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Volumn 271, Issue 1, 2000, Pages 46-57

Specific interaction between the hepatitis delta virus RNA and glyceraldehyde 3-phosphate dehydrogenase: An enhancement on ribozyme catalysis

Author keywords

GAPDH binding site; Glyceraldehyde 3 phosphate dehydrogenase (GAPDH); HDV ribozyme; HDV RNA binding protein; Hepatitis delta virus; Relocalization of GAPDH

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; RIBOZYME; VIRUS RNA;

EID: 0034713424     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2000.0302     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 0029102283 scopus 로고
    • Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein
    • Baxi M. D., Vishwanatha J. K. Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein. Biochemistry. 34:1995;9700-9707.
    • (1995) Biochemistry , vol.34 , pp. 9700-9707
    • Baxi, M.D.1    Vishwanatha, J.K.2
  • 2
    • 0029955347 scopus 로고    scopus 로고
    • Identification and characterization of hepatitis delta virus RNA transcriptional promoter
    • Beard M. R., Macnaughton T. B., Gowans E. J. Identification and characterization of hepatitis delta virus RNA transcriptional promoter. J. Virol. 70:1996;4986-4995.
    • (1996) J. Virol. , vol.70 , pp. 4986-4995
    • Beard, M.R.1    MacNaughton, T.B.2    Gowans, E.J.3
  • 3
    • 0029763579 scopus 로고    scopus 로고
    • A cellular homolog of hepatitis delta antigen: Implications for viral replication and evolution
    • Brazas R., Ganem D. A cellular homolog of hepatitis delta antigen: Implications for viral replication and evolution. Science. 274:1996;90-94.
    • (1996) Science , vol.274 , pp. 90-94
    • Brazas, R.1    Ganem, D.2
  • 5
    • 0028826113 scopus 로고
    • Hepatitis D virus RNA editing: Specific modification of adenosine in the antigenomic RNA
    • Casey J. L., Gerin J. L. Hepatitis D virus RNA editing: Specific modification of adenosine in the antigenomic RNA. J. Virol. 69:1995;7593-7600.
    • (1995) J. Virol. , vol.69 , pp. 7593-7600
    • Casey, J.L.1    Gerin, J.L.2
  • 7
    • 0028057430 scopus 로고
    • Mutational analysis of delta antigen: Effect on assembly and replication of hepatitis delta virus
    • Chang M.-F., Chen C.-J., Chang S. C. Mutational analysis of delta antigen: Effect on assembly and replication of hepatitis delta virus. J. Virol. 68:1994;646-653.
    • (1994) J. Virol. , vol.68 , pp. 646-653
    • Chang, M.-F.1    Chen, C.-J.2    Chang, S.C.3
  • 8
    • 0028940476 scopus 로고
    • Functional domains of delta antigens and viral RNA required for RNA packaging of hepatitis delta virus
    • Chang M.-F., Chen C.-H., Lin S.-L., Chen C.-J., Chang S. C. Functional domains of delta antigens and viral RNA required for RNA packaging of hepatitis delta virus. J. Virol. 69:1995;2508-2514.
    • (1995) J. Virol. , vol.69 , pp. 2508-2514
    • Chang, M.-F.1    Chen, C.-H.2    Lin, S.-L.3    Chen, C.-J.4    Chang, S.C.5
  • 9
    • 0027529174 scopus 로고
    • Functional motifs of delta antigen essential for RNA binding and replication of hepatitis delta virus
    • Chang M.-F., Sun C.-Y., Chen C.-J., Chang S. C. Functional motifs of delta antigen essential for RNA binding and replication of hepatitis delta virus. J. Virol. 67:1993;2529-2536.
    • (1993) J. Virol. , vol.67 , pp. 2529-2536
    • Chang, M.-F.1    Sun, C.-Y.2    Chen, C.-J.3    Chang, S.C.4
  • 10
    • 0030965882 scopus 로고    scopus 로고
    • Surprising specificity of PKR binding to delta agent genomic RNA
    • Circle D. A., Neel O. D., Robertson H. D., Clarke P. A., Mathews M. B. Surprising specificity of PKR binding to delta agent genomic RNA. RNA. 3:1997;438-448.
    • (1997) RNA , vol.3 , pp. 438-448
    • Circle, D.A.1    Neel, O.D.2    Robertson, H.D.3    Clarke, P.A.4    Mathews, M.B.5
  • 11
    • 0014690989 scopus 로고
    • Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into dimers or monomers by adenosine triphosphate
    • Constantinides S. M., Deal W. C. Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into dimers or monomers by adenosine triphosphate. J. Biol. Chem. 244:1969;5695-5702.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5695-5702
    • Constantinides, S.M.1    Deal, W.C.2
  • 12
    • 0029760743 scopus 로고    scopus 로고
    • Specific interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and la protein with cis-acting RNAs of human parainfluenza virus type 3
    • De B. P., Gupta S., Zhao H., Drazba J. A., Banerjee A. K. Specific interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and LA protein with cis-acting RNAs of human parainfluenza virus type 3. J. Biol. Chem. 271:1996;24728-24735.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24728-24735
    • De B., P.1    Gupta, S.2    Zhao, H.3    Drazba, J.A.4    Banerjee, A.K.5
  • 13
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J. D., Lebovitz R. M., Roeder R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 14
    • 0032497521 scopus 로고    scopus 로고
    • Crystal structure of a hepatitis delta virus ribozyme
    • Ferre-D'Amare A. R., Zhou K., Doudna J. A. Crystal structure of a hepatitis delta virus ribozyme. Nature. 395:1998;567-574.
    • (1998) Nature , vol.395 , pp. 567-574
    • Ferre-D'Amare, A.R.1    Zhou, K.2    Doudna, J.A.3
  • 15
    • 0027436027 scopus 로고
    • The RNAs of hepatitis delta virus are copied by RNA polymerase II in nuclear homogenates
    • Fu T. B., Taylor J. M. The RNAs of hepatitis delta virus are copied by RNA polymerase II in nuclear homogenates. J. Virol. 67:1993;6965-6972.
    • (1993) J. Virol. , vol.67 , pp. 6965-6972
    • Fu, T.B.1    Taylor, J.M.2
  • 16
    • 0024842159 scopus 로고
    • Identification and purification of a 62000-dalton protein that binds specifically to the polypyrimidine tract of introns
    • Garcia-Blanco M. A., Jamison S. F., Sharp P. A. Identification and purification of a 62000-dalton protein that binds specifically to the polypyrimidine tract of introns. Genes Dev. 3:1989;1874-1886.
    • (1989) Genes Dev. , vol.3 , pp. 1874-1886
    • Garcia-Blanco, M.A.1    Jamison, S.F.2    Sharp, P.A.3
  • 17
    • 0028120914 scopus 로고
    • The cellular polypeptide p57 (pyrimidine tract-binding protein) binds to multiple sites in the poliovirus 5′ nontranslated region
    • Hellen C. U. T., Pestova T. V., Litterst M., Wimmer E. The cellular polypeptide p57 (pyrimidine tract-binding protein) binds to multiple sites in the poliovirus 5′ nontranslated region. J. Virol. 68:1994;941-950.
    • (1994) J. Virol. , vol.68 , pp. 941-950
    • Hellen, C.U.T.1    Pestova, T.V.2    Litterst, M.3    Wimmer, E.4
  • 18
    • 0024554152 scopus 로고
    • Type D (delta) hepatitis
    • Hoofnagle J. H. Type D (delta) hepatitis. JAMA. 261:1989;1321-1325.
    • (1989) JAMA , vol.261 , pp. 1321-1325
    • Hoofnagle, J.H.1
  • 19
    • 0032500589 scopus 로고    scopus 로고
    • Identification and characterization of the RNA chaperone activity of hepatitis delta antigen peptides
    • Huang Z.-S., Wu H.-N. Identification and characterization of the RNA chaperone activity of hepatitis delta antigen peptides. J. Biol. Chem. 273:1998;26455-26461.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26455-26461
    • Huang, Z.-S.1    Wu, H.-N.2
  • 20
    • 0030045251 scopus 로고    scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis of mature cerebellar neurons in culture
    • Ishitani R., Sunaga K., Hirano A., Saunders P., Katsube N., Chuang D. M. Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis of mature cerebellar neurons in culture. J. Neurochem. 66:1996;928-935.
    • (1996) J. Neurochem. , vol.66 , pp. 928-935
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Saunders, P.4    Katsube, N.5    Chuang, D.M.6
  • 21
    • 0030812847 scopus 로고    scopus 로고
    • Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of the hepatitis C virus RNA genome
    • Ito T., Lai M. M. C. Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of the hepatitis C virus RNA genome. J. Virol. 71:1997;8698-8706.
    • (1997) J. Virol. , vol.71 , pp. 8698-8706
    • Ito, T.1    Lai, M.M.C.2
  • 22
    • 0025146035 scopus 로고
    • Cap-independent translation of encephalomyocarditis virus RNA: Structural elements of the internal ribosomal entry site and involvement of a cellular 57-kDa RNA binding protein
    • Jang S. K., Wimmer E. Cap-independent translation of encephalomyocarditis virus RNA: Structural elements of the internal ribosomal entry site and involvement of a cellular 57-kDa RNA binding protein. Genes Dev. 4:1990;1560-1572.
    • (1990) Genes Dev. , vol.4 , pp. 1560-1572
    • Jang, S.K.1    Wimmer, E.2
  • 23
    • 0015740243 scopus 로고
    • Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes
    • Kant J. A., Steck T. L. Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes. J. Biol. Chem. 248:1973;8457-8464.
    • (1973) J. Biol. Chem. , vol.248 , pp. 8457-8464
    • Kant, J.A.1    Steck, T.L.2
  • 24
    • 0019889692 scopus 로고
    • A basic isozyme of yeast glyceraldehyde-3-phosphate dehydrogenase with nucleic acid helix-destabilizing activity
    • Karpel R. L., Burchard A. C. A basic isozyme of yeast glyceraldehyde-3-phosphate dehydrogenase with nucleic acid helix-destabilizing activity. Biochim. Biophys. Acta. 654:1981;256-267.
    • (1981) Biochim. Biophys. Acta , vol.654 , pp. 256-267
    • Karpel, R.L.1    Burchard, A.C.2
  • 25
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto R. M., Caswell A. H. Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry. 25:1986;656-661.
    • (1986) Biochemistry , vol.25 , pp. 656-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 26
    • 0029969687 scopus 로고    scopus 로고
    • Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs
    • Kolupaeva V. G., Hellen C. U. T., Shatsky I. N. Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs. RNA. 2:1996;1199-1212.
    • (1996) RNA , vol.2 , pp. 1199-1212
    • Kolupaeva, V.G.1    Hellen, C.U.T.2    Shatsky, I.N.3
  • 28
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B., Matilla T., Burright E. N., Merry D. E., Fischbeck K. H., Orr H. T., Zoghbi H. Y. Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Hum. Mol. Genet. 5:1996;1311-1318.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3    Merry, D.E.4    Fischbeck, K.H.5    Orr, H.T.6    Zoghbi, H.Y.7
  • 29
    • 0020758755 scopus 로고
    • A porcine brain protein (35K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
    • Kumagi H., Sakai H. A porcine brain protein (35K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase. J. Biochem. 93:1983;1259-1269.
    • (1983) J. Biochem. , vol.93 , pp. 1259-1269
    • Kumagi, H.1    Sakai, H.2
  • 30
    • 0024511721 scopus 로고
    • Initiation of replication of the human hepatitis delta virus genome from cloned DNA: Role of delta antigen
    • Kuo M. Y.-P., Chao M., Taylor J. M. Initiation of replication of the human hepatitis delta virus genome from cloned DNA: Role of delta antigen. J. Virol. 63:1989;1945-1950.
    • (1989) J. Virol. , vol.63 , pp. 1945-1950
    • Kuo, M.Y.-P.1    Chao, M.2    Taylor, J.M.3
  • 31
    • 0023941342 scopus 로고
    • Molecular cloning of hepatitis delta virus RNA from an infected woodchuck liver: Sequence, structure, and application
    • Kuo M. Y.-P., Goldberg J., Coates L., Mason W., Gerin J., Taylor J. M. Molecular cloning of hepatitis delta virus RNA from an infected woodchuck liver: Sequence, structure, and application. J. Virol. 62:1988a;1855-1860.
    • (1988) J. Virol. , vol.62 , pp. 1855-1860
    • Kuo, M.Y.-P.1    Goldberg, J.2    Coates, L.3    Mason, W.4    Gerin, J.5    Taylor, J.M.6
  • 32
    • 0024209351 scopus 로고
    • Characterization of self-cleaving RNA sequences on the genome and antigenome of human hepatitis delta virus
    • Kuo M. Y.-P., Sharmeen L., Dinter-Gottlieb G., Taylor J. M. Characterization of self-cleaving RNA sequences on the genome and antigenome of human hepatitis delta virus. J. Virol. 62:1988b;4439-4444.
    • (1988) J. Virol. , vol.62 , pp. 4439-4444
    • Kuo, M.Y.-P.1    Sharmeen, L.2    Dinter-Gottlieb, G.3    Taylor, J.M.4
  • 33
    • 0028888173 scopus 로고
    • Intracellular cleavage and ligation of hepatitis delta virus genomic RNA: Regulation of ribozyme activity by cis-acting sequences and host factors
    • Lazinski D. W., Taylor J. M. Intracellular cleavage and ligation of hepatitis delta virus genomic RNA: Regulation of ribozyme activity by cis-acting sequences and host factors. J. Virol. 69:1995;1190-1200.
    • (1995) J. Virol. , vol.69 , pp. 1190-1200
    • Lazinski, D.W.1    Taylor, J.M.2
  • 34
    • 0032571350 scopus 로고    scopus 로고
    • The nucleolin-binding activity of hepatitis delta antigen is associated with nucleolus targeting
    • Lee C.-H., Chang S. C., Chen C.-J., Chang M.-F. The nucleolin-binding activity of hepatitis delta antigen is associated with nucleolus targeting. J. Biol. Chem. 273:1998;7650-7656.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7650-7656
    • Lee, C.-H.1    Chang, S.C.2    Chen, C.-J.3    Chang, M.-F.4
  • 35
    • 0025004448 scopus 로고
    • Characterization of hepatitis delta antigen: Specific binding to hepatitis delta virus RNA
    • Lin J.-H., Chang M.-F., Baker S. C., Govindarajan S., Lai M. M. C. Characterization of hepatitis delta antigen: Specific binding to hepatitis delta virus RNA. J. Virol. 64:1990;4051-4058.
    • (1990) J. Virol. , vol.64 , pp. 4051-4058
    • Lin, J.-H.1    Chang, M.-F.2    Baker, S.C.3    Govindarajan, S.4    Lai, M.M.C.5
  • 36
    • 0027496232 scopus 로고
    • Endogenous promoters can direct the transcription of hepatitis delta virus RNA from a recircularized cDNA template
    • Macnaughton T. B., Beard M. R., Chao M., Gowans E. J., Lai M. M. C. Endogenous promoters can direct the transcription of hepatitis delta virus RNA from a recircularized cDNA template. Virology. 196:1993a;629-636.
    • (1993) Virology , vol.196 , pp. 629-636
    • MacNaughton, T.B.1    Beard, M.R.2    Chao, M.3    Gowans, E.J.4    Lai, M.M.C.5
  • 37
    • 0026228682 scopus 로고
    • Hepatitis delta antigen is necessary for access of hepatitis delta virus RNA to the cell transcriptional machinery but is not part of the transcriptional complex
    • Macnaughton T. B., Gowans E. J., McNamara S. P., Burrell C. J. Hepatitis delta antigen is necessary for access of hepatitis delta virus RNA to the cell transcriptional machinery but is not part of the transcriptional complex. Virology. 184:1991;387-390.
    • (1991) Virology , vol.184 , pp. 387-390
    • MacNaughton, T.B.1    Gowans, E.J.2    McNamara, S.P.3    Burrell, C.J.4
  • 38
    • 0027535112 scopus 로고
    • Replication of hepatitis delta virus RNA: Effect of mutations of the autocatalytic cleavage sites
    • Macnaughton T. B., Wang Y. J., Lai M. M. C. Replication of hepatitis delta virus RNA: Effect of mutations of the autocatalytic cleavage sites. J. Virol. 67:1993b;2228-2234.
    • (1993) J. Virol. , vol.67 , pp. 2228-2234
    • MacNaughton, T.B.1    Wang, Y.J.2    Lai, M.M.C.3
  • 40
    • 84984533940 scopus 로고
    • Molecular biology of a human hepatitis delta virus RNA
    • W. Robinson, K. Koike, & H. Will. New York: Alan R. Liss
    • Makino S., Chang M.-F., Kamahora T., Vannier D. M., Govindarajan S., Lai M. M. C. Molecular biology of a human hepatitis delta virus RNA. Robinson W., Koike K., Will H. Hepadna viruses. 1987b;549-564 Alan R. Liss, New York.
    • (1987) Hepadna Viruses , pp. 549-564
    • Makino, S.1    Chang, M.-F.2    Kamahora, T.3    Vannier, D.M.4    Govindarajan, S.5    Lai, M.M.C.6
  • 42
    • 0023651444 scopus 로고
    • Oligonucleotide snythesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan J. F., Groebe D. R., Witherell G. W., Uhlenbeck O. C. Oligonucleotide snythesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res. 15:1987;8783-8798.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 43
    • 0022535636 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons
    • Morgenegg G., Winkler G. C., Hubscher U., Heizmann C. W., Mous J., Kuenzle C. C. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J. Neurochem. 47:1986;54-62.
    • (1986) J. Neurochem. , vol.47 , pp. 54-62
    • Morgenegg, G.1    Winkler, G.C.2    Hubscher, U.3    Heizmann, C.W.4    Mous, J.5    Kuenzle, C.C.6
  • 44
    • 0026480757 scopus 로고
    • Polypyrimidine tract-binding protein interacts with sequences involved in alternative splicing of β-tropomyosin pre-mRNA
    • Mulligan G. J., Guo W., Wormsley S., Helfman D. M. Polypyrimidine tract-binding protein interacts with sequences involved in alternative splicing of β-tropomyosin pre-mRNA. J. Biol. Chem. 267:1992;25480-25487.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25480-25487
    • Mulligan, G.J.1    Guo, W.2    Wormsley, S.3    Helfman, D.M.4
  • 45
    • 0028816615 scopus 로고
    • +-binding region (Rossmann fold)
    • +-binding region (Rossmann fold). J. Biol. Chem. 270:1995;2755-2763.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.C.2
  • 46
    • 0029042291 scopus 로고
    • Transgenic mice support replication of hepatitis delta virus RNA in multiple tissues, particularly in skeletal muscle
    • Polo J. M., Jeng K. S., Lim B., Govindarajan S., Hofman F., Sangiorgi F., Lai M. M. C. Transgenic mice support replication of hepatitis delta virus RNA in multiple tissues, particularly in skeletal muscle. J. Virol. 69:1995;4880-4887.
    • (1995) J. Virol. , vol.69 , pp. 4880-4887
    • Polo, J.M.1    Jeng, K.S.2    Lim, B.3    Govindarajan, S.4    Hofman, F.5    Sangiorgi, F.6    Lai, M.M.C.7
  • 47
    • 0029940185 scopus 로고    scopus 로고
    • RNA editing of hepatitis delta virus antigenome by dsRNA-adenosine deaminase
    • Polson A. G., Bass B. L., Casey J. L. RNA editing of hepatitis delta virus antigenome by dsRNA-adenosine deaminase. Nature. 380:1996;454-456.
    • (1996) Nature , vol.380 , pp. 454-456
    • Polson, A.G.1    Bass, B.L.2    Casey, J.L.3
  • 48
    • 0027214981 scopus 로고
    • Glycolytic enzymes as DNA binding proteins
    • Ronai Z. Glycolytic enzymes as DNA binding proteins. Int. J. Biochem. 25:1993;1073-1076.
    • (1993) Int. J. Biochem. , vol.25 , pp. 1073-1076
    • Ronai, Z.1
  • 49
    • 0027294692 scopus 로고
    • Ribonucleoprotein complex of hepatitis delta virus
    • Ryu W. S., Netter H. J., Bayer M., Taylor J. M. Ribonucleoprotein complex of hepatitis delta virus. J. Virol. 67:1993;3281-3287.
    • (1993) J. Virol. , vol.67 , pp. 3281-3287
    • Ryu, W.S.1    Netter, H.J.2    Bayer, M.3    Taylor, J.M.4
  • 50
    • 0029927267 scopus 로고    scopus 로고
    • Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis a virus
    • Schultz D. E., Hardin C. C., Lemon S. M. Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis A virus. J. Biol. Chem. 271:1996;14134-14142.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14134-14142
    • Schultz, D.E.1    Hardin, C.C.2    Lemon, S.M.3
  • 51
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein
    • Schulze H., Schuyler A., Stuber D., Dobeli H., Langen H., Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein. J. Neurochem. 60:1993;1915-1922.
    • (1993) J. Neurochem. , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuyler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 52
    • 0023747377 scopus 로고
    • Antigenomic RNA of human hepatitis delta virus can undergo self-cleavage
    • Sharmeen L., Kuo M. Y. P., Dinter-Gottlieb G., Taylor J. M. Antigenomic RNA of human hepatitis delta virus can undergo self-cleavage. J. Virol. 62:1988;2674-2679.
    • (1988) J. Virol. , vol.62 , pp. 2674-2679
    • Sharmeen, L.1    Kuo, M.Y.P.2    Dinter-Gottlieb, G.3    Taylor, J.M.4
  • 53
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R., Green M. R. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science. 259:1993;365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 54
    • 0029870382 scopus 로고    scopus 로고
    • Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase
    • Sioud M., Jespersen L. Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 257:1996;775-789.
    • (1996) J. Mol. Biol. , vol.257 , pp. 775-789
    • Sioud, M.1    Jespersen, L.2
  • 55
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover M. A. Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J. Cell. Biochem. 66:1997;133-140.
    • (1997) J. Cell. Biochem. , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 56
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M. A. New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 1432:1999;159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 57
    • 0028865070 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is overexpressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain
    • Sunaga K., Takahashi H., Chuang D. M., Ishitani R. Glyceraldehyde-3-phosphate dehydrogenase is overexpressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Neurosci. Lett. 200:1995;133-136.
    • (1995) Neurosci. Lett. , vol.200 , pp. 133-136
    • Sunaga, K.1    Takahashi, H.2    Chuang, D.M.3    Ishitani, R.4
  • 58
    • 0027396860 scopus 로고
    • Role of the large hepatitis B virus envelope protein in infectivity of the hepatitis delta virion
    • Sureau C., Guerra B., Lanford R. E. Role of the large hepatitis B virus envelope protein in infectivity of the hepatitis delta virion. J. Virol. 67:1993;366-372.
    • (1993) J. Virol. , vol.67 , pp. 366-372
    • Sureau, C.1    Guerra, B.2    Lanford, R.E.3
  • 59
    • 0027360814 scopus 로고
    • Hepatitis delta virus cDNA monomer can be used in transfection experiments to initiate viral RNA replication
    • Tai F.-P., Chen P.-J., Chang F.-L., Chen D.-S. Hepatitis delta virus cDNA monomer can be used in transfection experiments to initiate viral RNA replication. Virology. 197:1993;137-142.
    • (1993) Virology , vol.197 , pp. 137-142
    • Tai, F.-P.1    Chen, P.-J.2    Chang, F.-L.3    Chen, D.-S.4
  • 60
    • 0025723996 scopus 로고
    • Small-form hepatitis B surface antigen is sufficient to help in the assembly of hepatitis delta virus-like particles
    • Wang C.-J., Chen P.-J., Wu T.-C., Patel D., Chen D.-S. Small-form hepatitis B surface antigen is sufficient to help in the assembly of hepatitis delta virus-like particles. J. Virol. 65:1991;6630-6636.
    • (1991) J. Virol. , vol.65 , pp. 6630-6636
    • Wang, C.-J.1    Chen, P.-J.2    Wu, T.-C.3    Patel, D.4    Chen, D.-S.5
  • 61
    • 84984583407 scopus 로고    scopus 로고
    • Identification of the functional regions required for hepatitis D virus replication and transcription by linker-scanning mutagenesis of viral genome
    • Wang H.-W., Wu H.-L., Chen D.-S., Chen P.-J. Identification of the functional regions required for hepatitis D virus replication and transcription by linker-scanning mutagenesis of viral genome. Virology. 239:1997;119-131.
    • (1997) Virology , vol.239 , pp. 119-131
    • Wang, H.-W.1    Wu, H.-L.2    Chen, D.-S.3    Chen, P.-J.4
  • 64
    • 0029058615 scopus 로고
    • Cellular proteins specifically bind to the 5′-noncoding region of hepatitis C virus RNA
    • Yen J.-H., Chang S. C., Hu C.-R., Chu S.-C., Lin S.-S., Hsieh Y.-S., Chang M.-F. Cellular proteins specifically bind to the 5′-noncoding region of hepatitis C virus RNA. Virology. 208:1995;723-732.
    • (1995) Virology , vol.208 , pp. 723-732
    • Yen, J.-H.1    Chang, S.C.2    Hu, C.-R.3    Chu, S.-C.4    Lin, S.-S.5    Hsieh, Y.-S.6    Chang, M.-F.7


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