메뉴 건너뛰기




Volumn 384, Issue 1, 2003, Pages 25-37

Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)

Author keywords

Domain mapping; mRNA degradation; Protein protein interactions; Ribonuclease; RNA binding domains; RNA binding proteins

Indexed keywords

ARGININE; CYTOKINE; ISOPROTEIN; MESSENGER RNA; MESSENGER RNA BINDING PROTEIN AUF1; NUCLEOTIDE BINDING PROTEIN; OLIGONUCLEOTIDE; PROTEIN IMP 2; PROTEIN NSAP 1; PROTEIN NSEP 1; RECOMBINANT PROTEIN; RIBONUCLEASE; RNA BINDING PROTEIN; UBIQUITIN CONJUGATING ENZYME; UNCLASSIFIED DRUG; URACIL;

EID: 0037224504     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.004     Document Type: Review
Times cited : (48)

References (53)
  • 1
    • 0034663204 scopus 로고    scopus 로고
    • A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D
    • Arao, Y., Kuriyama, R., Kayama, F., and Kato, S. (2000). A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D. Arch. Biochem. Biophys. 380, 228-236.
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 228-236
    • Arao, Y.1    Kuriyama, R.2    Kayama, F.3    Kato, S.4
  • 2
    • 0029126514 scopus 로고
    • Analyzing protein-protein interactions using two-hybrid system
    • Bartel, P.L. and Fields, S. (1995). Analyzing protein-protein interactions using two-hybrid system. Methods Enzymol. 254, 241-263.
    • (1995) Methods Enzymol. , vol.254 , pp. 241-263
    • Bartel, P.L.1    Fields, S.2
  • 3
    • 0024591905 scopus 로고
    • The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro
    • Bernstein, P., Peitz, S.W., and Ross, J. (1989). The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol. Cell Biol.9, 659-670.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 659-670
    • Bernstein, P.1    Peitz, S.W.2    Ross, J.3
  • 4
    • 0026507321 scopus 로고
    • Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant
    • Bernstein, P.L., Herrick, D.J., Prokipcak, R.D., and Ross, J. (1992). Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant. Genes Dev. 6, 642-654.
    • (1992) Genes Dev. , vol.6 , pp. 642-654
    • Bernstein, P.L.1    Herrick, D.J.2    Prokipcak, R.D.3    Ross, J.4
  • 5
    • 0026640829 scopus 로고
    • AU RNA-binding factors differ in their binding specificities and affinities
    • Bohjanen, P.R., Petryniak, B., June, C.H., Thompson, C.B., and Lindsten, T. (1992). AU RNA-binding factors differ in their binding specificities and affinities. J. Biol. Chem. 267, 6302-6309.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6302-6309
    • Bohjanen, P.R.1    Petryniak, B.2    June, C.H.3    Thompson, C.B.4    Lindsten, T.5
  • 6
    • 0026337150 scopus 로고
    • An A+U-rich element RNA-binding factor regulates c-myc mRNA stability in vitro
    • Brewer, G. (1991). An A+U-rich element RNA-binding factor regulates c-myc mRNA stability in vitro. Mol. Cell Biol. 11, 2460-2466.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 2460-2466
    • Brewer, G.1
  • 7
    • 0033523031 scopus 로고    scopus 로고
    • Evidence for a 3′-5′ decay pathway for c-myc mRNA in mammalian cells
    • Brewer, G. (1999). Evidence for a 3′-5′ decay pathway for c-myc mRNA in mammalian cells. J. Biol. Chem. 274, 16174-16179.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16174-16179
    • Brewer, G.1
  • 8
    • 0034721760 scopus 로고    scopus 로고
    • Regulation of c-myc mRNA decay in vitro by a TPA-inducible, ribosome- associated component in differentiating megalkaryoblasts
    • Brewer, G. (2000). Regulation of c-myc mRNA decay in vitro by a TPA-inducible, ribosome- associated component in differentiating megalkaryoblasts. J. Biol. Chem. 275, 33336-45.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33336-33345
    • Brewer, G.1
  • 10
    • 10244230822 scopus 로고    scopus 로고
    • Increased granulocyte-macrophage colony-stimulating factor mRNA instability in cord versus adult mononuclear cells is translation- dependent and associated with increased levels of A+U-rich element binding factor
    • Buzby, J.S., Lee, S.M., Van Winkle, P., DeMaria, C.T., Brewer, G., and Cairo, M.S. (1996). Increased granulocyte-macrophage colony-stimulating factor mRNA instability in cord versus adult mononuclear cells is translation- dependent and associated with increased levels of A+U-rich element binding factor. Blood 88, 2889-2897.
    • (1996) Blood , vol.88 , pp. 2889-2897
    • Buzby, J.S.1    Lee, S.M.2    Van Winkle, P.3    DeMaria, C.T.4    Brewer, G.5    Cairo, M.S.6
  • 11
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey, J. (1991). Gel retardation. Methods Enzymol. 208, 103-117.
    • (1991) Methods Enzymol. , vol.208 , pp. 103-117
    • Carey, J.1
  • 12
  • 13
    • 0034326627 scopus 로고    scopus 로고
    • Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor
    • Croze, E., Usacheva, A., Asarnow, D., Minshall, R.D., Perez, H. D., and Colamonici, O. (2000). Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor. J. Immunol. 165, 5127-5132.
    • (2000) J. Immunol. , vol.165 , pp. 5127-5132
    • Croze, E.1    Usacheva, A.2    Asarnow, D.3    Minshall, R.D.4    Perez, H.D.5    Colamonici, O.6
  • 14
    • 15844383918 scopus 로고    scopus 로고
    • AUF1 binding affinity to A+U-rich elements correlates with rapid mRNA degradation
    • DeMaria, C.T. and Brewer, G. (1996). AUF1 binding affinity to A+U-rich elements correlates with rapid mRNA degradation. J. Biol. Chem. 271, 12179-12184.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12179-12184
    • DeMaria, C.T.1    Brewer, G.2
  • 15
    • 0030635952 scopus 로고    scopus 로고
    • Cell-free systems for analysis of cytoplasmic mRNA turnover
    • DeMaria, C.T. and Brewer, G. (1997). Cell-free systems for analysis of cytoplasmic mRNA turnover. Prog. Mol. Subcell. Biol. 18, 65-91.
    • (1997) Prog. Mol. Subcell. Biol. , vol.18 , pp. 65-91
    • DeMaria, C.T.1    Brewer, G.2
  • 16
    • 0035896531 scopus 로고    scopus 로고
    • Cold shock domain factors activate the granulocyte-macrophage colony-stimulating factor promoter in stimulated Jurkat T cells
    • Diamond, P., Shannon, M.F., Vadas, M.A., and Coles, L.S. (2001). Cold shock domain factors activate the granulocyte-macrophage colony-stimulating factor promoter in stimulated Jurkat T cells. J. Biol. Chem. 276, 7943-7951.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7943-7951
    • Diamond, P.1    Shannon, M.F.2    Vadas, M.A.3    Coles, L.S.4
  • 18
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • Fan, X.C. and Steitz, J.A. (1998). Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J. 17, 3448-3460.
    • (1998) EMBO J. , vol.17 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 19
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • Gao, M., Wilusz, C. J., Feltz, S. W., Wilusz, J. (2001). A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J. 20, 1134-1143.
    • (2001) EMBO J. , vol.20 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Feltz, S.W.3    Wilusz, J.4
  • 20
    • 0034730324 scopus 로고    scopus 로고
    • A mechanism for translationally coupled mRNA turnover: Interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex
    • Grosset, C., Chen, C.Y., Xu, N., Sonenberg, N., Jacquemin-Sablon, H., and Shyu, A.B. (2000). A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell 103, 29-40.
    • (2000) Cell , vol.103 , pp. 29-40
    • Grosset, C.1    Chen, C.Y.2    Xu, N.3    Sonenberg, N.4    Jacquemin-Sablon, H.5    Shyu, A.B.6
  • 21
    • 0027523417 scopus 로고
    • Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences
    • Hamilton, B.J., Nagy, E., Malter, J.S., Arrick, B.A., and Rigby, W.F. (1993). Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences. J. Biol. Chem. 268, 8881-8887.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8881-8887
    • Hamilton, B.J.1    Nagy, E.2    Malter, J.S.3    Arrick, B.A.4    Rigby, W.F.5
  • 22
    • 0032889252 scopus 로고    scopus 로고
    • A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice
    • Harris, C.E., Boden, R.A., and Astell, C.R. (1999). A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice. J. Virol. 73, 72-80.
    • (1999) J. Virol. , vol.73 , pp. 72-80
    • Harris, C.E.1    Boden, R.A.2    Astell, C.R.3
  • 23
    • 0032518188 scopus 로고    scopus 로고
    • Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimmune antibody: Immunological relationship with hnRNP P
    • Hassfeld, W., Chan, E.K.L., Mathison, D.A., Portman, D., Dreyfuss, G., Steiner, G., and Tan, E.M. (1998). Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimmune antibody: immunological relationship with hnRNP P. Nucleic Acids Res. 26, 439-445.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 439-445
    • Hassfeld, W.1    Chan, E.K.L.2    Mathison, D.A.3    Portman, D.4    Dreyfuss, G.5    Steiner, G.6    Tan, E.M.7
  • 24
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S.M., Sternglanz, R., Cheng, P.F., and Weintraub, H. (1995). Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell Biol. 15, 3813-3822.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 25
    • 0032823313 scopus 로고    scopus 로고
    • Induction of interleukin-8 synthesis integrates on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways
    • Holtmann, H., Winzen, R., Holland, P., Eickemeier, S., Hofmann, E., Wallach, D., Malinin, N.L., Cooper, J.A., Resch, K., and Kracht, M. (1999). Induction of interleukin-8 synthesis integrates on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways. Mol. Cell Biol. 19, 6742-6753.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6742-6753
    • Holtmann, H.1    Winzen, R.2    Holland, P.3    Eickemeier, S.4    Hofmann, E.5    Wallach, D.6    Malinin, N.L.7    Cooper, J.A.8    Resch, K.9    Kracht, M.10
  • 26
    • 0028285260 scopus 로고
    • AU-A, an RNA-binding activity distinct from hnRNP A1, is selective for AUUUA repeats and shuttles between the nucleus and the cytoplasm
    • Katz, D.A., Theodorakis, N.G., Cleveland, D.W., Lindsten, T., and Thompson, C.B. (1994). AU-A, an RNA-binding activity distinct from hnRNP A1, is selective for AUUUA repeats and shuttles between the nucleus and the cytoplasm. Nucleic Acids Res. 22, 238-246.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 238-246
    • Katz, D.A.1    Theodorakis, N.G.2    Cleveland, D.W.3    Lindsten, T.4    Thompson, C.B.5
  • 27
    • 0030856470 scopus 로고    scopus 로고
    • Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the α-globin mRNA stability complex
    • Kiledjian, M., DeMaria, C., Brewer, G., and Novick, K. (1997). Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the α-globin mRNA stability complex. Mol. Cell Biol. 17, 4870-4876.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4870-4876
    • Kiledjian, M.1    DeMaria, C.2    Brewer, G.3    Novick, K.4
  • 28
    • 0034607554 scopus 로고    scopus 로고
    • Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm
    • Kim, J.H., Hahm, B., Kim, Y.K., Choi, M., and Jang, S.K. (2000). Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. J. Mol. Biol. 298, 395-405.
    • (2000) J. Mol. Biol. , vol.298 , pp. 395-405
    • Kim, J.H.1    Hahm, B.2    Kim, Y.K.3    Choi, M.4    Jang, S.K.5
  • 29
    • 0025815967 scopus 로고
    • Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein
    • Kolluri, R. and Kinniburgh, A.J. (1991). Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein. Nucleic Acids Res. 19, 4771.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4771
    • Kolluri, R.1    Kinniburgh, A.J.2
  • 30
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia, G., Cuesta, R., Brewer, G., and Schneider, R.J. (1999). Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284, 499-502.
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 31
    • 0037133276 scopus 로고    scopus 로고
    • Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs
    • Laroia, G., Sarkar, B., and Schneider, R.J. (2002). Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs. Proc. Natl. Acad. Sci. USA 99, 1842-1846.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1842-1846
    • Laroia, G.1    Sarkar, B.2    Schneider, R.J.3
  • 32
    • 0023781398 scopus 로고
    • Activation of the transforming potential of the human fos proto-oncogene requires message stabilization and results in increased amounts of partially modified fos protein
    • Lee, W.M., Lin, C., and Curran, T. (1988). Activation of the transforming potential of the human fos proto-oncogene requires message stabilization and results in increased amounts of partially modified fos protein. Mol. Cell Biol. 8, 5521-5527.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 5521-5527
    • Lee, W.M.1    Lin, C.2    Curran, T.3
  • 33
    • 0027314350 scopus 로고
    • Hel-N1: An autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs
    • Levine, T. D., Gao, F., King, H. K., Andrews, L. G., and Keene, J. D. (1993). Hel-N1: an autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs. Mol. Cell Biol. 13, 3494-3504.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3494-3504
    • Levine, T.D.1    Gao, F.2    King, H.K.3    Andrews, L.G.4    Keene, J.D.5
  • 34
    • 0029787504 scopus 로고    scopus 로고
    • Translational repression dependent on the interaction of the Xenopus Y-box protein FRGY2 with mRNA. Role of the cold shock domain, tail domain, and selective RNA sequence recognition
    • Matsumoto, K., Meric, F., and Wolffe, A.P. (1996). Translational repression dependent on the interaction of the Xenopus Y-box protein FRGY2 with mRNA. Role of the cold shock domain, tail domain, and selective RNA sequence recognition. J. Biol. Chem. 271, 22706-22712.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22706-22712
    • Matsumoto, K.1    Meric, F.2    Wolffe, A.P.3
  • 35
    • 0032147094 scopus 로고    scopus 로고
    • Gene regulation by Y-box proteins: Coupling control of transcription and translation
    • Matsumoto, K. and Wolffe, A.P. (1998). Gene regulation by Y-box proteins: coupling control of transcription and translation. Trends Cell Biol. 8, 318-323.
    • (1998) Trends Cell Biol. , vol.8 , pp. 318-323
    • Matsumoto, K.1    Wolffe, A.P.2
  • 36
    • 0035985073 scopus 로고    scopus 로고
    • Analysis of the structural determinants for the RNA binding of the human protein AUF1/hnRNP D
    • Moraes, K.C.M., Lee, W.H., and Kobarg, J. (2002). Analysis of the structural determinants for the RNA binding of the human protein AUF1/hnRNP D. Biol. Chem. 383, 831-837.
    • (2002) Biol. Chem. , vol.383 , pp. 831-837
    • Moraes, K.C.M.1    Lee, W.H.2    Kobarg, J.3
  • 37
    • 0026604557 scopus 로고
    • Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins
    • Murray, M.T., Schiller, D.L., and Franke, W.W. (1992). Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins. Proc. Natl. Acad. Sci. USA 89, 11-15.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11-15
    • Murray, M.T.1    Schiller, D.L.2    Franke, W.W.3
  • 39
    • 0032908981 scopus 로고    scopus 로고
    • A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development
    • Nielsen, J., Christiansen, J., Lykke-Andersen, J., Johnsen, A.H., Wewer, U.M., and Nielsen, F.C. (1999). A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development. Mol. Cell Biol. 19, 1262-1270.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1262-1270
    • Nielsen, J.1    Christiansen, J.2    Lykke-Andersen, J.3    Johnsen, A.H.4    Wewer, U.M.5    Nielsen, F.C.6
  • 41
    • 0024290216 scopus 로고
    • The elav gene product of Drosophila, required in neurons, has three RNP consensus motifs
    • Robinow, S., Campos, A.R., Yao, K.M., and White, K. (1988). The elav gene product of Drosophila, required in neurons, has three RNP consensus motifs. Science 242, 1570-1572.
    • (1988) Science , vol.242 , pp. 1570-1572
    • Robinow, S.1    Campos, A.R.2    Yao, K.M.3    White, K.4
  • 42
    • 0029165020 scopus 로고
    • mRNA stability in mammalian cells
    • Ross, J. (1995). mRNA stability in mammalian cells. Microbiol. Rev. 59, 423-450.
    • (1995) Microbiol. Rev. , vol.59 , pp. 423-450
    • Ross, J.1
  • 43
    • 0035114391 scopus 로고    scopus 로고
    • Expression of deletion mutants of the hepatitis B virus protein HBx in E coli and characterization of their RNA binding activities
    • Rui, E., Moura, P.R. and Kobarg, J. (2001). Expression of deletion mutants of the hepatitis B virus protein HBx in E coli and characterization of their RNA binding activities. Virus Res. 74, 59-73.
    • (2001) Virus Res. , vol.74 , pp. 59-73
    • Rui, E.1    Moura, P.R.2    Kobarg, J.3
  • 44
    • 0034686029 scopus 로고    scopus 로고
    • Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein
    • Shnyreva, M., Schullery, D.S., Suzuki, H., Higaki, Y., and Bomsztyk, K. (2000). Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein. J. Biol. Chem. 275, 15498-15503.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15498-15503
    • Shnyreva, M.1    Schullery, D.S.2    Suzuki, H.3    Higaki, Y.4    Bomsztyk, K.5
  • 45
    • 0024948946 scopus 로고
    • A nuclear DNA attachment element mediates elevated and position-independent gene activity
    • Stief, A., Winter, D.M., Stratling, W.H., and Sippel, A.E. (1989). A nuclear DNA attachment element mediates elevated and position-independent gene activity. Nature 341, 343-345.
    • (1989) Nature , vol.341 , pp. 343-345
    • Stief, A.1    Winter, D.M.2    Stratling, W.H.3    Sippel, A.E.4
  • 46
    • 0029099409 scopus 로고
    • Ras-Raf interaction: Two-hybrid analysis
    • Vojtek, A.B. and Hollenberg, S.M. (1995). Ras-Raf interaction: two-hybrid analysis. Methods Enzymol. 255, 331-342.
    • (1995) Methods Enzymol. , vol.255 , pp. 331-342
    • Vojtek, A.B.1    Hollenberg, S.M.2
  • 47
    • 0032033151 scopus 로고    scopus 로고
    • Structure and genomic organization of the human AUF1 gene: Alternative pre-mRNA splicing generates four protein isoforms
    • Wagner, B.J., DeMaria, C.T, Sun, Y., Wilson, G.M., and Brewer, G. (1998). Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms. Genomics 48, 195-202.
    • (1998) Genomics , vol.48 , pp. 195-202
    • Wagner, B.J.1    DeMaria, C.T.2    Sun, Y.3    Wilson, G.M.4    Brewer, G.5
  • 49
    • 0033585005 scopus 로고    scopus 로고
    • Assembly of AUF1 oligomers on U-rich RNA targets by sequential dimer association
    • Wilson, G.M., Sun, Y., Lu, H., and Brewer, G. (1999). Assembly of AUF1 oligomers on U-rich RNA targets by sequential dimer association. J. Biol. Chem. 274, 33374-33381.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33374-33381
    • Wilson, G.M.1    Sun, Y.2    Lu, H.3    Brewer, G.4
  • 50
    • 0033568608 scopus 로고    scopus 로고
    • The MAP kinase pathway signals for cytokine-induced mRNA stabilization via kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism
    • Winzen, R., Kracht, M., Ritter, B., Wihelm, A., Chen, C.Y., Shyu, A.B., Muller, M., Gaestel, M., Resch, K., and Holtmann, H. (1999). The MAP kinase pathway signals for cytokine-induced mRNA stabilization via kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism. EMBO J. 18, 4969-4980.
    • (1999) EMBO J. , vol.18 , pp. 4969-4980
    • Winzen, R.1    Kracht, M.2    Ritter, B.3    Wihelm, A.4    Chen, C.Y.5    Shyu, A.B.6    Muller, M.7    Gaestel, M.8    Resch, K.9    Holtmann, H.10
  • 51
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • Xu, N., Chyi-Ying, A.C., and Shyu, A.B. (2001). Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol. Cell Biol. 21, 6960-6971.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 6960-6971
    • Xu, N.1    Chyi-Ying, A.C.2    Shyu, A.B.3
  • 52
    • 0033526101 scopus 로고    scopus 로고
    • A novel cytoplasmic protein with RNA-binding motifs is an autoantigen in human hepatocellular carcinoma
    • Zhang, J.Y., Chan, E.K., Peng, X.X., and Tan, E.M. (1999). A novel cytoplasmic protein with RNA-binding motifs is an autoantigen in human hepatocellular carcinoma. J. Exp. Med. 189, 1101-1110.
    • (1999) J. Exp. Med. , vol.189 , pp. 1101-1110
    • Zhang, J.Y.1    Chan, E.K.2    Peng, X.X.3    Tan, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.