메뉴 건너뛰기




Volumn 332, Issue 3, 2005, Pages 831-836

Rational design of highly potent HIV-1 fusion inhibitory proteins: Implication for developing antiviral therapeutics

Author keywords

gp41; Heptad repeat regions; HIV 1 fusion inhibitors; Protein inhibitors

Indexed keywords

ANTIVIRUS AGENT; HUMAN IMMUNODEFICIENCY VIRUS 1 FUSION INHIBITORY PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; PROTEIN HR 212; PROTEIN HR121; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 19744363341     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.05.037     Document Type: Article
Times cited : (22)

References (19)
  • 1
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • E.O. Freed, and M.A. Martin The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection J. Biol. Chem. 270 1995 23883 23886
    • (1995) J. Biol. Chem. , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 2
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • D.M. Eckert, and P.S. Kim Mechanisms of viral membrane fusion and its inhibition Annu. Rev. Biochem. 70 2001 777 810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 3
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • M. Lu, and P.S. Kim A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein J. Biomol. Struct. Dyn. 15 1997 465 471
    • (1997) J. Biomol. Struct. Dyn. , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 5
    • 0034645796 scopus 로고    scopus 로고
    • Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation
    • Y. Kliger, and Y. Shai Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation J. Mol. Biol. 295 2000 163 168
    • (2000) J. Mol. Biol. , vol.295 , pp. 163-168
    • Kliger, Y.1    Shai, Y.2
  • 7
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • C.T. Wild, D.C. Shugars, T.K. Greenwell, C.B. McDanal, and T.J. Matthews Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection Proc. Natl. Acad. Sci. USA 91 1994 9770 9774
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 8
    • 0032899254 scopus 로고    scopus 로고
    • Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: Implications for viral membrane fusion
    • M. Lu, H. Ji, and S. Shen Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion J. Virol. 73 1999 4433 4438
    • (1999) J. Virol. , vol.73 , pp. 4433-4438
    • Lu, M.1    Ji, H.2    Shen, S.3
  • 9
    • 0036926562 scopus 로고    scopus 로고
    • The fusion protein core of measles virus forms stable coiled-coil trimer
    • J. Zhu, C.W. Zhang, Y. Qi, P. Tien, and G.F. Gao The fusion protein core of measles virus forms stable coiled-coil trimer Biochem. Biophys. Res. Commun. 299 2002 897 902
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 897-902
    • Zhu, J.1    Zhang, C.W.2    Qi, Y.3    Tien, P.4    Gao, G.F.5
  • 10
    • 0345701489 scopus 로고    scopus 로고
    • Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion
    • E. Wang, X. Sun, Y. Qian, L. Zhao, P. Tien, and G.F. Gao Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion Biochem. Biophys. Res. Commun. 302 2003 469 475
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 469-475
    • Wang, E.1    Sun, X.2    Qian, Y.3    Zhao, L.4    Tien, P.5    Gao, G.F.6
  • 12
    • 9444292849 scopus 로고    scopus 로고
    • Enfuvirtide: A new class of antiretroviral therapy for HIV infection
    • J.C. Leao, C. Frezzini, and S. Porter Enfuvirtide: a new class of antiretroviral therapy for HIV infection Oral Dis. 10 2004 327 329
    • (2004) Oral Dis. , vol.10 , pp. 327-329
    • Leao, J.C.1    Frezzini, C.2    Porter, S.3
  • 13
    • 0031798443 scopus 로고    scopus 로고
    • Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41
    • Y. Weng, and C.D. Weiss Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41 J. Virol. 72 1998 9676 9682
    • (1998) J. Virol. , vol.72 , pp. 9676-9682
    • Weng, Y.1    Weiss, C.D.2
  • 14
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • M.J. Root, M.S. Kay, and P.S. Kim Protein design of an HIV-1 entry inhibitor Science 291 2001 884 888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 15
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • M. Lu, S.C. Blacklow, and P.S. Kim A trimeric structural domain of the HIV-1 transmembrane glycoprotein Nat. Struct. Biol. 2 1995 1075 1082
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 16
    • 0035800816 scopus 로고    scopus 로고
    • Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • J.M. Louis, C.A. Bewley, and G.M. Clore Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity J. Biol. Chem. 276 2001 29485 29489
    • (2001) J. Biol. Chem. , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 17
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • D.M. Eckert, V.N. Malashkevich, L.H. Hong, P.A. Carr, and P.S. Kim Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket Cell 99 1999 103 115
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 18
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • D.M. Eckert, and P.S. Kim Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region Proc. Natl. Acad. Sci. USA 98 2001 11187 11192
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 19
    • 15444363201 scopus 로고    scopus 로고
    • Design of recombinant protein-based SARS-CoV entry inhibitors targeting the heptad-repeat regions of the spike protein S2 domain
    • L. Ni, J. Zhu, J. Zhang, M. Yan, G.F. Gao, and P. Tien Design of recombinant protein-based SARS-CoV entry inhibitors targeting the heptad-repeat regions of the spike protein S2 domain Biochem. Biophys. Res. Commun. 330 2005 39 45
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 39-45
    • Ni, L.1    Zhu, J.2    Zhang, J.3    Yan, M.4    Gao, G.F.5    Tien, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.