메뉴 건너뛰기




Volumn 349, Issue 2, 2000, Pages 417-425

Evidence for phosphorylation and ubiquitinylation of the turnip yellow mosaic virus RNA-dependent RNA polymerase domain expressed in a baculovirus-insect cell system

Author keywords

PEST sequence; Positive strand RNA virus; TYMV; Viral replication

Indexed keywords

GLUTAMIC ACID; HISTIDINE; MONOCLONAL ANTIBODY; PHOSPHATASE; PHOSPHOAMINO ACID; PROLINE; PROTEASOME; RNA DIRECTED RNA POLYMERASE; SERINE; THREONINE; UBIQUITIN;

EID: 0034662167     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3490417     Document Type: Article
Times cited : (64)

References (55)
  • 1
    • 0023770852 scopus 로고
    • Evolution of plus-strand RNA viruses
    • 1 Goldbach, R. and Wellink, J. (1988) Evolution of plus-strand RNA viruses. Intervirology 29, 260-267
    • (1988) Intervirology , vol.29 , pp. 260-267
    • Goldbach, R.1    Wellink, J.2
  • 2
    • 0024284515 scopus 로고
    • Overlapping open reading frames revealed by complete nucleotide sequencing of turnip yellow mosaic virus genomic RNA
    • 2 Morch, M. D., Boyer, J. C. and Haenni, A. L. (1988) Overlapping open reading frames revealed by complete nucleotide sequencing of turnip yellow mosaic virus genomic RNA. Nucleic Acids Res. 16, 6157-6173
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6157-6173
    • Morch, M.D.1    Boyer, J.C.2    Haenni, A.L.3
  • 3
    • 0030332528 scopus 로고    scopus 로고
    • Comparison of the replication of positive-stranded RNA viruses of plants and animals
    • 3 Buck, K. W. (1996) Comparison of the replication of positive-stranded RNA viruses of plants and animals. Adv. Virus Res. 47, 159-251
    • (1996) Adv. Virus Res. , vol.47 , pp. 159-251
    • Buck, K.W.1
  • 4
    • 0024979026 scopus 로고
    • Infectious TYMV RNA from cloned cDNA: Effects in vitro and in vivo of point substitutions in the initiation codons of two extensively overlapping ORFs
    • 4 Weiland, J. J. and Dreher, T. W. (1989) Infectious TYMV RNA from cloned cDNA: effects in vitro and in vivo of point substitutions in the initiation codons of two extensively overlapping ORFs. Nucleic Acids Res. 17, 4675-4687
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4675-4687
    • Weiland, J.J.1    Dreher, T.W.2
  • 5
    • 0024851189 scopus 로고
    • Proteolytic origin of the 150-kilodalton protein encoded by turnip yellow mosaic virus genomic RNA
    • 5 Morch, M. D., Drugeon, G., Szafranski, P. and Haenni, A. L. (1989) Proteolytic origin of the 150-kilodalton protein encoded by turnip yellow mosaic virus genomic RNA. J. Virol. 63, 5153-5158
    • (1989) J. Virol. , vol.63 , pp. 5153-5158
    • Morch, M.D.1    Drugeon, G.2    Szafranski, P.3    Haenni, A.L.4
  • 6
    • 0028805921 scopus 로고
    • Expression of the turnip yellow mosaic virus proteinase in Escherichia coli and determination of the cleavage site within the 206 kDa protein
    • 6 Kadaré, G., Rozanov, M. and Haenni, A. L. (1995) Expression of the turnip yellow mosaic virus proteinase in Escherichia coli and determination of the cleavage site within the 206 kDa protein. J. Gen. Virol. 76, 2853-2857
    • (1995) J. Gen. Virol. , vol.76 , pp. 2853-2857
    • Kadaré, G.1    Rozanov, M.2    Haenni, A.L.3
  • 7
    • 0029963275 scopus 로고    scopus 로고
    • Identification of the cleavage site recognized by the turnip yellow mosaic virus protease
    • 7 Bransom, K. L. Wallace, S. E. and Dreher, T. W. (1996) Identification of the cleavage site recognized by the turnip yellow mosaic virus protease. Virology 217, 404-406
    • (1996) Virology , vol.217 , pp. 404-406
    • Bransom, K.L.1    Wallace, S.E.2    Dreher, T.W.3
  • 8
    • 0022608734 scopus 로고
    • Immunocytochemical localization of TYMV-coded structural and nonstructural proteins by the Protein A-gold technique
    • 8 Garnier, M., Candresse, T. and Bové, J. M. (1986) Immunocytochemical localization of TYMV-coded structural and nonstructural proteins by the Protein A-gold technique. Virology 151, 100-109
    • (1986) Virology , vol.151 , pp. 100-109
    • Garnier, M.1    Candresse, T.2    Bové, J.M.3
  • 9
    • 0027176917 scopus 로고
    • Cis-preferential replication of the turnip yellow mosaic virus RNA genome
    • 9 Weiland, J. J. and Dreher, T. W. (1993) Cis-preferential replication of the turnip yellow mosaic virus RNA genome. Proc. Natl. Acad. Sci. U.S.A. 90, 6095-6099
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6095-6099
    • Weiland, J.J.1    Dreher, T.W.2
  • 10
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • 10 Poch, O., Sauvaget, I., Delarue, M. and Tordo, N. (1989) Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8, 3867-3874
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 11
    • 0028881713 scopus 로고
    • Polymerase structures and function: Variations on a theme?
    • 11 Joyce, C. M. and Steitz, T. A. (1995) Polymerase structures and function: variations on a theme? J. Bacteriol. 177, 6321-6329
    • (1995) J. Bacteriol. , vol.177 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 12
    • 0016371490 scopus 로고
    • Turnip yellow mosaic virus-RNA replicase: Partial purification of the enzyme from the solubilized enzyme-template complex
    • 12 Mouchès, C., Bové, C. and Bové, J. M. (1974) Turnip yellow mosaic virus-RNA replicase: partial purification of the enzyme from the solubilized enzyme-template complex. Virology 58, 409-423
    • (1974) Virology , vol.58 , pp. 409-423
    • Mouchès, C.1    Bové, C.2    Bové, J.M.3
  • 13
    • 0030744360 scopus 로고    scopus 로고
    • The role of the pseudoknot at the 3′ end of turnip yellow mosaic virus RNA in minus-strand synthesis by the viral RNA-dependent RNA polymerase
    • 13 Deiman, B. A., Kortlever, R. M. and Pleij, C. W. (1997) The role of the pseudoknot at the 3′ end of turnip yellow mosaic virus RNA in minus-strand synthesis by the viral RNA-dependent RNA polymerase. J. Virol. 71, 5990-5996
    • (1997) J. Virol. , vol.71 , pp. 5990-5996
    • Deiman, B.A.1    Kortlever, R.M.2    Pleij, C.W.3
  • 14
    • 0026038512 scopus 로고
    • The 3′ promoter region involved in RNA synthesis directed by the turnip yellow mosaic virus genome in vitro
    • 14 Gargouri-Bouzid, R., David, C. and Haenni, A. L (1991) The 3′ promoter region involved in RNA synthesis directed by the turnip yellow mosaic virus genome in vitro. FEBS Lett. 294, 56-58
    • (1991) FEBS Lett. , vol.294 , pp. 56-58
    • Gargouri-Bouzid, R.1    David, C.2    Haenni, A.L.3
  • 15
    • 0030812346 scopus 로고    scopus 로고
    • Turnip yellow mosaic virus RNA-dependent RNA polymerase: Initiation of minus strand synthesis in vitro
    • 15 Singh, R. N. and Dreher, T. W. (1997) Turnip yellow mosaic virus RNA-dependent RNA polymerase: initiation of minus strand synthesis in vitro. Virology 233, 430-439
    • (1997) Virology , vol.233 , pp. 430-439
    • Singh, R.N.1    Dreher, T.W.2
  • 16
    • 0025758176 scopus 로고
    • Expression and characterization of poliovirus proteins 3BVPg, 3Cpro, and 3Dpol in recombinant baculovirus-infected Spodoptera frugiperda cells
    • 16 Neufeld, K. L., Richards, O. C. and Ehrenfeld, E. (1991) Expression and characterization of poliovirus proteins 3BVPg, 3Cpro, and 3Dpol in recombinant baculovirus-infected Spodoptera frugiperda cells. Virus Res. 19, 173-188
    • (1991) Virus Res. , vol.19 , pp. 173-188
    • Neufeld, K.L.1    Richards, O.C.2    Ehrenfeld, E.3
  • 17
    • 0030560951 scopus 로고    scopus 로고
    • RNA polymerase activity catalyzed by a potyvirus-encoded RNA-dependent RNA polymerase
    • 17 Hong, Y. and Hunt, A. G. (1996) RNA polymerase activity catalyzed by a potyvirus-encoded RNA-dependent RNA polymerase. Virology 226, 146-151
    • (1996) Virology , vol.226 , pp. 146-151
    • Hong, Y.1    Hunt, A.G.2
  • 18
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus
    • 18 Behrens, S. E., Tomei, L. and De Francesco, R. (1996) Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus. EMBO J. 15, 12-22
    • (1996) EMBO J. , vol.15 , pp. 12-22
    • Behrens, S.E.1    Tomei, L.2    De Francesco, R.3
  • 19
    • 0026325741 scopus 로고
    • Purification, characterization, and comparison of poliovirus RNA polymerase from native and recombinant sources
    • 19 Neufeld, K. L., Richards, O. C. and Ehrenfeld, E. (1991) Purification, characterization, and comparison of poliovirus RNA polymerase from native and recombinant sources. J. Biol. Chem. 266, 24212-24219
    • (1991) J. Biol. Chem. , vol.266 , pp. 24212-24219
    • Neufeld, K.L.1    Richards, O.C.2    Ehrenfeld, E.3
  • 22
    • 0027412448 scopus 로고
    • Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells
    • 22 Chaabihi, H., Ogliastro, M. H., Martin, M., Giraud, C., Devauchelle, G. and Cerutti, M. (1993) Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells. J. Virol. 67, 2664-2671
    • (1993) J. Virol. , vol.67 , pp. 2664-2671
    • Chaabihi, H.1    Ogliastro, M.H.2    Martin, M.3    Giraud, C.4    Devauchelle, G.5    Cerutti, M.6
  • 23
    • 0027517116 scopus 로고
    • Paracrystalline structure of cauliflower mosaic virus aphid transmission factor produced both in plants and in a heterologous system and relationship with a solubilized active form
    • 23 Blanc, S., Schmidt, I., Kuhl, G., Esperandieu, P., Lebeurier, G., Hull, R., Cerutti, M. and Louis, C. (1993) Paracrystalline structure of cauliflower mosaic virus aphid transmission factor produced both in plants and in a heterologous system and relationship with a solubilized active form. Virology 197, 283-292
    • (1993) Virology , vol.197 , pp. 283-292
    • Blanc, S.1    Schmidt, I.2    Kuhl, G.3    Esperandieu, P.4    Lebeurier, G.5    Hull, R.6    Cerutti, M.7    Louis, C.8
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 24 Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0032924359 scopus 로고    scopus 로고
    • Proteome analysis of polyacrylamide gel-separated proteins visualized by reversible negative staining using imidazole-zinc salts
    • 25 Castellanos-Serra, L., Proenza, W., Huerta, V., Moritz, R. L. and Simpson, R. J. (1999) Proteome analysis of polyacrylamide gel-separated proteins visualized by reversible negative staining using imidazole-zinc salts. Electrophoresis 20, 732-737
    • (1999) Electrophoresis , vol.20 , pp. 732-737
    • Castellanos-Serra, L.1    Proenza, W.2    Huerta, V.3    Moritz, R.L.4    Simpson, R.J.5
  • 26
    • 0031089374 scopus 로고    scopus 로고
    • Efficient transcription of the tRNA-like structure of turnip yellow mosaic virus by a template-dependent and specific viral RNA polymerase obtained by a new procedure
    • 26 Deiman, B. A., Seron, K., Jaspars, E. M. and Pleij, C. W. (1997) Efficient transcription of the tRNA-like structure of turnip yellow mosaic virus by a template-dependent and specific viral RNA polymerase obtained by a new procedure. J Virol. Methods 64, 181-195
    • (1997) J Virol. Methods , vol.64 , pp. 181-195
    • Deiman, B.A.1    Seron, K.2    Jaspars, E.M.3    Pleij, C.W.4
  • 27
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • 27 Fujimuro, M., Sawada, H. and Yokosawa, H. (1994) Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett. 349, 173-180
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 28
    • 0025948991 scopus 로고
    • Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to Immobilon
    • 28 Kamps, M. P. (1991) Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to Immobilon. Methods Enzymol. 201, 21-27
    • (1991) Methods Enzymol , vol.201 , pp. 21-27
    • Kamps, M.P.1
  • 29
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • 29 Duclos, B., Marcandier, S. and Cozzone, A. J. (1991) Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol 201, 10-21
    • (1991) Methods Enzymol , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.J.3
  • 30
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • 30 Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T. and Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature (London) 379, 466-469
    • (1996) Nature (London) , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 31
    • 0021967194 scopus 로고
    • Purification of proteins by IMAC
    • 31 Sulkowski, E. (1985) Purification of proteins by IMAC. Trends Biotechnol. 3, 1-7
    • (1985) Trends Biotechnol. , vol.3 , pp. 1-7
    • Sulkowski, E.1
  • 32
    • 0024637005 scopus 로고
    • Expression of eukaryotic genes in insect cultures
    • 32 Fraser, M. J. (1989) Expression of eukaryotic genes in insect cultures. In Vitro Cell. Dev. Biol. 25, 225-235
    • (1989) In Vitro Cell. Dev. Biol. , vol.25 , pp. 225-235
    • Fraser, M.J.1
  • 33
    • 0024408630 scopus 로고
    • The transition of RNA polymerase II from initiation to elongation is associated with phosphorylation of the carboxyl-terminal domain of subunit IIa
    • 33 Payne, J. M., Laybourn, P. J. and Dahmus, M. E. (1989) The transition of RNA polymerase II from initiation to elongation is associated with phosphorylation of the carboxyl-terminal domain of subunit IIa. J. Biol. Chem. 264, 19621-19629
    • (1989) J. Biol. Chem. , vol.264 , pp. 19621-19629
    • Payne, J.M.1    Laybourn, P.J.2    Dahmus, M.E.3
  • 34
    • 0031579246 scopus 로고    scopus 로고
    • Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization
    • 34 Hwang, S. B., Park, K. J., Kim, Y. S., Sung, Y. C. and Lai, M. M. (1997) Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization. Virology 227, 439-446
    • (1997) Virology , vol.227 , pp. 439-446
    • Hwang, S.B.1    Park, K.J.2    Kim, Y.S.3    Sung, Y.C.4    Lai, M.M.5
  • 35
    • 0029916915 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1995
    • 35 Bairoch, A., Bucher, P. and Hofmann, K. (1996) The PROSITE database, its status in 1995. Nucleic Acids Res. 24, 189-196
    • (1996) Nucleic Acids Res. , vol.24 , pp. 189-196
    • Bairoch, A.1    Bucher, P.2    Hofmann, K.3
  • 36
    • 0032553017 scopus 로고    scopus 로고
    • Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: Alpha 4 is glutamylated at two residues
    • 36 Redeker, V., Rossier, J. and Frankfurter, A. (1998) Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: alpha 4 is glutamylated at two residues. Biochemistry 37, 14838-14844
    • (1998) Biochemistry , vol.37 , pp. 14838-14844
    • Redeker, V.1    Rossier, J.2    Frankfurter, A.3
  • 37
    • 0028362020 scopus 로고
    • An approach to locate phosphorylation sites in a phosphoprotein: Mass mapping by combining specific enzymatic degradation with matrix-assisted laser desorption/ionization mass spectrometry
    • 37 Liao, P. C., Leykam, J., Andrews, P. C., Gage, D. A. and Allison, J. (1994) An approach to locate phosphorylation sites in a phosphoprotein: mass mapping by combining specific enzymatic degradation with matrix-assisted laser desorption/ionization mass spectrometry. Anal. Biochem 219, 9-20
    • (1994) Anal. Biochem , vol.219 , pp. 9-20
    • Liao, P.C.1    Leykam, J.2    Andrews, P.C.3    Gage, D.A.4    Allison, J.5
  • 38
    • 0033238004 scopus 로고    scopus 로고
    • Enhanced detection of phosphopeptides in matrix-assisted laser desorption/ionization mass spectrometry using ammonium salts
    • 38 Asara, J. M. and Allison, J. (1999) Enhanced detection of phosphopeptides in matrix-assisted laser desorption/ionization mass spectrometry using ammonium salts. J. Am. Soc. Mass Spectrom. 10, 35-44
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 35-44
    • Asara, J.M.1    Allison, J.2
  • 39
    • 0031871699 scopus 로고    scopus 로고
    • Suppression effects in enzymatic peptide ladder sequencing using ultraviolet matrix assisted laser desorption/ionization mass spectrometry
    • 39 Kratzer, R., Eckerskorn, C., Karas, M. and Lottspeich, F. (1998) Suppression effects in enzymatic peptide ladder sequencing using ultraviolet matrix assisted laser desorption/ionization mass spectrometry. Electrophoresis 19, 1910-1919
    • (1998) Electrophoresis , vol.19 , pp. 1910-1919
    • Kratzer, R.1    Eckerskorn, C.2    Karas, M.3    Lottspeich, F.4
  • 40
    • 0025743809 scopus 로고
    • The phytogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses
    • 40 Koonin, E. V. (1991) The phytogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses. J. Gen. Virol. 72, 2197-2206
    • (1991) J. Gen. Virol. , vol.72 , pp. 2197-2206
    • Koonin, E.V.1
  • 41
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • 41 Rechsteiner, M. and Rogers, S. W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 42
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • 42 Rogers, S , Wells, R. and Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234, 364-368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 43
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability
    • 43 Lin, R., Beauparlant, P., Makris, C., Meloche, S. and Hiscott, J. (1996) Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. Mol. Cell. Biol. 16, 1401-1409
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 44
    • 0029670193 scopus 로고    scopus 로고
    • Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation
    • 44 Lanker, S., Valdivieso, M. H. and Wittenberg, C. (1996) Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation. Science 271, 1597-1601
    • (1996) Science , vol.271 , pp. 1597-1601
    • Lanker, S.1    Valdivieso, M.H.2    Wittenberg, C.3
  • 45
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease
    • 45 Marchal, C., Haguenauer-Tsapis, R. and Urban-Grimal, D. (1998) A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease. Mol. Cell. Biol. 18, 314-321
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 314-321
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 46
    • 0025912370 scopus 로고
    • Proteolytic maturation of the 206-kDa nonstructural protein encoded by turnip yellow mosaic virus RNA
    • 46 Bransom, K. L., Weiland, J. J. and Dreher, T. W. (1991) Proteolytic maturation of the 206-kDa nonstructural protein encoded by turnip yellow mosaic virus RNA. Virology 184, 351-358
    • (1991) Virology , vol.184 , pp. 351-358
    • Bransom, K.L.1    Weiland, J.J.2    Dreher, T.W.3
  • 47
    • 0026558786 scopus 로고
    • Comparison of the strategies of expression of five tymovirus RNAs by in vitro translation studies
    • 47 Kadaré, G, Drugeon, G., Savithri, H. S. and Haenni, A. L. (1992) Comparison of the strategies of expression of five tymovirus RNAs by in vitro translation studies. J. Gen. Virol. 73, 493-498
    • (1992) J. Gen. Virol. , vol.73 , pp. 493-498
    • Kadaré, G.1    Drugeon, G.2    Savithri, H.S.3    Haenni, A.L.4
  • 48
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • 48 Ciechanover, A. (1998) The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17, 7151-7160
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 49
    • 0028108747 scopus 로고
    • Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system
    • 49 Cahoreau, C., Garnier, L., Djiane, J., Devauchelle, G. and Cerutti, M. (1994) Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system. FEBS Lett. 350, 230-234
    • (1994) FEBS Lett. , vol.350 , pp. 230-234
    • Cahoreau, C.1    Garnier, L.2    Djiane, J.3    Devauchelle, G.4    Cerutti, M.5
  • 50
    • 0031881237 scopus 로고    scopus 로고
    • Characterization of the interactions of human papillomavirus type 16 E6 with p53 and E6-associated protein in insect and human cells
    • 50 Daniels, P. R., Sanders, C. M. and Maitland, N. J. (1998) Characterization of the interactions of human papillomavirus type 16 E6 with p53 and E6-associated protein in insect and human cells. J. Gen. Virol. 79, 489-499
    • (1998) J. Gen. Virol. , vol.79 , pp. 489-499
    • Daniels, P.R.1    Sanders, C.M.2    Maitland, N.J.3
  • 51
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • 51 Vierstra, R. D. (1996) Proteolysis in plants: mechanisms and functions. Plant Mol. Biol. 32, 275-302
    • (1996) Plant Mol. Biol. , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 52
    • 0023852637 scopus 로고
    • Proteases involved in the processing of viral polyproteins
    • 52 Wellink, J. and van Kammen, A. (1988) Proteases involved in the processing of viral polyproteins. Arch. Virol. 98, 1-26
    • (1988) Arch. Virol. , vol.98 , pp. 1-26
    • Wellink, J.1    Van Kammen, A.2
  • 53
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • 53 Strauss, J. H. and Strauss, E. G. (1994) The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 58, 491-562
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 55
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • 55 Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. U.S.A. 93, 12142-12149
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12142-12149
    • Varshavsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.