus 로고    scopus 로고
    • The spatial targeting and nuclear matrix binding domains of SR m160
    • Stefan, W., Simion, C. and Nickerson, J.A. The spatial targeting and nuclear matrix binding domains of SR m160. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 3269-3274.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3269-3274
    • Stefan, W.1    Simion, C.2    Nickerson, J.A.3
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., Gibson, and T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 11 (1994) 4673-4680.
    • (1994) Nucleic Acids Res. , vol.11 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 18
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney, E., Kumar, S. and Krainer, A.R. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 21 (1993) 5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 19
    • 0034927769 scopus 로고    scopus 로고
    • Cell- and stage-specific high-level expression of TBP-related factor 2 (TRF2) during mouse spermatogenesis
    • Zhang, D., Penttila, T.L., Morris, P.L. and Roeder, R.G. Cell- and stage-specific high-level expression of TBP-related factor 2 (TRF2) during mouse spermatogenesis. Mech. Dev. 106 (2001) 203-205.
    • (2001) Mech. Dev. , vol.106 , pp. 203-205
    • Zhang, D.1    Penttila, T.L.2    Morris, P.L.3    Roeder, R.G.4
  • 20
    • 0042786842 scopus 로고    scopus 로고
    • Expression of the mouse Aven gene during spermatogenesis, analyzed by subtraction screening using Mvh-knockout mice
    • Ina, S., Tsunekawa, N., Nakamura, A. and Noce, T. Expression of the mouse Aven gene during spermatogenesis, analyzed by subtraction screening using Mvh-knockout mice. Gene Expr. Patterns 5 (2003) 635-638.
    • (2003) Gene Expr. Patterns , vol.5 , pp. 635-638
    • Ina, S.1    Tsunekawa, N.2    Nakamura, A.3    Noce, T.4
  • 22
    • 0034235347 scopus 로고    scopus 로고
    • Unique and redundant functions of SR proteins, a conserved family of splicing factors, in Caenorhabditis elegants development
    • Taizo, K. and Masaki, F.T. Unique and redundant functions of SR proteins, a conserved family of splicing factors, in Caenorhabditis elegants development. Mech. Dev. 95 (2000) 67-76.
    • (2000) Mech. Dev. , vol.95 , pp. 67-76
    • Taizo, K.1    Masaki, F.T.2
  • 23
    • 0029912882 scopus 로고    scopus 로고
    • A Negative feedback mechanism revealed by functional analysis of the alternative isoforms of the Drosophila splicing regulator transformer-2
    • Mattox, W., McGuffin, M.E. and Baker, B.S. A Negative feedback mechanism revealed by functional analysis of the alternative isoforms of the Drosophila splicing regulator transformer-2. Genetics 143 (1996) 303-314.
    • (1996) Genetics , vol.143 , pp. 303-314
    • Mattox, W.1    McGuffin, M.E.2    Baker, B.S.3
  • 25
    • 0037150676 scopus 로고    scopus 로고
    • Unique chromatin remodeling and transcriptional regulation in spermatogenesis
    • Sassone-Corsi, P. Unique chromatin remodeling and transcriptional regulation in spermatogenesis. Science 296 (2002) 2176-2178
    • (2002) Science , vol.296 , pp. 2176-2178
    • Sassone-Corsi, P.1
  • 26
    • 4043121708 scopus 로고    scopus 로고
    • Testis-specific transcription mechanisms promoting male germ-cell differentiation
    • Kimmins, S., Kotaja, N., Davidson, I. and Sassone-Corsi, P. Testis-specific transcription mechanisms promoting male germ-cell differentiation. Repro. 128 (2004) 5-12
    • (2004) Repro. , vol.128 , pp. 5-12
    • Kimmins, S.1    Kotaja, N.2    Davidson, I.3    Sassone-Corsi, P.4
  • 27
    • 20244368961 scopus 로고    scopus 로고
    • Ovol1 regulates meiotic pachytene progression during spermatogenesis by repressing Id2 expression
    • Baoan, L., Mahalakshmi, N. and Mackay, D.R. Ovol1 regulates meiotic pachytene progression during spermatogenesis by repressing Id2 expression. Development 132 (2005)1463-1473
    • (2005) Development , vol.132 , pp. 1463-1473
    • Baoan, L.1    Mahalakshmi, N.2    Mackay, D.R.3
  • 28
    • 0034710982 scopus 로고    scopus 로고
    • The pachytene checkpoint prevents accumulation and phosphorylation of the meiosis-specific transcription factor Ndt80
    • Tung, K-S. and Bilanchone, V. The pachytene checkpoint prevents accumulation and phosphorylation of the meiosis-specific transcription factor Ndt80. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 12187-12192.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12187-12192
    • Tung, K.-S.1    Bilanchone, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.