메뉴 건너뛰기




Volumn 266, Issue 1, 2000, Pages 42-51

Actin-binding cellular proteins inside human immunodeficiency virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; BINDING PROTEIN; ELONGATION FACTOR 1ALPHA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 60; ISOMERASE; LEUKOSIALIN; NUCLEOSIDE DIPHOSPHATE KINASE; PHOSPHATIDYLETHANOLAMINE; PROTEINASE; SUBTILISIN; VIRUS PROTEIN;

EID: 0034606670     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.0075     Document Type: Article
Times cited : (114)

References (58)
  • 3
    • 0031592573 scopus 로고    scopus 로고
    • Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations
    • Bess J. W. Jr., Gorelick R. J., Bosche W. J., Henderson L. E., Arthur L. O. Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations. Virology. 230:1997;134-144.
    • (1997) Virology , vol.230 , pp. 134-144
    • Bess J.W., Jr.1    Gorelick, R.J.2    Bosche, W.J.3    Henderson, L.E.4    Arthur, L.O.5
  • 4
    • 0026592529 scopus 로고
    • Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses
    • Bess J. W. Jr., Powell P. J., Issaq H. J., Schumack L. J., Grimes M. K., Henderson L. E., Arthur L. O. Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses. J. Virol. 66:1992;840-847.
    • (1992) J. Virol. , vol.66 , pp. 840-847
    • Bess J.W., Jr.1    Powell, P.J.2    Issaq, H.J.3    Schumack, L.J.4    Grimes, M.K.5    Henderson, L.E.6    Arthur, L.O.7
  • 5
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin a is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten D., Franke E. K., Luban J. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70:1996;3551-3560.
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 8
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • Dever T. E., Costello C. E., Owens C. L., Rosenberry T. L., Merrick W. C. Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. J. Biol. Chem. 264:1989;20518-20525.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 9
    • 0021288310 scopus 로고
    • Cytoskeleton-associated Pr65gag and assembly of retrovirus temperature-sensitive mutants in chronically infected cells
    • Edbauer C. A., Naso R. B. Cytoskeleton-associated Pr65gag and assembly of retrovirus temperature-sensitive mutants in chronically infected cells. Virology. 134:1984;389-397.
    • (1984) Virology , vol.134 , pp. 389-397
    • Edbauer, C.A.1    Naso, R.B.2
  • 10
    • 0029020353 scopus 로고
    • PH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha
    • Edmonds B. T., Murray J., Condeelis J. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha. J. Biol. Chem. 270:1995;15222-15230.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 11
    • 0032493656 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/nucleoside diphosphate kinase A: Two old enzymes combine for the novel Nm23 protein phosphotransferase function
    • Engel M., Seifert M., Theisinger B., Seyfert U., Welter C. Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/nucleoside diphosphate kinase A: Two old enzymes combine for the novel Nm23 protein phosphotransferase function. J. Biol. Chem. 273:1998;20058-20065.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20058-20065
    • Engel, M.1    Seifert, M.2    Theisinger, B.3    Seyfert, U.4    Welter, C.5
  • 13
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin a into HIV-1 virions
    • Franke E. K., Yuan H. E. H., Luban J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature. 372:1994;359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 14
    • 0031917789 scopus 로고    scopus 로고
    • Expression of phosphatidylethanolamine-binding protein in the male reproductive tract: Immunolocalisation and expression in prepubertal and adult rat testes and epididymides
    • Frayne J., McMillen A., Love S., Hall L. Expression of phosphatidylethanolamine-binding protein in the male reproductive tract: Immunolocalisation and expression in prepubertal and adult rat testes and epididymides. Mol. Reprod. Dev. 49:1998;454-460.
    • (1998) Mol. Reprod. Dev. , vol.49 , pp. 454-460
    • Frayne, J.1    McMillen, A.2    Love, S.3    Hall, L.4
  • 15
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom H. R. Assembly and morphology of HIV: potential effect of structure on viral function. AIDS. 5:1991;617-638.
    • (1991) AIDS , vol.5 , pp. 617-638
    • Gelderblom, H.R.1
  • 16
    • 0031592609 scopus 로고    scopus 로고
    • Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations
    • Gluschankof P., Mondor I., Gelderblom H. R., Sattentau Q. J. Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations. Virology. 230:1997;125-133.
    • (1997) Virology , vol.230 , pp. 125-133
    • Gluschankof, P.1    Mondor, I.2    Gelderblom, H.R.3    Sattentau, Q.J.4
  • 17
    • 0028136693 scopus 로고
    • Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu
    • Gonen H., Smith C. E., Siegel N. R., Kahana C., Merrick W. C., Chakraburtty K., Schwartz A. L., Ciechanover A. Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proc. Natl. Acad. Sci. USA. 91:1994;7648-7652.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7648-7652
    • Gonen, H.1    Smith, C.E.2    Siegel, N.R.3    Kahana, C.4    Merrick, W.C.5    Chakraburtty, K.6    Schwartz, A.L.7    Ciechanover, A.8
  • 18
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation
    • He H., Watanabe T., Zhan X., Huang C., Schuuring E., Fukami K., Takenawa T., Kumar C. C., Simpson R. J., Maruta H. Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation. Mol. Cell. Biol. 18:1998;3829-3837.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 19
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processings, and complete amino acid sequences
    • Henderson L. E., Bowers M. A., Sowder II R. C., Serabyn S., Johnson D. G., Bess J. W. Jr., Arthur L. O., Bryant D. K., Fenselau C. Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processings, and complete amino acid sequences. J. Virol. 66:1992;1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder R.C. II3    Serabyn, S.4    Johnson, D.G.5    Bess J.W., Jr.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 20
    • 0001106826 scopus 로고
    • Chemical and immunological characterizations of equine infectious anemia virus gag-encoded proteins
    • Henderson L. E., Sowder II R. C., Smythers G., Oroszlan S. Chemical and immunological characterizations of equine infectious anemia virus gag-encoded proteins. J. Virol. 61:1988;2587-2595.
    • (1988) J. Virol. , vol.61 , pp. 2587-2595
    • Henderson, L.E.1    Sowder R.C. II2    Smythers, G.3    Oroszlan, S.4
  • 21
    • 0032506212 scopus 로고    scopus 로고
    • Inhibition of cellular glycoprotein incorporation into human immunodeficiency virus-like particles by coexpression of additional cellular interaction partner
    • Henriksson P., Bosch V. Inhibition of cellular glycoprotein incorporation into human immunodeficiency virus-like particles by coexpression of additional cellular interaction partner. Virology. 251:1998;16-21.
    • (1998) Virology , vol.251 , pp. 16-21
    • Henriksson, P.1    Bosch, V.2
  • 23
    • 0024374371 scopus 로고
    • Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage
    • Kitamura D., Kaneko H., Miyagoe Y., Ariyasu T., Watanabe T. Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage. Nucleic Acids Res. 17:1989;9367-9379.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9367-9379
    • Kitamura, D.1    Kaneko, H.2    Miyagoe, Y.3    Ariyasu, T.4    Watanabe, T.5
  • 25
    • 0032587326 scopus 로고    scopus 로고
    • Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin
    • Liu B., Dai R., Tian C. J., Dawson L., Gorelick R., Yu X. F. Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin. J. Virol. 73:1999;2901-2908.
    • (1999) J. Virol. , vol.73 , pp. 2901-2908
    • Liu, B.1    Dai, R.2    Tian, C.J.3    Dawson, L.4    Gorelick, R.5    Yu, X.F.6
  • 27
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K. P., Hanes S. D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 28
    • 0028267575 scopus 로고
    • Viral interactions with the host-cell cytoskeleton: The role of retroviral proteases
    • Luftig R. B., Lupo L. D. Viral interactions with the host-cell cytoskeleton: the role of retroviral proteases. Trends Microbiol. 2:1994;178-182.
    • (1994) Trends Microbiol. , vol.2 , pp. 178-182
    • Luftig, R.B.1    Lupo, L.D.2
  • 30
    • 0024788703 scopus 로고
    • Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments
    • Mejean C., Pons F., Benyamin Y., Roustan C. Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments. Biochem. J. 264:1989;671-677.
    • (1989) Biochem. J. , vol.264 , pp. 671-677
    • Mejean, C.1    Pons, F.2    Benyamin, Y.3    Roustan, C.4
  • 31
    • 0028816615 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold)
    • Nagy E., Rigby W. F. Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-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.2
  • 32
    • 0027332763 scopus 로고
    • Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV
    • Orentas R. J., Hildreth J. E. K. Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV. AIDS Res. Hum. Retroviruses. 9:1993;1157-1165.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1157-1165
    • Orentas, R.J.1    Hildreth, J.E.K.2
  • 33
    • 0030930244 scopus 로고    scopus 로고
    • Cellular proteins in HIV
    • Ott D. E. Cellular proteins in HIV. Rev. Med. Virol. 7:1997;167-180.
    • (1997) Rev. Med. Virol. , vol.7 , pp. 167-180
    • Ott, D.E.1
  • 34
    • 0032889226 scopus 로고    scopus 로고
    • Mutational analysis of the hydrophobic tail of the human immunodeficiency virus type 1 p6(Gag) protein produces a mutant that fails to package its envelope protein
    • Ott D. E., Chertova E. N., Busch L. K., Coren L. V., Gagliardi T. D., Johnson D. G. Mutational analysis of the hydrophobic tail of the human immunodeficiency virus type 1 p6(Gag) protein produces a mutant that fails to package its envelope protein. J. Virol. 73:1999;19-28.
    • (1999) J. Virol. , vol.73 , pp. 19-28
    • Ott, D.E.1    Chertova, E.N.2    Busch, L.K.3    Coren, L.V.4    Gagliardi, T.D.5    Johnson, D.G.6
  • 35
    • 0029151733 scopus 로고
    • Analysis and localization of cyclophilin a found in the virions of human immunodeficiency virus type 1 MN strain
    • Ott D. E., Coren L. V., Johnson D. G., Sowder R. C. II, Arthur L. O., Henderson L. E. Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain. AIDS Res. Hum. Retroviruses. 11:1995a;1003-1006.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1003-1006
    • Ott, D.E.1    Coren, L.V.2    Johnson, D.G.3    Sowder R.C. II4    Arthur, L.O.5    Henderson, L.E.6
  • 37
    • 0028904526 scopus 로고
    • The majority of cells are superinfected in a cloned cell line that produces high levels of human immunodeficiency virus type 1 strain MN
    • Ott D. E., Nigida S. M. Jr., Henderson L. E., Arthur L. O. The majority of cells are superinfected in a cloned cell line that produces high levels of human immunodeficiency virus type 1 strain MN. J. Virol. 69:1995b;2443-2450.
    • (1995) J. Virol. , vol.69 , pp. 2443-2450
    • Ott, D.E.1    Nigida S.M., Jr.2    Henderson, L.E.3    Arthur, L.O.4
  • 39
    • 0028217413 scopus 로고
    • Role of the cytoskeleton in cell-to-cell transmission of human immunodeficiency virus
    • Pearce-Pratt R., Malamud D., Phillips D. M. Role of the cytoskeleton in cell-to-cell transmission of human immunodeficiency virus. J. Virol. 68:1994;2898-2905.
    • (1994) J. Virol. , vol.68 , pp. 2898-2905
    • Pearce-Pratt, R.1    Malamud, D.2    Phillips, D.M.3
  • 40
    • 0033102128 scopus 로고    scopus 로고
    • Tagging the human immunodeficiency virus gag protein with green fluorescent protein: Minimal evidence for colocalisation with actin
    • Perrin-Tricaud C., Davoust J., Jones I. M. Tagging the human immunodeficiency virus gag protein with green fluorescent protein: Minimal evidence for colocalisation with actin. Virology. 255:1999;20-25.
    • (1999) Virology , vol.255 , pp. 20-25
    • Perrin-Tricaud, C.1    Davoust, J.2    Jones, I.M.3
  • 42
    • 0026345896 scopus 로고
    • A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base
    • Poorman R. A., Tomasselli A. G., Heinrikson R. L., Kezdy F. J. A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base. J. Biol. Chem. 266:1991;14554-14561.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14554-14561
    • Poorman, R.A.1    Tomasselli, A.G.2    Heinrikson, R.L.3    Kezdy, F.J.4
  • 43
    • 0029941433 scopus 로고    scopus 로고
    • HIV-1 Gag protein associates with F-actin present in microfilaments
    • Rey O., Canon J., Krogstad P. HIV-1 Gag protein associates with F-actin present in microfilaments. Virology. 220:1996;530-534.
    • (1996) Virology , vol.220 , pp. 530-534
    • Rey, O.1    Canon, J.2    Krogstad, P.3
  • 44
    • 0028901720 scopus 로고
    • Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells
    • Sasaki H., Nakamura M., Ohno T., Matsuda Y., Yuda Y., Nonomura Y. Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells. Proc. Natl. Acad. Sci. USA. 92:1995;2026-2030.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2026-2030
    • Sasaki, H.1    Nakamura, M.2    Ohno, T.3    Matsuda, Y.4    Yuda, Y.5    Nonomura, Y.6
  • 45
    • 0030958826 scopus 로고    scopus 로고
    • Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest
    • Selig L., Benichou S., Rogel M. E., Wu L. I., Vodicka M. A., Sire J., Benarous R., Emerman M. Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest. J. Virol. 71:1997;4842-4846.
    • (1997) J. Virol. , vol.71 , pp. 4842-4846
    • Selig, L.1    Benichou, S.2    Rogel, M.E.3    Wu, L.I.4    Vodicka, M.A.5    Sire, J.6    Benarous, R.7    Emerman, M.8
  • 46
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
    • Shen M., Stukenberg P. T., Kirschner M. W., Lu K. P. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12:1998;706-720.
    • (1998) Genes Dev. , vol.12 , pp. 706-720
    • Shen, M.1    Stukenberg, P.T.2    Kirschner, M.W.3    Lu, K.P.4
  • 47
    • 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
  • 48
    • 0029006230 scopus 로고
    • The mode of actions of glyceraldehyde-3-phosphate dehydrogenase identified as an immunoglobulin production stimulating factor
    • Sugahara T., Shirahata S., Sasaki T., Murakami H. The mode of actions of glyceraldehyde-3-phosphate dehydrogenase identified as an immunoglobulin production stimulating factor. FEBS Lett. 368:1995;92-96.
    • (1995) FEBS Lett. , vol.368 , pp. 92-96
    • Sugahara, T.1    Shirahata, S.2    Sasaki, T.3    Murakami, H.4
  • 50
    • 0029009255 scopus 로고
    • LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck
    • Takemoto Y., Furuta M., Li X. K., Strong-Sparks W. J., Hashimoto Y. LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck. EMBO J. 14:1995;3403-3414.
    • (1995) EMBO J. , vol.14 , pp. 3403-3414
    • Takemoto, Y.1    Furuta, M.2    Li, X.K.3    Strong-Sparks, W.J.4    Hashimoto, Y.5
  • 51
    • 0029828378 scopus 로고    scopus 로고
    • Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules
    • Takemoto Y., Sato M., Furuta M., Hashimoto Y. Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules. Int. Immunol. 8:1996;1699-1705.
    • (1996) Int. Immunol. , vol.8 , pp. 1699-1705
    • Takemoto, Y.1    Sato, M.2    Furuta, M.3    Hashimoto, Y.4
  • 53
    • 0343341327 scopus 로고
    • The presence of actin in enveloped viruses
    • R. Goldman, T. Pollard, & J. Rosenbaums. Cold Spring Harbor: Cold Spring Harbor Laboratory
    • Wang E., Wolf B. A., Lamb R. A., Choppin P. W., Goldberg A. R. The presence of actin in enveloped viruses. Goldman R., Pollard T., Rosenbaums J. Cell Motility. 1976;589-599 Cold Spring Harbor Laboratory, Cold Spring Harbor.
    • (1976) Cell Motility , pp. 589-599
    • Wang, E.1    Wolf, B.A.2    Lamb, R.A.3    Choppin, P.W.4    Goldberg, A.R.5
  • 54
    • 0032982141 scopus 로고    scopus 로고
    • Actin associates with the nucleocapsid domain of the human immunodeficiency virus gag polyprotein
    • Wilk T., Gowen B., Fuller S. D. Actin associates with the nucleocapsid domain of the human immunodeficiency virus gag polyprotein. J. Virol. 73:1999;1931-1940.
    • (1999) J. Virol. , vol.73 , pp. 1931-1940
    • Wilk, T.1    Gowen, B.2    Fuller, S.D.3
  • 56
    • 0025000290 scopus 로고
    • Identification of an actin-binding protein from Dictyostelium as elongation factor 1α
    • Yang F., Demma M., Warren V., Dharmawardhane S., Condeelis J. Identification of an actin-binding protein from Dictyostelium as elongation factor 1α Nature. 347:1990;494-496.
    • (1990) Nature , vol.347 , pp. 494-496
    • Yang, F.1    Demma, M.2    Warren, V.3    Dharmawardhane, S.4    Condeelis, J.5
  • 57
    • 0032529511 scopus 로고    scopus 로고
    • Identification of glyceraldehyde-3-phosphate dehydrogenase as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element
    • Zang W. Q., Fieno A. M., Grant R. A., Yen T. S. Identification of glyceraldehyde-3-phosphate dehydrogenase as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element. Virology. 248:1998;46-52.
    • (1998) Virology , vol.248 , pp. 46-52
    • Zang, W.Q.1    Fieno, A.M.2    Grant, R.A.3    Yen, T.S.4
  • 58
    • 0020361496 scopus 로고
    • The pseudotypic paradox
    • Zavada J. The pseudotypic paradox. J. Gen. Virol. 63:1982;15-24.
    • (1982) J. Gen. Virol. , vol.63 , pp. 15-24
    • Zavada, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.