메뉴 건너뛰기




Volumn 387, Issue 4, 2006, Pages 477-483

A fluorescence assay for rapid detection of ligand binding affinity to HIV-1 gp41

Author keywords

Fluorescence; Fusion inhibitors; gp41 peptides; High throughput screening; Metal ion ligation

Indexed keywords

FERROUS ION; GLYCOPROTEIN GP 41; PEPTIDE; PROTEIN INHIBITOR; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 33645760751     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2006.063     Document Type: Article
Times cited : (28)

References (18)
  • 2
    • 0034705987 scopus 로고    scopus 로고
    • A virtual library approach to investigate protein folding and internal packing
    • Case, M.A. and McLendon, G.L. (2000). A virtual library approach to investigate protein folding and internal packing. J. Am. Chem. Soc. 122, 8089-8090.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8089-8090
    • Case, M.A.1    McLendon, G.L.2
  • 3
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • USA
    • Chan, D.C., Chutkowski, C.T., and Kim, P.S. (1998). Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA 95, 15613-15617.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 4
    • 0033965256 scopus 로고    scopus 로고
    • HIV-1 gp41, role in HIV entry and prevention
    • Chen, Y.-H., Xiao, Y., and Dierich, M.P. (2000). HIV-1 gp41, role in HIV entry and prevention. Immunobiology 201, 308-316.
    • (2000) Immunobiology , vol.201 , pp. 308-316
    • Chen, Y.-H.1    Xiao, Y.2    Dierich, M.P.3
  • 5
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry, discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D.M., Malashkevich, V.N., Hong, L.H., Carr, P.A., and Kim, P.S. (1999). Inhibiting HIV-1 entry, discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99, 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
  • 6
    • 0037130657 scopus 로고    scopus 로고
    • Structural characterization of a paramagnetic metal-ion-assembled three-stranded α-helical coiled coil
    • Gochin, M., Khorosheva, V., and Case, M.A. (2002). Structural characterization of a paramagnetic metal-ion-assembled three-stranded α-helical coiled coil. J. Am. Chem. Soc. 124, 11018-11028.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11018-11028
    • Gochin, M.1    Khorosheva, V.2    Case, M.A.3
  • 7
    • 0344444157 scopus 로고    scopus 로고
    • A metallopeptide assembly of the HIV-1 gp41 coiled coil is an ideal receptor in fluorescence detection of ligand binding
    • Gochin, M., Guy, R.K., and Case, M.A. (2003). A metallopeptide assembly of the HIV-1 gp41 coiled coil is an ideal receptor in fluorescence detection of ligand binding. Angew. Chem. Int. Ed. 42, 5325-5328.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 5325-5328
    • Gochin, M.1    Guy, R.K.2    Case, M.A.3
  • 8
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang, S., Lin, K., Zhang, L., and Debnath, A.K. (1999). A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 80, 85-96.
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 9
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore, N.R., Salzwedel, K., Reddick, M., Allaway, G.P., and Wild, C.T. (2003). Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virol. 77, 7669-7672.
    • (2003) J. Virol. , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 10
    • 0004040064 scopus 로고    scopus 로고
    • New York/London: Plenum Press
    • nd Edition (New York/London: Plenum Press), pp. 237-265.
    • (1999) nd Edition , pp. 237-265
    • Lakowitz, J.R.1
  • 11
    • 0346729750 scopus 로고    scopus 로고
    • Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides, applicable for identification of HIV-1 fusion inhibitors
    • Liu, S., Zhao, Q., and Jiang, S. (2003). Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides, applicable for identification of HIV-1 fusion inhibitors. Peptides 24, 1303-1313.
    • (2003) Peptides , vol.24 , pp. 1303-1313
    • Liu, S.1    Zhao, Q.2    Jiang, S.3
  • 12
    • 0344494656 scopus 로고    scopus 로고
    • Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan
    • Marme, N., Knemeyer, J.-P., Sauer, M., and Wolfrum, J. (2003). Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan. Bioconjug. Chem. 14, 1133-1139.
    • (2003) Bioconjug. Chem. , vol.14 , pp. 1133-1139
    • Marme, N.1    Knemeyer, J.-P.2    Sauer, M.3    Wolfrum, J.4
  • 13
    • 7044231888 scopus 로고    scopus 로고
    • Conserved residues in the coiled-coil pocket of human immunodeficiency virus type 1 gp41 are essential for viral replication and interhelical interaction
    • Mo, H., Konstantinidis, A.K., Stewart, K.D., Dekhtyar, T., Ng, T., Swift, K., Matayoshi, E.D., Kati, W., Kohlbrenner, W., and Molla, A. (2004). Conserved residues in the coiled-coil pocket of human immunodeficiency virus type 1 gp41 are essential for viral replication and interhelical interaction. Virology 329, 319-327.
    • (2004) Virology , vol.329 , pp. 319-327
    • Mo, H.1    Konstantinidis, A.K.2    Stewart, K.D.3    Dekhtyar, T.4    Ng, T.5    Swift, K.6    Matayoshi, E.D.7    Kati, W.8    Kohlbrenner, W.9    Molla, A.10
  • 14
    • 0031023335 scopus 로고    scopus 로고
    • The crystal structure of the designed trimeric coiled coil coil-VaLd, implications for engineering crystals and supramolecular assemblies
    • Ogihara, N.L., Weiss, M.S., Degrado, W.F., and Eisenberg, D. (1997). The crystal structure of the designed trimeric coiled coil coil-VaLd, implications for engineering crystals and supramolecular assemblies. Protein Sci. 6, 80-88.
    • (1997) Protein Sci. , vol.6 , pp. 80-88
    • Ogihara, N.L.1    Weiss, M.S.2    Degrado, W.F.3    Eisenberg, D.4
  • 16
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • Root, M. and Steger, H. (2004). HIV-1 gp41 as a target for viral entry inhibition. Curr. Pharm. Des. 10, 1805-1825.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1805-1825
    • Root, M.1    Steger, H.2
  • 18
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • USA
    • Wild, C.T., Shugars, D.C., Greenwell, T.K., McDanal, C.B., and Matthews, T.J. (1994). Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91, 9770-9774.
    • (1994) Proc. Natl. Acad. Sci. , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.