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Volumn 135, Issue 3, 2004, Pages 447-453

Blocking of Human Immunodeficiency Virus Type-1 Virion Autolysis by Autologous p2gag Peptide

Author keywords

HIV 1; HIV 1 protease; p2gag peptide; Processing; Suicidal inhibition

Indexed keywords

ALANINE; ALANYLGLUTAMYLALANYLMETHIONYLSERYLGLUTAMINYLVALYLTHREONYLASPARAGINE; ALANYLGLUTAMYLALANYLMETHIONYLSERYLGLUTAMINYLVALYLTHREONYLASPARAGINYLTHREONY LALANYLTHREONYLISOLEUCYLMETHIONINE; AMINO ACID; ASPARAGINE; METHIONINE; MONOCLONAL ANTIBODY; PEPTIDE; STRUCTURAL PROTEIN; THREONINE; UNCLASSIFIED DRUG;

EID: 1942455749     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh052     Document Type: Article
Times cited : (4)

References (29)
  • 4
    • 0028857910 scopus 로고
    • An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivity
    • Konvalinka, J., Litterst, M.A., Welker, R., Kottler, H., Rippmann, F., Heuser, A.M., and Kräusslich, H.G. (1995) An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivity. J. Virol. 69, 7180-7186
    • (1995) J. Virol. , vol.69 , pp. 7180-7186
    • Konvalinka, J.1    Litterst, M.A.2    Welker, R.3    Kottler, H.4    Rippmann, F.5    Heuser, A.M.6    Kräusslich, H.G.7
  • 6
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit, S.C., Moody, M.D., Webbie, R.S., Kaplan, A.H., Nantermet, P.V., Klein, C.A., and Swanstrom, R. (1994) The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J. Virol. 68, 8017-8027
    • (1994) J. Virol. , vol.68 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Webbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6    Swanstrom, R.7
  • 7
    • 0035138477 scopus 로고    scopus 로고
    • Maintenance of the Gag/Gag-Pol Ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity
    • Shehu-Xhilaga, M., Crowe, S.M., and Mak, J. (2001) Maintenance of the Gag/Gag-Pol Ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity. J. Virol. 75, 1834-1841
    • (2001) J. Virol. , vol.75 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crowe, S.M.2    Mak, J.3
  • 8
    • 0034807088 scopus 로고    scopus 로고
    • Evidence as a HIV-1 self-defense vaccine of cyclic chimeric dodecapeptide warped from undecapeptidyl arch of extracellular loop 2 in both CCR5 and CXCR4
    • Misumi, S., Takamune, N., Ido, Y., Hayashi, S., Endo, M., Mukai, R., Tachibana, K., Umeda, M., and Shoji, S. (2001) Evidence as a HIV-1 self-defense vaccine of cyclic chimeric dodecapeptide warped from undecapeptidyl arch of extracellular loop 2 in both CCR5 and CXCR4. Biochem. Biophys. Res. Commun. 285, 1309-1316
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 1309-1316
    • Misumi, S.1    Takamune, N.2    Ido, Y.3    Hayashi, S.4    Endo, M.5    Mukai, R.6    Tachibana, K.7    Umeda, M.8    Shoji, S.9
  • 11
    • 0023870815 scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • Jacks, T., Power, M.D., Masiarz, F.R., Luciw, P.A., Barr, P.J., and Varmus, H.E. (1988) Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 331, 280-283
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3    Luciw, P.A.4    Barr, P.J.5    Varmus, H.E.6
  • 12
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers, K., Rutter, G., Kottler, H., Tessmer, U., Hohenberg, H., and Krausslich, H.G. (1998) Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72, 2846-2854
    • (1998) J. Virol. , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.G.6
  • 13
    • 17444392445 scopus 로고    scopus 로고
    • Auto-processing of HIV-1 protease is tightly coupled to protein folding
    • Louis, J.M., Clore, G.M., and Gronenborn, A.M. (1999) Auto-processing of HIV-1 protease is tightly coupled to protein folding. Nat. Struct. Biol. 6, 868-875
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 868-875
    • Louis, J.M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 14
    • 0033618280 scopus 로고    scopus 로고
    • Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein
    • Paulus, C., Hellebrand, S., Tessmer, U., Wolf, H., Kräusslich, H.G., and Wagner, R. (1999) Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein. J. Biol. Chem. 274, 21539-21543
    • (1999) J. Biol. Chem. , vol.274 , pp. 21539-21543
    • Paulus, C.1    Hellebrand, S.2    Tessmer, U.3    Wolf, H.4    Kräusslich, H.G.5    Wagner, R.6
  • 15
    • 0029417217 scopus 로고
    • In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes
    • Lindhofer, H., von der Helm, K., and Nitschko, H. (1995) In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes. Virology 214, 624-627
    • (1995) Virology , vol.214 , pp. 624-627
    • Lindhofer, H.1    Von Der Helm, K.2    Nitschko, H.3
  • 17
    • 0034856077 scopus 로고    scopus 로고
    • Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation
    • Shehu-Xhilaga, M., Kraeusslich, H.G., Pettit, S., Swanstrom, R., Lee, J.Y., Marshall, J.A., Crowe, S.M., and Mak, J. (2001) Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation. J. Virol. 75, 9156-9164
    • (2001) J. Virol. , vol.75 , pp. 9156-9164
    • Shehu-Xhilaga, M.1    Kraeusslich, H.G.2    Pettit, S.3    Swanstrom, R.4    Lee, J.Y.5    Marshall, J.A.6    Crowe, S.M.7    Mak, J.8
  • 18
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D., Joliot, A.H., Chassaing, G., and Prochiantz, A. (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269, 10444-10450
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 19
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi, D., Chassaing, G., and Prochiantz, A. (1998) Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 8, 84-87
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 20
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G., and Prochiantz, A. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271, 18188-18193
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 22
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S., Suzuki, T., Ohashi, W., Yagami, T., Tanaka, S., Ueda, K., and Sugiura, Y. (2001) Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 5836-5840
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 23
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Lin, Y.Z., Yao, S., Veach, R.A., Torgerson, T.R. and Hawiger, J. (1995) Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 270, 14255-14258
    • (1995) J. Biol. Chem. , vol.270 , pp. 14255-14258
    • Lin, Y.Z.1    Yao, S.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 25
    • 0031959657 scopus 로고    scopus 로고
    • Genetic engineering of proteins with cell membrane permeability
    • Rojas, M., Donahue, J.P., Tan, Z., and Lin, Y.Z. (1998) Genetic engineering of proteins with cell membrane permeability. Nat. Biotechnol. 16, 370-375
    • (1998) Nat. Biotechnol. , vol.16 , pp. 370-375
    • Rojas, M.1    Donahue, J.P.2    Tan, Z.3    Lin, Y.Z.4
  • 26
    • 0029861248 scopus 로고    scopus 로고
    • Controlling epidermal growth factor (EGF)-stimulated Ras activation in intact cells by a cell-permeable peptide mimicking phosphorylated EGF receptor
    • Rojas, M., Yao, S., and Lin, Y.Z. (1996) Controlling epidermal growth factor (EGF)-stimulated Ras activation in intact cells by a cell-permeable peptide mimicking phosphorylated EGF receptor. J. Biol. Chem. 271, 27456-27461
    • (1996) J. Biol. Chem. , vol.271 , pp. 27456-27461
    • Rojas, M.1    Yao, S.2    Lin, Y.Z.3
  • 27
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze, S.R., Ho, A., Vocero-Akbani, A., and Dowdy, S.F. (1999) In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285, 1569-1572
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 28
    • 0034141430 scopus 로고    scopus 로고
    • In vivo protein transduction: Intracellular delivery of biologically active proteins, compounds and DNA
    • chwarze, S.R. and Dowdy, S.F. (2000) In vivo protein transduction: intracellular delivery of biologically active proteins, compounds and DNA. Trends Pharmacol. Sci. 21, 45-48
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 45-48
    • Schwarze, S.R.1    Dowdy, S.F.2
  • 29
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives, E., Brodin, P., and Lebleu, B. (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16010-16017
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.