메뉴 건너뛰기




Volumn 371, Issue 2, 2003, Pages 331-340

A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins

Author keywords

Heterogeneous nuclear ribonucleoprotein (hnRNP); Peptide mass fingerprinting; Poly(ADP ribose) (pADPr); Proteomic

Indexed keywords

CELLS; DATABASE SYSTEMS; LASER APPLICATIONS; MEMBRANES;

EID: 0038641860     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021675     Document Type: Article
Times cited : (95)

References (41)
  • 1
    • 0018723423 scopus 로고
    • Poly(ADP-ribose) levels in carcinogen-treated cells
    • Juarez-Salinas, H., Sims, J. L. and Jacobson, M. K. (1979) Poly(ADP-ribose) levels in carcinogen-treated cells. Nature (London) 282, 740-741
    • (1979) Nature (London) , vol.282 , pp. 740-741
    • Juarez-Salinas, H.1    Sims, J.L.2    Jacobson, M.K.3
  • 2
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl, T., Satoh, M. S., Poirier, G. G. and Klungland, A. (1995) Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20, 405-411
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 3
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours, D., Desnoyers, S., D'Silva, I. and Poirier, G. G. (1999) Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342, 249-268
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 5
    • 0036069642 scopus 로고    scopus 로고
    • tej defines a role for poly(ADP-ribosyl)ation in establishing period length of the Arabidopsis circadian oscillator
    • Panda, S., Poirier, G. G. and Kay, S. A. (2002) tej defines a role for poly(ADP-ribosyl)ation in establishing period length of the Arabidopsis circadian oscillator. Dev. Cell 3, 51-61
    • (2002) Dev. Cell , vol.3 , pp. 51-61
    • Panda, S.1    Poirier, G.G.2    Kay, S.A.3
  • 7
    • 0019876860 scopus 로고
    • Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei
    • Ogata, N., Ueda, K., Kawaichi, M. and Hayaishi, O. (1981) Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei. J. Biol. Chem. 256, 4135-4137
    • (1981) J. Biol. Chem. , vol.256 , pp. 4135-4137
    • Ogata, N.1    Ueda, K.2    Kawaichi, M.3    Hayaishi, O.4
  • 8
    • 0033153348 scopus 로고    scopus 로고
    • hnRNP complexes: Composition, structure, and function
    • Krecic, A. M. and Swanson, M. S. (1999) hnRNP complexes: composition, structure, and function. Curr. Opin. Cell Biol. 11, 363-371
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 363-371
    • Krecic, A.M.1    Swanson, M.S.2
  • 9
    • 0026770678 scopus 로고
    • Differential binding of heterogeneous nuclear ribonucleoproteins to mRNA precursors prior to spliceosome assembly in vitro
    • Bennett, M., Pinol-Roma, S., Staknis, D., Dreyfuss, G. and Reed, R. (1992) Differential binding of heterogeneous nuclear ribonucleoproteins to mRNA precursors prior to spliceosome assembly in vitro. Mol. Cell. Biol. 12, 3165-3175
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3165-3175
    • Bennett, M.1    Pinol-Roma, S.2    Staknis, D.3    Dreyfuss, G.4    Reed, R.5
  • 10
    • 0035369702 scopus 로고    scopus 로고
    • Selection and identification of proteins bound to DNA triple-helical structures by combination of 2D-electrophoresis and MALDI-TOF mass spectrometry
    • Guillonneau, F., Guieysse, A. L., Le Caer, J. P., Rossier, J. and Praseuth, D. (2001) Selection and identification of proteins bound to DNA triple-helical structures by combination of 2D-electrophoresis and MALDI-TOF mass spectrometry. Nucleic Acids Res. 29, 2427-2436
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2427-2436
    • Guillonneau, F.1    Guieysse, A.L.2    Le Caer, J.P.3    Rossier, J.4    Praseuth, D.5
  • 11
    • 0034744376 scopus 로고    scopus 로고
    • Interaction between hnRNPA1 and IκBα is required for maximal activation of NF-κB-dependent transcription
    • Hay, D. C., Kemp, G. D., Dargemont, C. and Hay, R. T. (2001) Interaction between hnRNPA1 and IκBα is required for maximal activation of NF-κB-dependent transcription. Mol. Cell. Biol. 21, 3482-3490
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3482-3490
    • Hay, D.C.1    Kemp, G.D.2    Dargemont, C.3    Hay, R.T.4
  • 13
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway
    • Michael, W. M., Choi, M. and Dreyfuss, G. (1995) A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83, 415-422
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 14
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma, S. and Dreyfuss, G. (1992) Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature (London) 355, 730-732
    • (1992) Nature (London) , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 15
    • 0037148269 scopus 로고    scopus 로고
    • A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation
    • Ford, L. P., Wright, W. E. and Shay, J. W. (2002) A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation. Oncogene 21, 580-583
    • (2002) Oncogene , vol.21 , pp. 580-583
    • Ford, L.P.1    Wright, W.E.2    Shay, J.W.3
  • 17
    • 0027481140 scopus 로고
    • Mammalian heterogeneous ribonucleoprotein A1 and its constituent domains. Nucleic acid interaction, structural stability and self-association
    • Casas-Finet, J. R., Smith, Jr, J. D., Kumar, A., Kim, J. G., Wilson, S. H. and Karpel, R. L. (1993) Mammalian heterogeneous ribonucleoprotein A1 and its constituent domains. Nucleic acid interaction, structural stability and self-association. J. Mol. Biol. 229, 873-889
    • (1993) J. Mol. Biol. , vol.229 , pp. 873-889
    • Casas-Finet, J.R.1    Smith J.D., Jr.2    Kumar, A.3    Kim, J.G.4    Wilson, S.H.5    Karpel, R.L.6
  • 18
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda, A., Munroe, S. H., Caceres, J. F. and Krainer, A. R. (1994) Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. EMBO J. 13, 5483-5495
    • (1994) EMBO J. , vol.13 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 19
    • 0032561365 scopus 로고    scopus 로고
    • Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3
    • Brockstedt, E., Rickers, A., Kostka, S., Laubersheimer, A., Dorken, B., Wittmann-Liebold, B., Bommert, K. and Otto, A. (1998) Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3. J. Biol. Chem. 273, 28057-28064
    • (1998) J. Biol. Chem. , vol.273 , pp. 28057-28064
    • Brockstedt, E.1    Rickers, A.2    Kostka, S.3    Laubersheimer, A.4    Dorken, B.5    Wittmann-Liebold, B.6    Bommert, K.7    Otto, A.8
  • 20
    • 0035854661 scopus 로고    scopus 로고
    • Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis
    • Thiede, B., Dimmler, C., Siejak, F. and Rudel, T. (2001) Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J. Biol. Chem. 276, 26044-26050
    • (2001) J. Biol. Chem. , vol.276 , pp. 26044-26050
    • Thiede, B.1    Dimmler, C.2    Siejak, F.3    Rudel, T.4
  • 21
    • 0036668524 scopus 로고    scopus 로고
    • Prediction of translocation and cleavage of heterogeneous ribonuclear proteins and Rho guanine nucleotide dissociation inhibitor 2 during apoptosis by subcellular proteome analysis
    • Thiede, B., Siejak, F., Dimmler, C. and Rudel, T. (2002) Prediction of translocation and cleavage of heterogeneous ribonuclear proteins and Rho guanine nucleotide dissociation inhibitor 2 during apoptosis by subcellular proteome analysis. Proteomics 2, 996-1006
    • (2002) Proteomics , vol.2 , pp. 996-1006
    • Thiede, B.1    Siejak, F.2    Dimmler, C.3    Rudel, T.4
  • 22
    • 0035525595 scopus 로고    scopus 로고
    • Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis
    • Mortz, E., Krogh, T. N., Vorum, H. and Gorg, A. (2001) Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 1, 1359-1363
    • (2001) Proteomics , vol.1 , pp. 1359-1363
    • Mortz, E.1    Krogh, T.N.2    Vorum, H.3    Gorg, A.4
  • 23
    • 0023375254 scopus 로고
    • Rapid assay of poly(ADP-ribose) glycohydrolase
    • Ménard, L. and Poirier, G. G. (1987) Rapid assay of poly(ADP-ribose) glycohydrolase. Biochem. Cell. Biol. 65, 668-673
    • (1987) Biochem. Cell. Biol. , vol.65 , pp. 668-673
    • Ménard, L.1    Poirier, G.G.2
  • 24
    • 0021475340 scopus 로고
    • Poly(ADP-ribose) polymerase is a zinc metalloenzyme
    • Zahradka, P. and Ebisuzaki, K. (1984) Poly(ADP-ribose) polymerase is a zinc metalloenzyme. Eur. J. Biochem. 142, 503-509
    • (1984) Eur. J. Biochem. , vol.142 , pp. 503-509
    • Zahradka, P.1    Ebisuzaki, K.2
  • 27
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke, J. M., Kleczkowska, H. E., Strohm, M. and Althaus, F. R. (2000) Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 30
    • 0026781175 scopus 로고
    • Retroviral insertions downstream of the heterogeneous nuclear ribonucleoprotein A1 gene in erythroleukemia cells: Evidence that A1 is not essential for cell growth
    • Ben-David, Y., Bani, M. R., Chabot, B., De Koven, A. and Bernstein, A. (1992) Retroviral insertions downstream of the heterogeneous nuclear ribonucleoprotein A1 gene in erythroleukemia cells: evidence that A1 is not essential for cell growth. Mol. Cell. Biol. 12, 4449-4455
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4449-4455
    • Ben-David, Y.1    Bani, M.R.2    Chabot, B.3    De Koven, A.4    Bernstein, A.5
  • 31
    • 0031800617 scopus 로고    scopus 로고
    • Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase
    • LaBranche, H., Dupuis, S., Ben-David, Y., Bani, M. R., Wellinger, R. J. and Chabot, B. (1998) Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase. Nat. Genet. 19, 199-202
    • (1998) Nat. Genet. , vol.19 , pp. 199-202
    • LaBranche, H.1    Dupuis, S.2    Ben-David, Y.3    Bani, M.R.4    Wellinger, R.J.5    Chabot, B.6
  • 33
    • 0027944584 scopus 로고
    • ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells
    • Prasad, S., Walent, J. and Dritschilo, A. (1994) ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells. Biochem. Biophys. Res. Commun. 204, 772-779
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 772-779
    • Prasad, S.1    Walent, J.2    Dritschilo, A.3
  • 34
    • 0026506694 scopus 로고
    • Noncovalent interactions of poly(adenosine diphosphate ribose) with histones
    • Panzeter, P. L., Realini, C. A. and Althaus, F. R. (1992) Noncovalent interactions of poly(adenosine diphosphate ribose) with histones. Biochemistry 31, 1379-1385
    • (1992) Biochemistry , vol.31 , pp. 1379-1385
    • Panzeter, P.L.1    Realini, C.A.2    Althaus, F.R.3
  • 35
    • 0028303576 scopus 로고
    • Non-covalent interaction between poly(ADP-ribose) and cellular proteins: An application of a poly(ADP-ribose)-Western blotting method to detect poly(ADP-ribose) binding on protein-blotted filter
    • Nozaki, T., Masutani, M., Akagawa, T., Sugimura, T. and Esumi, H. (1994) Non-covalent interaction between poly(ADP-ribose) and cellular proteins: an application of a poly(ADP-ribose)-Western blotting method to detect poly(ADP-ribose) binding on protein-blotted filter. Biochem. Biophys. Res. Commun. 198, 45-51
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 45-51
    • Nozaki, T.1    Masutani, M.2    Akagawa, T.3    Sugimura, T.4    Esumi, H.5
  • 36
    • 0032496235 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions
    • Malanga, M., Pleschke, J. M., Kleczkowska, H. E. and Althaus, F. R. (1998) Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J. Biol. Chem. 273, 11839-11843
    • (1998) J. Biol. Chem. , vol.273 , pp. 11839-11843
    • Malanga, M.1    Pleschke, J.M.2    Kleczkowska, H.E.3    Althaus, F.R.4
  • 37
    • 0033527555 scopus 로고    scopus 로고
    • Selective loss of poly(ADP-ribose) and the 85-kDa fragment of poly(ADP-ribose) polymerase in nucleoli during alkylation-induced apoptosis of HeLa cells
    • Alvarez-Gonzalez, R., Spring, H., Muller, M. and Burkle, A. (1999) Selective loss of poly(ADP-ribose) and the 85-kDa fragment of poly(ADP-ribose) polymerase in nucleoli during alkylation-induced apoptosis of HeLa cells. J. Biol. Chem. 274, 32122-32126
    • (1999) J. Biol. Chem. , vol.274 , pp. 32122-32126
    • Alvarez-Gonzalez, R.1    Spring, H.2    Muller, M.3    Burkle, A.4
  • 38
    • 0033214624 scopus 로고    scopus 로고
    • Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7
    • Germain, M., Affar, E. B., D'Amours, D., Dixit, V. M., Salvesen, G. S. and Poirier, G. G. (1999) Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. J. Biol. Chem. 274, 28379-28384
    • (1999) J. Biol. Chem. , vol.274 , pp. 28379-28384
    • Germain, M.1    Affar, E.B.2    D'Amours, D.3    Dixit, V.M.4    Salvesen, G.S.5    Poirier, G.G.6
  • 39
    • 0034961678 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 regulates the stability of the wild-type p53 protein
    • Wesierska-Gadek, J. and Schmid, G. (2001) Poly(ADP-ribose) polymerase-1 regulates the stability of the wild-type p53 protein. Cell. Mol. Biol. Lett. 6, 117-140
    • (2001) Cell. Mol. Biol. Lett. , vol.6 , pp. 117-140
    • Wesierska-Gadek, J.1    Schmid, G.2
  • 41
    • 0036529482 scopus 로고    scopus 로고
    • Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1
    • Vitali, J., Ding, J., Jiang, J., Zhang, Y., Krainer, A. R. and Xu, R. M. (2002) Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. Nucleic Acids Res. 30, 1531-1538
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1531-1538
    • Vitali, J.1    Ding, J.2    Jiang, J.3    Zhang, Y.4    Krainer, A.R.5    Xu, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.