메뉴 건너뛰기




Volumn 283, Issue 2, 2003, Pages 184-195

Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; MESSENGER RNA; NUCLEIC ACID BINDING PROTEIN; ONCOPROTEIN; PROTEIN; PROTEIN SC35; PROTEIN SR; PROTEIN SRM160; PROTEIN SRP75; PROTO ONCOPROTEIN TLS FUS; RECOMBINANT PROTEIN; SPLICING FACTOR PTB; UNCLASSIFIED DRUG;

EID: 0344407006     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(02)00046-0     Document Type: Article
Times cited : (97)

References (59)
  • 1
  • 2
    • 0032979579 scopus 로고    scopus 로고
    • Direct visualization of a protein nuclear architecture
    • Hendzel M.J., Boisvert F., Bazett Jones D.P. Direct visualization of a protein nuclear architecture. Mol. Biol. Cell. 10:1999;2051-2062.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2051-2062
    • Hendzel, M.J.1    Boisvert, F.2    Bazett Jones, D.P.3
  • 5
    • 0029799798 scopus 로고    scopus 로고
    • Functional interrelationships between nuclear structure and transcriptional control: Contributions to regulation of cell cycle- and tissue-specific gene expression
    • Stein G.S., Stein J.L., Lian J.B., van Wijnen A.J., Montecino M. Functional interrelationships between nuclear structure and transcriptional control contributions to regulation of cell cycle- and tissue-specific gene expression . J. Cell. Biochem. 62:1996;198-209.
    • (1996) J. Cell. Biochem. , vol.62 , pp. 198-209
    • Stein, G.S.1    Stein, J.L.2    Lian, J.B.3    Van Wijnen, A.J.4    Montecino, M.5
  • 7
    • 0033560042 scopus 로고    scopus 로고
    • Self assembly of NuMA: Multiarm oligomers as structural units of a nuclear lattice
    • Harborth J., Wang J., Gueth Hallonet C., Weber K., Osborn M. Self assembly of NuMA multiarm oligomers as structural units of a nuclear lattice . EMBO J. 18:1999;1689-1700.
    • (1999) EMBO J. , vol.18 , pp. 1689-1700
    • Harborth, J.1    Wang, J.2    Gueth Hallonet, C.3    Weber, K.4    Osborn, M.5
  • 8
    • 0022521416 scopus 로고
    • The nonchromatin substructures of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy
    • Fey E.G., Krochmalnic G., Penman S. The nonchromatin substructures of the nucleus the ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy . J. Cell Biol. 102:1986;1654-1665.
    • (1986) J. Cell Biol. , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Krochmalnic, G.2    Penman, S.3
  • 9
    • 0033538831 scopus 로고    scopus 로고
    • Three-dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles
    • Wei X., Somanathan S., Samarabandu J., Berezney R. Three-dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles. J. Cell Biol. 146:1999;543-558.
    • (1999) J. Cell Biol. , vol.146 , pp. 543-558
    • Wei, X.1    Somanathan, S.2    Samarabandu, J.3    Berezney, R.4
  • 10
    • 0031834613 scopus 로고    scopus 로고
    • The cellular organization of gene expression
    • Misteli T., Spector D.L. The cellular organization of gene expression. Curr. Opin. Cell Biol. 10:1998;323-331.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 323-331
    • Misteli, T.1    Spector, D.L.2
  • 11
    • 0030909002 scopus 로고    scopus 로고
    • Dynamic relocation of transcription and splicing factors dependent upon transcriptional activity
    • Zeng C., Kim E., Warren S.L., Berget S.M. Dynamic relocation of transcription and splicing factors dependent upon transcriptional activity. EMBO J. 16:1997;1401-1412.
    • (1997) EMBO J. , vol.16 , pp. 1401-1412
    • Zeng, C.1    Kim, E.2    Warren, S.L.3    Berget, S.M.4
  • 13
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Kramer 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
    • Kramer, A.1
  • 15
    • 0027160003 scopus 로고
    • Distinct functions of SR proteins in alternative pre-mRNA splicing
    • Zahler A.M., Neugebauer K.M., Lane W.S., Roth M.B. Distinct functions of SR proteins in alternative pre-mRNA splicing. Science. 260:1993;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
  • 16
    • 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
  • 17
    • 0033152209 scopus 로고    scopus 로고
    • Determinants of SR protein specificity
    • Tacke R., Manley J.L. Determinants of SR protein specificity. Curr. Opin. Cell Biol. 11:1999;358-362.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 358-362
    • Tacke, R.1    Manley, J.L.2
  • 19
    • 0033022124 scopus 로고    scopus 로고
    • The SRm160/300 splicing coactivator is required for exon-enhancer function
    • Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J. The SRm160/300 splicing coactivator is required for exon-enhancer function. Proc. Natl. Acad. Sci. USA. 96:1999;6125-6130.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6125-6130
    • Eldridge, A.G.1    Li, Y.2    Sharp, P.A.3    Blencowe, B.J.4
  • 20
    • 0029053747 scopus 로고
    • Association of SARFH (sarcoma- associated RNA-binding fly homolog) with regions of chromatin transcribed by RNA polymerase II
    • Immanuel D., Zinszner H., Ron D. Association of SARFH (sarcoma- associated RNA-binding fly homolog) with regions of chromatin transcribed by RNA polymerase II. Mol. Cell. Biol. 15:1995;4562-4571.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4562-4571
    • Immanuel, D.1    Zinszner, H.2    Ron, D.3
  • 21
    • 0032561190 scopus 로고    scopus 로고
    • Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing
    • Yang L., Embree L.J., Tsai S., Hickstein D.D. Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing. J. Biol. Chem. 273:1998;27761-27764.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27761-27764
    • Yang, L.1    Embree, L.J.2    Tsai, S.3    Hickstein, D.D.4
  • 22
    • 0027276357 scopus 로고
    • Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma
    • Rabbitts T.H., Forster A., Larson R., Nathan P. Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma. Nature Genet. 4:1993;175-180.
    • (1993) Nature Genet. , vol.4 , pp. 175-180
    • Rabbitts, T.H.1    Forster, A.2    Larson, R.3    Nathan, P.4
  • 23
    • 0027227651 scopus 로고
    • Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
    • Crozat A., Aman P., Mandahl N., Ron D. Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature. 363:1993;640-644.
    • (1993) Nature , vol.363 , pp. 640-644
    • Crozat, A.1    Aman, P.2    Mandahl, N.3    Ron, D.4
  • 24
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner H., Sok J., Immanuel D., Yin Y., Ron D. TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J. Cell Sci. 110:1997;1741-1750.
    • (1997) J. Cell Sci. , vol.110 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5
  • 25
    • 0027972301 scopus 로고
    • A 69-kD protein that associates reversibly with the Sm core domain of several spliceosomal snRNP species
    • Hackl W., Fischer U., Luhrmann R. A 69-kD protein that associates reversibly with the Sm core domain of several spliceosomal snRNP species. J. Cell Biol. 124:1994;261-272.
    • (1994) J. Cell Biol. , vol.124 , pp. 261-272
    • Hackl, W.1    Fischer, U.2    Luhrmann, R.3
  • 26
    • 0030588652 scopus 로고    scopus 로고
    • Cloning and mapping of a human RBP56 gene encoding a putative RNA binding protein similar to FUS/TLS and EWS proteins
    • Morohoshi F., Arai K., Takahashi E.I., Tanigami A., Ohki M. Cloning and mapping of a human RBP56 gene encoding a putative RNA binding protein similar to FUS/TLS and EWS proteins. Genomics. 38:1996;51-57.
    • (1996) Genomics , vol.38 , pp. 51-57
    • Morohoshi, F.1    Arai, K.2    Takahashi, E.I.3    Tanigami, A.4    Ohki, M.5
  • 28
    • 0029812470 scopus 로고    scopus 로고
    • HTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • Bertolotti A., Lutz Y., Heard D.J., Chambon P., Tora L. hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II. EMBO J. 15:1996;5022-5031.
    • (1996) EMBO J. , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 29
    • 0029372980 scopus 로고
    • Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry
    • Calvio C., Neubauer G., Mann M., Lamond A.I. Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry. RNA. 1:1995;724-733.
    • (1995) RNA , vol.1 , pp. 724-733
    • Calvio, C.1    Neubauer, G.2    Mann, M.3    Lamond, A.I.4
  • 30
    • 0027970712 scopus 로고
    • A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
    • Zinszner H., Albalat R., Ron D. A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP. Genes Dev. 8:1994;2513-2526.
    • (1994) Genes Dev. , vol.8 , pp. 2513-2526
    • Zinszner, H.1    Albalat, R.2    Ron, D.3
  • 31
    • 0031883847 scopus 로고    scopus 로고
    • Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing
    • Zhang W.J., Wu J.Y. Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing. Mol. Cell. Biol. 18:1998;676-684.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 676-684
    • Zhang, W.J.1    Wu, J.Y.2
  • 32
    • 0034053964 scopus 로고    scopus 로고
    • TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins
    • Yang L., Embree L.J., Hickstein D.D. TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Mol. Cell. Biol. 20:2000;3345-3354.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3345-3354
    • Yang, L.1    Embree, L.J.2    Hickstein, D.D.3
  • 33
    • 0033527059 scopus 로고    scopus 로고
    • Human POMp75 is identified as the pro-oncoprotein TLS/FUS: Both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation
    • Bertrand P., Akhmedov A.T., Delacote F., Durrbach A., Lopez B.S. Human POMp75 is identified as the pro-oncoprotein TLS/FUS both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation . Oncogene. 18:1999;4515-4521.
    • (1999) Oncogene , vol.18 , pp. 4515-4521
    • Bertrand, P.1    Akhmedov, A.T.2    Delacote, F.3    Durrbach, A.4    Lopez, B.S.5
  • 36
    • 0031053676 scopus 로고    scopus 로고
    • Identification of human common nuclear-matrix proteins as heterogeneous nuclear ribonucleoproteins H and H′ by sequencing and mass spectrometry
    • Holzmann K., Korosec T., Gerner C., Grimm R., Sauermann G. Identification of human common nuclear-matrix proteins as heterogeneous nuclear ribonucleoproteins H and H′ by sequencing and mass spectrometry. Eur. J. Biochem. 244:1997;479-486.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 479-486
    • Holzmann, K.1    Korosec, T.2    Gerner, C.3    Grimm, R.4    Sauermann, G.5
  • 37
  • 38
    • 0022962481 scopus 로고
    • Analysis of cytoskeletal structures using blot-purified monospecific antibodies
    • Olmsted, J.B. Analysis of cytoskeletal structures using blot-purified monospecific antibodies. Methods Enzymol. (1986) 134467-134472.
    • (1986) Methods Enzymol. , pp. 134467-134472
    • Olmsted, J.B.1
  • 39
    • 0032401696 scopus 로고    scopus 로고
    • Similarity between nuclear matrix proteins of various cells revealed by an improved isolation method
    • Gerner C., Holzmann K., Grimm R., Sauermann G. Similarity between nuclear matrix proteins of various cells revealed by an improved isolation method. J. Cell. Biochem. 71:1998;363-374.
    • (1998) J. Cell. Biochem. , vol.71 , pp. 363-374
    • Gerner, C.1    Holzmann, K.2    Grimm, R.3    Sauermann, G.4
  • 40
    • 0027151934 scopus 로고
    • Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF [published erratum appears in Mol. Cell. Biol. 13 (1993) 4458]
    • Mayeda A., Helfman D.M., Krainer A.R. Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF [published erratum appears in Mol. Cell. Biol. 13 (1993) 4458]. Mol. Cell. Biol. 13:1993;2993-3001.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2993-3001
    • Mayeda, A.1    Helfman, D.M.2    Krainer, A.R.3
  • 42
    • 0033953914 scopus 로고    scopus 로고
    • Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB
    • Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G. Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB. J. Cell. Biochem. 76:2000;559-566.
    • (2000) J. Cell. Biochem. , vol.76 , pp. 559-566
    • Meissner, M.1    Dechat, T.2    Gerner, C.3    Grimm, R.4    Foisner, R.5    Sauermann, G.6
  • 43
    • 0031409292 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis reveals a nuclear matrix-associated nucleolin complex of basic isoelectric point
    • Gotzmann J., Eger A., Meissner M., Grimm R., Gerner C., Sauermann G., Foisner R. Two-dimensional electrophoresis reveals a nuclear matrix-associated nucleolin complex of basic isoelectric point. Electrophoresis. 18:1997;2645-2653.
    • (1997) Electrophoresis , vol.18 , pp. 2645-2653
    • Gotzmann, J.1    Eger, A.2    Meissner, M.3    Grimm, R.4    Gerner, C.5    Sauermann, G.6    Foisner, R.7
  • 44
    • 0033997258 scopus 로고    scopus 로고
    • A method to produce Ponceau replicas from blots: Application for Western analysis
    • Gotzmann J., Gerner C. A method to produce Ponceau replicas from blots application for Western analysis . Electrophoresis. 21:2000;523-525.
    • (2000) Electrophoresis , vol.21 , pp. 523-525
    • Gotzmann, J.1    Gerner, C.2
  • 45
    • 0021223245 scopus 로고
    • Normal and mutant human beta-globin pre-mRNAs are faithfully and efficiently spliced in vitro
    • Krainer A.R., Maniatis T., Ruskin B., Green M.R. Normal and mutant human beta-globin pre-mRNAs are faithfully and efficiently spliced in vitro. Cell. 36:1984;993-1005.
    • (1984) Cell , vol.36 , pp. 993-1005
    • Krainer, A.R.1    Maniatis, T.2    Ruskin, B.3    Green, M.R.4
  • 46
    • 0024967111 scopus 로고
    • Structure of an Arabidopsis thaliana cDNA encoding rubisco activase
    • Werneke J.M., Ogren W.L. Structure of an Arabidopsis thaliana cDNA encoding rubisco activase. Nucleic Acids Res. 17:1989;2871.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 2871
    • Werneke, J.M.1    Ogren, W.L.2
  • 47
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • Misteli T., Caceres J.F., Clement J.Q., Krainer A.R., Wilkinson M.F., Spector D.L. Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo. J. Cell Biol. 143:(2):1998;297-307.
    • (1998) J. Cell Biol. , vol.143 , Issue.2 , pp. 297-307
    • Misteli, T.1    Caceres, J.F.2    Clement, J.Q.3    Krainer, A.R.4    Wilkinson, M.F.5    Spector, D.L.6
  • 48
    • 0033559277 scopus 로고    scopus 로고
    • Nuclear matrix proteins specific for subtypes of human hematopoietic cells
    • Gerner C., Sauermann G. Nuclear matrix proteins specific for subtypes of human hematopoietic cells. J. Cell. Biochem. 72:1999;470-482.
    • (1999) J. Cell. Biochem. , vol.72 , pp. 470-482
    • Gerner, C.1    Sauermann, G.2
  • 49
    • 0030829950 scopus 로고    scopus 로고
    • Common nuclear matrix proteins in rat tissues
    • Korosec T., Gerner C., Sauermann G. Common nuclear matrix proteins in rat tissues. Electrophoresis. 18:1997;2109-2115.
    • (1997) Electrophoresis , vol.18 , pp. 2109-2115
    • Korosec, T.1    Gerner, C.2    Sauermann, G.3
  • 51
    • 0025856790 scopus 로고
    • Characterization and molecular cloning of polypyrimidine tract-binding protein: A component of a complex necessary for pre-mRNA splicing
    • Patton J.G., Mayer S.A., Tempst P., Nadal Ginard B. Characterization and molecular cloning of polypyrimidine tract-binding protein a component of a complex necessary for pre-mRNA splicing . Genes Dev. 5:1991;1237-1251.
    • (1991) Genes Dev. , vol.5 , pp. 1237-1251
    • Patton, J.G.1    Mayer, S.A.2    Tempst, P.3    Nadal Ginard, B.4
  • 52
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth M.B., Zahler A.M., Stolk J.A. A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J. Cell Biol. 115:1991;587-596.
    • (1991) J. Cell Biol. , vol.115 , pp. 587-596
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 53
    • 0028034042 scopus 로고
    • Association of nuclear matrix antigens with exon-containing splicing complexes
    • Blencowe B.J., Nickerson J.A., Issner R., Penman S., Sharp P.A. Association of nuclear matrix antigens with exon-containing splicing complexes. J. Cell Biol. 127:1994;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
  • 54
    • 0025719396 scopus 로고
    • Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors
    • Huang S., Spector D.L. Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors. Genes Dev. 5:1991;2288-2302.
    • (1991) Genes Dev. , vol.5 , pp. 2288-2302
    • Huang, S.1    Spector, D.L.2
  • 55
    • 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., Mayeda A., Maniatis T., Krainer A.R. 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. 89:1992;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
  • 56
    • 0030855063 scopus 로고    scopus 로고
    • Identification of a human protein that recognizes the 3′ splice site during the second step of pre-mRNA splicing
    • Wu S., Green M.R. Identification of a human protein that recognizes the 3′ splice site during the second step of pre-mRNA splicing. EMBO J. 16:1997;4421-4432.
    • (1997) EMBO J. , vol.16 , pp. 4421-4432
    • Wu, S.1    Green, M.R.2
  • 57
    • 0032570707 scopus 로고    scopus 로고
    • The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS
    • Hallier M., Lerga A., Barnache S., Tavitian A., Moreau Gachelin F. The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS. J. Biol. Chem. 273:1998;4838-4842.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4838-4842
    • Hallier, M.1    Lerga, A.2    Barnache, S.3    Tavitian, A.4    Moreau Gachelin, F.5
  • 58
    • 0031935157 scopus 로고    scopus 로고
    • EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: Interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes
    • Bertolotti A., Melot T., Acker J., Vigneron M., Delattre O., Tora L. EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes . Mol. Cell. Biol. 18:1998;1489-1497.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1489-1497
    • Bertolotti, A.1    Melot, T.2    Acker, J.3    Vigneron, M.4    Delattre, O.5    Tora, L.6
  • 59


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.