메뉴 건너뛰기




Volumn 224, Issue 1, 1996, Pages 268-275

Comparative properties of feline immunodeficiency virus (FIV) and human immunodeficiency virus type 1 (HIV-1) proteinases prepared by total chemical synthesis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; PROTEINASE INHIBITOR; SYNTHETIC PEPTIDE;

EID: 0010738069     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0528     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 0025049031 scopus 로고
    • Immunologic abnormalities in pathogen-free cats experimentally infected with feline immunodeficiency virus
    • Ackley, C. D., Yamamoto, J. K., Levy, N., Pedersen, N. C., and Cooper, M. D. (1990). Immunologic abnormalities in pathogen-free cats experimentally infected with feline immunodeficiency virus. J. Virol. 64, 5652-5655.
    • (1990) J. Virol. , vol.64 , pp. 5652-5655
    • Ackley, C.D.1    Yamamoto, J.K.2    Levy, N.3    Pedersen, N.C.4    Cooper, M.D.5
  • 2
    • 0025169561 scopus 로고
    • An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection
    • Ashorn, P., McQuade, T. J., Thaisrivongs, S., Tomasselli, A. G., Tarpley, W. G., and Moss, B. (1990). An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection. Proc. Natl. Acad. Sci. USA 87, 7472-7476.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7472-7476
    • Ashorn, P.1    McQuade, T.J.2    Thaisrivongs, S.3    Tomasselli, A.G.4    Tarpley, W.G.5    Moss, B.6
  • 5
    • 0021931766 scopus 로고
    • A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins
    • Crawford, S., and Goff, S. P. (1985). A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins. J. Virol. 53, 899-907.
    • (1985) J. Virol. , vol.53 , pp. 899-907
    • Crawford, S.1    Goff, S.P.2
  • 6
  • 7
    • 0028013171 scopus 로고
    • Generation and characterization of a human immunodeficiency virus type 1 (HIV-1) mutant resistant to an HIV-1 protease inhibitor
    • El-Farrash, M. A., Kuroda, M. J., Kitazaki, T., Masuda, T., Kalo, K., Hatanaka, M., and Harada, S. (1994). Generation and characterization of a human immunodeficiency virus type 1 (HIV-1) mutant resistant to an HIV-1 protease inhibitor. J. Virol. 68, 233-239.
    • (1994) J. Virol. , vol.68 , pp. 233-239
    • El-Farrash, M.A.1    Kuroda, M.J.2    Kitazaki, T.3    Masuda, T.4    Kalo, K.5    Hatanaka, M.6    Harada, S.7
  • 9
    • 0026721254 scopus 로고
    • Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic-or -aromatic*pro-cleavage sites
    • Griffiths, J. T., Phylip, L. H., Konvalinka, J., Strop, P., Gustchina, A., Wlodawer, A., Davenport, R. J., Briggs, R., Dunn, B. M., and Kay, J. (1992). Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic-or -aromatic*pro-cleavage sites. Biochemistry 31, 5193-5200.
    • (1992) Biochemistry , vol.31 , pp. 5193-5200
    • Griffiths, J.T.1    Phylip, L.H.2    Konvalinka, J.3    Strop, P.4    Gustchina, A.5    Wlodawer, A.6    Davenport, R.J.7    Briggs, R.8    Dunn, B.M.9    Kay, J.10
  • 10
    • 0025952925 scopus 로고
    • HIV protease: A novel chemotherapeutic target for AIDS
    • Huff, J. R. (1991). HIV protease: a novel chemotherapeutic target for AIDS. [Review] J. Med. Chem. 34, 2305-2314.
    • (1991) J. Med. Chem. , vol.34 , pp. 2305-2314
    • Huff, J.R.1
  • 11
    • 0026005186 scopus 로고
    • Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism
    • Hyland, L. J., Tomaszek, T. A. Jr., and Meek, T. D. (1991a). Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism. Biochemistry 30, 8454-8463.
    • (1991) Biochemistry , vol.30 , pp. 8454-8463
    • Hyland, L.J.1    Tomaszek T.A., Jr.2    Meek, T.D.3
  • 13
    • 0026325601 scopus 로고
    • Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S
    • Ido, E., Han, H. P., Kezdy, F. J., Tang, J. (1991). Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S. J. Biol. Chem. 266, 24359-24366.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24359-24366
    • Ido, E.1    Han, H.P.2    Kezdy, F.J.3    Tang, J.4
  • 15
    • 0021846499 scopus 로고
    • Murine leukemia virus maturation: Protease region required for conversion from "immature" to "mature" core form and for virus infectivity
    • Katoh, I., Yoshinaka, Y., Rein, A., Shibuya, M., Odaka, T., and Oroszlan, S. (1985). Murine leukemia virus maturation: Protease region required for conversion from "immature" to "mature" core form and for virus infectivity. Virology 145, 280-292.
    • (1985) Virology , vol.145 , pp. 280-292
    • Katoh, I.1    Yoshinaka, Y.2    Rein, A.3    Shibuya, M.4    Odaka, T.5    Oroszlan, S.6
  • 17
    • 0022546859 scopus 로고
    • HTLV-III gag protein is processed in yeast cells by the virus pol-protease
    • Kramer, R. A., Schaber, M. D., Skalka, A. M., Ganguly, K., Wong-Staa, I. F., and Reddy, E. P. (1986). HTLV-III gag protein is processed in yeast cells by the virus pol-protease. Science. 231, 1580-1584.
    • (1986) Science , vol.231 , pp. 1580-1584
    • Kramer, R.A.1    Schaber, M.D.2    Skalka, A.M.3    Ganguly, K.4    Wong-Staa, I.F.5    Reddy, E.P.6
  • 18
    • 0024492495 scopus 로고
    • Crystal structure of a retroviral protease proves relationship to aspartic protease family
    • Miller, M., Jaskolski, M., Rao, J. K., Leis, J., and Wlodawer, A. (1989). Crystal structure of a retroviral protease proves relationship to aspartic protease family. Nature. 337, 576-579.
    • (1989) Nature , vol.337 , pp. 576-579
    • Miller, M.1    Jaskolski, M.2    Rao, J.K.3    Leis, J.4    Wlodawer, A.5
  • 20
    • 0025186450 scopus 로고
    • Molecular targets for AIDS therapy
    • Mitsuya, H., Yarchoan, R., and Broder, S. (1990). Molecular targets for AIDS therapy. [Review] Science. 249, 1533-1544.
    • (1990) Science , vol.249 , pp. 1533-1544
    • Mitsuya, H.1    Yarchoan, R.2    Broder, S.3
  • 21
    • 0024366204 scopus 로고
    • Nucleotide sequence analysis of feline immunodeficiency virus: Genome organization and relationship to other lentiviruses
    • Olmsted, R. A., Hirsch, V. M., Purcell, R. H., and Johnson, P. R. (1989). Nucleotide sequence analysis of feline immunodeficiency virus: genome organization and relationship to other lentiviruses. Proc. Natl. Acad. Sci. USA 86, 8088-8092.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8088-8092
    • Olmsted, R.A.1    Hirsch, V.M.2    Purcell, R.H.3    Johnson, P.R.4
  • 22
    • 0027219220 scopus 로고
    • In vitro isolation and identification of human immunodeficiency virus (HIV) variants with reduced sensitivity to C-2 symmetrical inhibitors of HIV type 1 protease
    • Otto, M. J., Garber, S., Winslow, D. L., Reid, C. D., Aldrich, P., Jadhav, P. K., Patterson, C. E., Hodge, C. N., and Cheng, Y. S. (1993). In vitro isolation and identification of human immunodeficiency virus (HIV) variants with reduced sensitivity to C-2 symmetrical inhibitors of HIV type 1 protease. Proc. Natl. Acad. Sci. USA 90, 7543-7547.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7543-7547
    • Otto, M.J.1    Garber, S.2    Winslow, D.L.3    Reid, C.D.4    Aldrich, P.5    Jadhav, P.K.6    Patterson, C.E.7    Hodge, C.N.8    Cheng, Y.S.9
  • 23
    • 0023137671 scopus 로고
    • Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome
    • Pedersen, N. C., Ho, E. W., Brown, M. L., and Yamamoto, J. K. (1987). Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome. Science 235, 790-793.
    • (1987) Science , vol.235 , pp. 790-793
    • Pedersen, N.C.1    Ho, E.W.2    Brown, M.L.3    Yamamoto, J.K.4
  • 24
    • 0025053644 scopus 로고
    • Comparison of two host cell range variants of feline immunodeficiency virus
    • Phillips, T. R., Talbott, R. L., Lamont, C., Muir, S., Lovelace, K., and Elder, J. H. (1990). Comparison of two host cell range variants of feline immunodeficiency virus. J. Virol. 64, 4605-4613.
    • (1990) J. Virol. , vol.64 , pp. 4605-4613
    • Phillips, T.R.1    Talbott, R.L.2    Lamont, C.3    Muir, S.4    Lovelace, K.5    Elder, J.H.6
  • 26
    • 0019627519 scopus 로고
    • Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction
    • Sarin, V. K., Kent, S. B., Tam, J. P., and Merrifield, R. B. (1981). Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction. Anal. Biochem. 117, 147-157.
    • (1981) Anal. Biochem. , vol.117 , pp. 147-157
    • Sarin, V.K.1    Kent, S.B.2    Tam, J.P.3    Merrifield, R.B.4
  • 27
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnölzer, M., Alewood, P., Jones, A., Alewood, D., and Kent, S. B. (1992a). In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int. J. Peptide Protein Res. 40, 180-193.
    • (1992) Int. J. Peptide Protein Res. , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 28
    • 0026747625 scopus 로고
    • Lonspray tandem mass spectrometry in peptide synthesis: Structural characterization of minor by-products in the synthesis of ACP(65-74)
    • Schnölzer, M., Jones, A., Alewood, P. F., and Kent, S. B. (1992b). lonspray tandem mass spectrometry in peptide synthesis: structural characterization of minor by-products in the synthesis of ACP(65-74). Anal. Biochem. 204, 335-343.
    • (1992) Anal. Biochem. , vol.204 , pp. 335-343
    • Schnölzer, M.1    Jones, A.2    Alewood, P.F.3    Kent, S.B.4
  • 29
    • 0029569075 scopus 로고
    • Selectivity in the inhibition of HIV and FIV protease: Inhibitory and mechanistic studies of pyrrolidine-containing α-keto amide and hydroxyethylamine core structures
    • Slee, D. H., Laslo, K. L., Elder, J. H., Oilman, I. R., Gustchina, A., Kervinen, J., Zdanov, A., Wlodawer, A., and Wong, C.-H. (1995). Selectivity in the inhibition of HIV and FIV protease: inhibitory and mechanistic studies of pyrrolidine-containing α-keto amide and hydroxyethylamine core structures. J. Am. Chem. Soc. 117, 11867-11878.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11867-11878
    • Slee, D.H.1    Laslo, K.L.2    Elder, J.H.3    Oilman, I.R.4    Gustchina, A.5    Kervinen, J.6    Zdanov, A.7    Wlodawer, A.8    Wong, C.-H.9
  • 31
    • 0025663423 scopus 로고
    • A simple, continuous fluorometric assay for HIV protease
    • Toth, M. V., and Marshall, G. R. (1990). A simple, continuous fluorometric assay for HIV protease. Int. J. Peptide Protein Res. 36, 544-550.
    • (1990) Int. J. Peptide Protein Res. , vol.36 , pp. 544-550
    • Toth, M.V.1    Marshall, G.R.2
  • 33
    • 0024554259 scopus 로고
    • Inhibition of HIV replication in cell culture by the specific aspartic protease inhibitor pepstatin A
    • von der Helm, K., Gurtler, L., Eberle, J., and Deinhardt, F. (1989). Inhibition of HIV replication in cell culture by the specific aspartic protease inhibitor pepstatin A. FEBS Lett. 247, 349-352.
    • (1989) FEBS Lett. , vol.247 , pp. 349-352
    • Von Der Helm, K.1    Gurtler, L.2    Eberle, J.3    Deinhardt, F.4
  • 35
    • 0025963927 scopus 로고
    • The effect of salt on the Michaelis-Menten constant of the HIV-1 protease correlates with the Hofmeister series
    • Wondrak, E. M., Louis, J. M., and Oroszlan, S. (1991). The effect of salt on the Michaelis-Menten constant of the HIV-1 protease correlates with the Hofmeister series. FEBS Lett. 280, 344-346.
    • (1991) FEBS Lett. , vol.280 , pp. 344-346
    • Wondrak, E.M.1    Louis, J.M.2    Oroszlan, S.3
  • 36
    • 0024969273 scopus 로고
    • Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission
    • Yamamoto, J. K., Hansen, H., Ho, E. W., Morishita, T. Y., Okuda, T., Sawa, T. R., Nakamura, R. M., and Pedersen, N.C. (1989). Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission. J. Am. Vet. Med. Assoc. 194, 213-220.
    • (1989) J. Am. Vet. Med. Assoc. , vol.194 , pp. 213-220
    • Yamamoto, J.K.1    Hansen, H.2    Ho, E.W.3    Morishita, T.Y.4    Okuda, T.5    Sawa, T.R.6    Nakamura, R.M.7    Pedersen, N.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.