메뉴 건너뛰기




Volumn 18, Issue 1, 1998, Pages 334-342

A novel functional human eukaryotic translation initiation factor 4G

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; INITIATION FACTOR; POLYPEPTIDE; PROTEIN SUBUNIT;

EID: 0031982683     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.1.334     Document Type: Article
Times cited : (252)

References (48)
  • 1
    • 0027296959 scopus 로고
    • Rapid cDNa sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNa library
    • Adams, M. D., M. B. Soares, A. R. Kerlavage, C. F. Fields, and J. C. Venter. 1993. Rapid cDNA sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNA library. Nat. Genet. 4:373-380.
    • (1993) Nat. Genet. , vol.4 , pp. 373-380
    • Adams, M.D.1    Soares, M.B.2    Kerlavage, A.R.3    Fields, C.F.4    Venter, J.C.5
  • 2
    • 0028787554 scopus 로고
    • Efficient cleavage of p220 by poliovirus 2A protease expression in mammalian cells: Effects on vaccinia virus
    • Aldabe, R., E. Feduchi, I. Novoa, and L. Carrasco. 1995. Efficient cleavage of p220 by poliovirus 2A protease expression in mammalian cells: effects on vaccinia virus. Biochem. Biophys. Res. Commun. 215:928-936.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 928-936
    • Aldabe, R.1    Feduchi, E.2    Novoa, I.3    Carrasco, L.4
  • 3
    • 0026457301 scopus 로고
    • Isolation and sequence of the cDNAs encoding the subunits of the isozyme form of wheat protein synthesis initiation factor 4F
    • Allen, M. L., A. M. Metz, R. T. Timmer, R. E. Rhoads, and K. S. Browning. 1992. Isolation and sequence of the cDNAs encoding the subunits of the isozyme form of wheat protein synthesis initiation factor 4F. J. Biol. Chem. 267:23232-23236.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23232-23236
    • Allen, M.L.1    Metz, A.M.2    Timmer, R.T.3    Rhoads, R.E.4    Browning, K.S.5
  • 4
    • 0026680845 scopus 로고
    • Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-fos
    • Blanar, M., and W. Rutter. 1992. Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-fos. Science 256:1014-1018.
    • (1992) Science , vol.256 , pp. 1014-1018
    • Blanar, M.1    Rutter, W.2
  • 5
    • 0023134622 scopus 로고
    • Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection
    • Bonneau, A.-M., and N. Sonenberg. 1987. Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection. J. Virol. 61:986-991.
    • (1987) J. Virol. , vol.61 , pp. 986-991
    • Bonneau, A.-M.1    Sonenberg, N.2
  • 6
    • 0026781543 scopus 로고
    • Identification of an isozyme form of protein synthesis initiation factor 4F in plants
    • Browning, K. S., C. Webster, J. K. Roberts, and J. M. Ravel. 1992. Identification of an isozyme form of protein synthesis initiation factor 4F in plants. J. Biol. Chem. 267:10096-10100.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10096-10100
    • Browning, K.S.1    Webster, C.2    Roberts, J.K.3    Ravel, J.M.4
  • 7
    • 0024272950 scopus 로고
    • Genomic structure and amino acid sequence domains of the human la autoantigen
    • Chambers, J. C., D. Kenan, B. J. Martin, and J. D. Keene. 1988. Genomic structure and amino acid sequence domains of the human La autoantigen. J. Biol. Chem. 263:18043-18051.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18043-18051
    • Chambers, J.C.1    Kenan, D.2    Martin, B.J.3    Keene, J.D.4
  • 9
    • 85036685913 scopus 로고    scopus 로고
    • Craig, A., and N. Sonenberg. Unpublished observations
    • 8a. Craig, A., and N. Sonenberg. Unpublished observations.
  • 10
    • 0024238770 scopus 로고
    • High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin
    • Edery, I., M. Altmann, and N. Sonenberg. 1988. High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin. Gene 74:517-525.
    • (1988) Gene , vol.74 , pp. 517-525
    • Edery, I.1    Altmann, M.2    Sonenberg, N.3
  • 11
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison, D., S. C. Milburn, I. Edery, N. Sonenberg, and J. W. Hershey. 1982. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J. Biol. Chem. 257:14806-14810.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 12
    • 0000233999 scopus 로고
    • Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 13
    • 0027219266 scopus 로고
    • TIF4631 and TIF4632: Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function
    • Goyer, C., M. Altmann, H. S. Lee, A. Blanc, M. Deshmukh, J. Woolford, Jr., H. Trachsel, and N. Sonenberg. 1993. TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell. Biol. 13:4860-4874.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4860-4874
    • Goyer, C.1    Altmann, M.2    Lee, H.S.3    Blanc, A.4    Deshmukh, M.5    Woolford Jr., J.6    Trachsel, H.7    Sonenberg, N.8
  • 14
    • 85036684347 scopus 로고    scopus 로고
    • Gradi, A. Unpublished observations
    • 12a. Gradi, A. Unpublished observations.
  • 15
    • 0029861190 scopus 로고    scopus 로고
    • The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase
    • Haghighat, A., Y. Svitkin, I. Novoa, E. Kuechler, T. Skern, and N. Sonenberg. 1996. The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase. J. Virol. 70:8444-8450.
    • (1996) J. Virol. , vol.70 , pp. 8444-8450
    • Haghighat, A.1    Svitkin, Y.2    Novoa, I.3    Kuechler, E.4    Skern, T.5    Sonenberg, N.6
  • 16
    • 0031024024 scopus 로고    scopus 로고
    • eIF4G: A multipurpose ribosome adapter?
    • Hentze, M. W. 1997. eIF4G: a multipurpose ribosome adapter? Science 275:500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 17
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • Imataka, H., H. S. Olsen, and N. Sonenberg. 1997. A new translational regulator with homology to eukaryotic translation initiation factor 4G. EMBO J. 16:817-825.
    • (1997) EMBO J. , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, H.S.2    Sonenberg, N.3
  • 18
    • 0028874823 scopus 로고
    • Monensin and nigericin prevent the inhibition of host translation by poliovirus, without affecting p220 cleavage
    • Irurzun, A., S. Sánchez-Palomino, I. Novoa, and L. Carrasco. 1995. Monensin and nigericin prevent the inhibition of host translation by poliovirus, without affecting p220 cleavage. J. Virol. 69:7453-7460.
    • (1995) J. Virol. , vol.69 , pp. 7453-7460
    • Irurzun, A.1    Sánchez-Palomino, S.2    Novoa, I.3    Carrasco, L.4
  • 19
    • 0026039803 scopus 로고
    • RNA unwinding in translation: Assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B
    • Jaramillo, M., T. E. Dever, W. C. Merrick, and N. Sonenberg. 1991. RNA unwinding in translation: assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B. Mol. Cell. Biol. 11:5992-5997.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5992-5997
    • Jaramillo, M.1    Dever, T.E.2    Merrick, W.C.3    Sonenberg, N.4
  • 20
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear, B. J., R. Kirchweger, T. Skern, and R. E. Rhoads. 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J. Biol. Chem. 270:21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 21
    • 0027182923 scopus 로고
    • Mapping the cleavage site in protein synthesis initiation factor eIF-4 γ of the 2A proteases from human coxsackievirus and rhinovirus
    • Lamphear, B. J., R. Yan, F. Yang, D. Waters, H. D. Liebig, H. Klump, E. Kuechler, T. Skern, and R. E. Rhoads. 1993. Mapping the cleavage site in protein synthesis initiation factor eIF-4 γ of the 2A proteases from human coxsackievirus and rhinovirus. J. Biol. Chem. 268:19200-19203.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19200-19203
    • Lamphear, B.J.1    Yan, R.2    Yang, F.3    Waters, D.4    Liebig, H.D.5    Klump, H.6    Kuechler, E.7    Skern, T.8    Rhoads, R.E.9
  • 22
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas, A., K. S. Montine, and N. Sonenberg. 1990. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345:544-547.
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 23
    • 0031017473 scopus 로고    scopus 로고
    • DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death
    • Levy-Strumpf, N., L. P. Deiss, H. Berissi, and A. Kimchi. 1997. DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death. Mol. Cell. Biol. 17:1615-1625.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1615-1625
    • Levy-Strumpf, N.1    Deiss, L.P.2    Berissi, H.3    Kimchi, A.4
  • 25
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor cIF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., H. Lee, A. Pause, and N. Sonenberg. 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor cIF-4γ and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15:4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 26
    • 0018400571 scopus 로고
    • Assays for eukaryotic protein synthesis
    • Merrick, W. C. 1979. Assays for eukaryotic protein synthesis. Methods Enzymol. 60:108-123.
    • (1979) Methods Enzymol. , vol.60 , pp. 108-123
    • Merrick, W.C.1
  • 27
    • 0028331455 scopus 로고
    • The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence
    • Méthot, N., A. Pause, J. W. B. Hershey, and N. Sonenberg. 1994. The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol. Cell. Biol. 14:2307-2316.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2307-2316
    • Méthot, N.1    Pause, A.2    Hershey, J.W.B.3    Sonenberg, N.4
  • 28
    • 0031054338 scopus 로고    scopus 로고
    • The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by cIF4E-binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate
    • Ohlmann, T., V. M. Pain, W. Wood, M. Rau, and S. J. Morley. 1997. The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by cIF4E-binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate. EMBO J. 16:844-855.
    • (1997) EMBO J. , vol.16 , pp. 844-855
    • Ohlmann, T.1    Pain, V.M.2    Wood, W.3    Rau, M.4    Morley, S.J.5
  • 29
    • 0028901902 scopus 로고
    • Proteolytic cleavage of initiation factor eIF-4G in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs
    • Ohlmann, T., M. Rau, S. J. Morley, and V. M. Pain. 1995. Proteolytic cleavage of initiation factor eIF-4G in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs. Nucleic Acids Res. 23:334-340.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 334-340
    • Ohlmann, T.1    Rau, M.2    Morley, S.J.3    Pain, V.M.4
  • 30
    • 0029976319 scopus 로고    scopus 로고
    • The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E
    • Ohlmann, T., M. Rau, V. M. Pain, and S. J. Morley. 1996. The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E. EMBO J. 15:1371-1382.
    • (1996) EMBO J. , vol.15 , pp. 1371-1382
    • Ohlmann, T.1    Rau, M.2    Pain, V.M.3    Morley, S.J.4
  • 31
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain, V. M. 1996. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236:747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 32
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., G. J. Belsham, A. C. Gingras, O. Donzé, T. A. Lin, J. C. Lawrence, and N. Sonenberg. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371:762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donzé, O.4    Lin, T.A.5    Lawrence, J.C.6    Sonenberg, N.7
  • 33
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian translation initiation factor eIF-4a define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation
    • Pause, A., N. Méthot, Y. V. Svitkin, W. C. Merrick, and N. Sonenberg. 1994. Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation. EMBO J. 13:1205-1215.
    • (1994) EMBO J. , vol.13 , pp. 1205-1215
    • Pause, A.1    Méthot, N.2    Svitkin, Y.V.3    Merrick, W.C.4    Sonenberg, N.5
  • 34
    • 0026750639 scopus 로고
    • Lack of direct correlation between p220 cleavage and the shut-off of host translation after poliovirus infection
    • Pérez, L., and L. Carrasco. 1992. Lack of direct correlation between p220 cleavage and the shut-off of host translation after poliovirus infection. Virology 189:178-186.
    • (1992) Virology , vol.189 , pp. 178-186
    • Pérez, L.1    Carrasco, L.2
  • 35
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova, T. V., C. U. T. Hellen, and I. N. Shatsky. 1996. Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol. Cell. Biol. 16:6859-6869.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.T.2    Shatsky, I.N.3
  • 36
    • 0029968997 scopus 로고    scopus 로고
    • Functional dissection of eukaryotic initiation factor 4F: The 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes
    • Pestova, T. V., I. N. Shatsky, and C. U. T. Hellen. 1996. Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes. Mol. Cell. Biol. 16:6870-6878.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6870-6878
    • Pestova, T.V.1    Shatsky, I.N.2    Hellen, C.U.T.3
  • 37
    • 85036676712 scopus 로고    scopus 로고
    • Personal communication
    • 34a. Poncet, D., et al. Personal communication.
    • Poncet, D.1
  • 39
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., I. Edery, K. Meerovitch, T. E. Dever, W. C. Merrick, and N. Sonenberg. 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell. Biol. 10:1134-1144.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 40
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: Translation initiation in eukaryotes
    • Sachs, A. B., P. Sarnow, and M. W. Hentze. 1997. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89:831-838.
    • (1997) Cell , vol.89 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 41
    • 0026527758 scopus 로고
    • Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for comparative protein modelling
    • Smith, R. F., and T. F. Smith. 1992. Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for comparative protein modelling. Protein Eng. 5:35-41.
    • (1992) Protein Eng. , vol.5 , pp. 35-41
    • Smith, R.F.1    Smith, T.F.2
  • 44
    • 0000831271 scopus 로고    scopus 로고
    • mRNA 5′ cap-binding protein eIF4E and control of cell growth
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth, p. 245-269. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1996) Translational Control , pp. 245-269
    • Sonenberg, N.1
  • 45
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF4G
    • Tarun, S. Z., and A. B. Sachs. 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF4G. EMBO J. 15:7168-7177.
    • (1996) EMBO J. , vol.15 , pp. 7168-7177
    • Tarun, S.Z.1    Sachs, A.B.2
  • 46
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
    • Tarun, S. Z., S. Wells, J. Deardorff, and A. B. Sachs. 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94:9046-9051.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1    Wells, S.2    Deardorff, J.3    Sachs, A.B.4
  • 47
    • 0031048641 scopus 로고    scopus 로고
    • A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme
    • Yamanaka, S., K. S. Poksay, K. S. Arnold, and T. L. Innerarity. 1997. A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme. Genes Dev. 11:321-333.
    • (1997) Genes Dev. , vol.11 , pp. 321-333
    • Yamanaka, S.1    Poksay, K.S.2    Arnold, K.S.3    Innerarity, T.L.4
  • 48
    • 0026463868 scopus 로고
    • Amino acid sequence of the human protein synthesis initiation factor eIF-4γ
    • Yan, R., W. Rychlik, D. Etchison, and R. E. Rhoads. 1992. Amino acid sequence of the human protein synthesis initiation factor eIF-4γ. J. Biol. Chem. 267:23226-23231.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23226-23231
    • Yan, R.1    Rychlik, W.2    Etchison, D.3    Rhoads, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.