메뉴 건너뛰기




Volumn 44, Issue 15, 2005, Pages 5853-5861

The role of the N-terminal heptad repeat of HIV-1 in the actual lipid mixing step as revealed by its substitution with distant coiled coils

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; DISEASES; LIPIDS; OLIGOMERS; POLYPEPTIDES; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 17144397565     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047666g     Document Type: Article
Times cited : (21)

References (61)
  • 1
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. (1992) Membrane fusion, Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 2
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L. V., and Kozlov, M. M. (2003) Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 72, 175-207.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 3
    • 0035955695 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer
    • Zhang, C. W., Chishti, Y., Hussey, R. E., and Reinherz, E. L. (2001) Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer, J. Biol. Chem. 276, 39577-39585.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39577-39585
    • Zhang, C.W.1    Chishti, Y.2    Hussey, R.E.3    Reinherz, E.L.4
  • 4
    • 0036317971 scopus 로고    scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface
    • Center, R. J., Leapman, R. D., Lebowitz, J., Arthur, L. O., Earl, P. L., and Moss, B. (2002) Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface, J. Virol. 76, 7863-7867.
    • (2002) J. Virol. , vol.76 , pp. 7863-7867
    • Center, R.J.1    Leapman, R.D.2    Lebowitz, J.3    Arthur, L.O.4    Earl, P.L.5    Moss, B.6
  • 5
    • 0036329849 scopus 로고    scopus 로고
    • Cell surface receptors, virus entry and tropism of primate lentiviruses
    • Clapham, P. R., and McKnight, A. (2002) Cell surface receptors, virus entry and tropism of primate lentiviruses, J. Gen. Virol. 83, 1809-1829.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1809-1829
    • Clapham, P.R.1    McKnight, A.2
  • 6
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and Kim, P. S. (1998) HIV entry and its inhibition, Cell 93, 681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 7
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat
    • Delwart, E. L., Mosialos, G., and Gilmore, T. (1990) Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat, AIDS Res. Hum. Retroviruses 6, 703-706.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 8
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., Dubay, J. W., Greenwell, T., Baird, T., Jr., Oas, T. G., McDanal, C., Hunter, E., and Matthews, T. (1994) Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex, Proc. Natl. Acad. Sci. U.S.A. 91, 12676-12680.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 9
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H., Johnson, P. F., and McKnight, S. L. (1988) The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins, Science 240, 1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 10
    • 0001248650 scopus 로고
    • α-Helical coiled coils - A widespread motif in proteins
    • Cohen, C., and Parry, D. A. D. (1986) α-Helical coiled coils - a widespread motif in proteins, TIBS 11, 245-248.
    • (1986) TIBS , vol.11 , pp. 245-248
    • Cohen, C.1    Parry, D.A.D.2
  • 12
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition, Annu. Rev. Biochem. 70, 777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 13
    • 0035839477 scopus 로고    scopus 로고
    • Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes
    • Dimitrov, A. S., Xiao, X., Dimitrov, D. S., and Blumenthal, R. (2001) Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes, J. Biol. Chem. 276, 30335-30341.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30335-30341
    • Dimitrov, A.S.1    Xiao, X.2    Dimitrov, D.S.3    Blumenthal, R.4
  • 14
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors
    • Jones, P. L., Korte, T., and Blumenthal, R. (1998) Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors, J. Biol. Chem. 273, 404-409.
    • (1998) J. Biol. Chem. , vol.273 , pp. 404-409
    • Jones, P.L.1    Korte, T.2    Blumenthal, R.3
  • 16
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., Wild, C. T., Weng, Y., and Weiss, C. D. (1998) Capture of an early fusion-active conformation of HIV-1 gp41, Nat. Struct. Biol. 5, 276-279.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 17
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., Markosyan, R. M., Hemmati, H., Delmedico, M. K., Lambert, D. M., and Cohen, F. S. (2000) Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion, J. Cell. Biol. 151, 413-423.
    • (2000) J. Cell. Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 18
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell, S. R., Martin, I., Ruysschaert, J. M., Shai, Y., and Blumenthal, R. (1997) What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review), Mol. Membr. Biol. 14, 97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.M.3    Shai, Y.4    Blumenthal, R.5
  • 19
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M., and Lawrence, M. C. (2003) The structural biology of type I viral membrane fusion, Nat. Rev. Mol. Cell. Biol. 4, 309-319.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 21
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997) Core structure of gp41 from the HIV envelope glycoprotein, Cell 89, 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 22
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso, I., Durell, S., Sakaguchi, K., Appella, E., and Blumenthal, R. (1998) Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41, J. Cell. Biol. 140, 315-323.
    • (1998) J. Cell. Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 23
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 Envelope Proteins Complete Their Folding into Six-helix Bundles Immediately after Fusion Pore Formation
    • Markosyan, R. M., Cohen, F. S., and Melikyan, G. B. (2003) HIV-1 Envelope Proteins Complete Their Folding into Six-helix Bundles Immediately after Fusion Pore Formation, Mol. Biol. Cell. 14, 926-938.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 24
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., Delwart, E. L., Buchschacher, G. L., Jr., and Panganiban, A. T. (1992) A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity, Proc. Natl. Acad. Sci. U.S.A. 89, 70-74.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher Jr., G.L.3    Panganiban, A.T.4
  • 25
    • 0033621026 scopus 로고    scopus 로고
    • Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes
    • Pritsker, M., Rucker, J., Hoffman, T. L., Doms, R. W., and Shai, Y. (1999) Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes, Biochemistry 38, 11359-11371.
    • (1999) Biochemistry , vol.38 , pp. 11359-11371
    • Pritsker, M.1    Rucker, J.2    Hoffman, T.L.3    Doms, R.W.4    Shai, Y.5
  • 26
    • 0031010455 scopus 로고    scopus 로고
    • Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study
    • Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R., and Shai, Y. (1997) Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study, J. Biol. Chem. 272, 13496-13505.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13496-13505
    • Kliger, Y.1    Aharoni, A.2    Rapaport, D.3    Jones, P.4    Blumenthal, R.5    Shai, Y.6
  • 27
    • 0028934164 scopus 로고
    • Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution
    • Pereira, F. B., Goni, F. M., and Nieva, J. L. (1995) Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution, FEBS Lett. 362, 243-246.
    • (1995) FEBS Lett. , vol.362 , pp. 243-246
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 28
    • 0037379448 scopus 로고    scopus 로고
    • Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides
    • Yang, R., Yang, J., and Weliky, D. P. (2003) Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides, Biochemistry 42, 3527-3535.
    • (2003) Biochemistry , vol.42 , pp. 3527-3535
    • Yang, R.1    Yang, J.2    Weliky, D.P.3
  • 29
    • 0346057944 scopus 로고    scopus 로고
    • Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization
    • Lau, W. L., Ege, D. S., Lear, J. D., Hammer, D. A., and DeGrado, W. F. (2004) Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization, Biophys. J. 86, 272-284.
    • (2004) Biophys. J. , vol.86 , pp. 272-284
    • Lau, W.L.1    Ege, D.S.2    Lear, J.D.3    Hammer, D.A.4    DeGrado, W.F.5
  • 30
    • 0037046147 scopus 로고    scopus 로고
    • The HIV-1 gp41 N-terminal heptad repeat plays an essential role in membrane fusion
    • Sackett, K., and Shai, Y. (2002) The HIV-1 gp41 N-terminal heptad repeat plays an essential role in membrane fusion, Biochemistry 41, 4678-4685.
    • (2002) Biochemistry , vol.41 , pp. 4678-4685
    • Sackett, K.1    Shai, Y.2
  • 31
    • 0033551053 scopus 로고    scopus 로고
    • Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins
    • Kobe, B., Center, R. J., Kemp, B. E., and Poumbourios, P. (1999) Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins, Proc. Natl. Acad. Sci. U.S.A. 96, 4319-4324.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4319-4324
    • Kobe, B.1    Center, R.J.2    Kemp, B.E.3    Poumbourios, P.4
  • 32
    • 0035902564 scopus 로고    scopus 로고
    • The trimer-of-hairpins motif in membrane fusion: Visna virus
    • Malashkevich, V. N., Singh, M., and Kim, P. S. (2001) The trimer-of-hairpins motif in membrane fusion: Visna virus, Proc. Natl. Acad. Sci. U.S.A. 98, 8502-8506.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8502-8506
    • Malashkevich, V.N.1    Singh, M.2    Kim, P.S.3
  • 33
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao, X., Singh, M., Malashkevich, V. N., and Kim, P. S. (2000) Structural characterization of the human respiratory syncytial virus fusion protein core, Proc. Natl. Acad. Sci. U.S.A. 97, 14172-14177.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 34
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn, W., Carfi, A., Lee, K. H., Skehel, J. J., and Wiley, D. C. (1998) Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain, Mol. Cell 2, 605-616.
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 35
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P. B., Zhang, T., Kim, P. S., and Alber, T. (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants, Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 36
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin A (1-33)
    • Merrifield, R. B., Vizioli, L. D., and Boman, H. G. (1982) Synthesis of the antibacterial peptide cecropin A (1-33), Biochemistry 21, 5020-5031.
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Vizioli, L.D.2    Boman, H.G.3
  • 37
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai, Y., Bach, D., and Yanovsky, A. (1990) Channel formation properties of synthetic pardaxin and analogues, J. Biol. Chem. 265, 20202-20209.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 38
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng, T. M., Griffin, J. H., and Dawson, P. E. (1999) Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology, Proc. Natl. Acad. Sci. U.S.A. 96, 10068-10073.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 39
    • 0036317785 scopus 로고    scopus 로고
    • Comparison of predicted scaffold-compatible sequence variation in the triple-hairpin structure of human imunodeficiency virus type 1 gp41 with patient data
    • Boutonnet, N., Janssens, W., Boutton, C., Verscheide, J. L., Heyndrickx, L., Beirnaert, E., van der Groen, G., and Lasters, I. (2002) Comparison of predicted scaffold-compatible sequence variation in the triple-hairpin structure of human imunodeficiency virus type 1 gp41 with patient data, J. Virol. 76, 7595-7606.
    • (2002) J. Virol. , vol.76 , pp. 7595-7606
    • Boutonnet, N.1    Janssens, W.2    Boutton, C.3    Verscheide, J.L.4    Heyndrickx, L.5    Beirnaert, E.6    Van Der Groen, G.7    Lasters, I.8
  • 40
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans, T. C., Jr., Benner, J., and Xu, M. Q. (1998) Semisynthesis of cytotoxic proteins using a modified protein splicing element, Protein Sci. 7, 2256-2264.
    • (1998) Protein Sci. , vol.7 , pp. 2256-2264
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.Q.3
  • 41
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • Gazit, E., Miller, I. R., Biggin, P. C., Sansom, M. S., and Shai, Y. (1996) Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes, J. Mol. Biol. 258, 860-870.
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.4    Shai, Y.5
  • 42
    • 0034700998 scopus 로고    scopus 로고
    • The polar region consecutive to the HIV fusion peptide participates in membrane fusion
    • Peisajovich, S. G., Epand, R. F., Pritsker, M., Shai, Y., and Epand, R. M. (2000) The polar region consecutive to the HIV fusion peptide participates in membrane fusion, Biochemistry 39, 1826-1833.
    • (2000) Biochemistry , vol.39 , pp. 1826-1833
    • Peisajovich, S.G.1    Epand, R.F.2    Pritsker, M.3    Shai, Y.4    Epand, R.M.5
  • 43
    • 0036071621 scopus 로고    scopus 로고
    • A structure for the trimeric MHC class II-associated invariant chain transmembrane domain
    • Kukol, A., Torres, J., and Arkin, I. T. (2002) A structure for the trimeric MHC class II-associated invariant chain transmembrane domain, J. Mol. Biol. 320, 1109-1117.
    • (2002) J. Mol. Biol. , vol.320 , pp. 1109-1117
    • Kukol, A.1    Torres, J.2    Arkin, I.T.3
  • 44
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 45
    • 0027953945 scopus 로고
    • Mode of action of the antibacterial cecropin B2: A spectrofluorometric study
    • Gazit, E., Lee, W. J., Brey, P. T., and Shai, Y. (1994) Mode of action of the antibacterial cecropin B2: a spectrofluorometric study, Biochemistry 33, 10681-10692.
    • (1994) Biochemistry , vol.33 , pp. 10681-10692
    • Gazit, E.1    Lee, W.J.2    Brey, P.T.3    Shai, Y.4
  • 46
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion, Biochemistry 20, 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 47
    • 0035795730 scopus 로고    scopus 로고
    • Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance
    • Mozsolits, H., Wirth, H. J., Werkmeister, J., and Aguilar, M. I. (2001) Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance, Biochim. Biophys. Acta 1512, 64-76.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 64-76
    • Mozsolits, H.1    Wirth, H.J.2    Werkmeister, J.3    Aguilar, M.I.4
  • 48
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides
    • Papo, N., and Shai, Y. (2003) Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides, Biochemistry 42, 458-466.
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 49
    • 0141457555 scopus 로고    scopus 로고
    • How structure correlates to function for membrane associated HIV-1 gp41 constructs corresponding to the N-terminal half of the ectodomain
    • Sackett, K., and Shai, Y. (2003) How structure correlates to function for membrane associated HIV-1 gp41 constructs corresponding to the N-terminal half of the ectodomain, J. Mol. Biol. 333, 47-58.
    • (2003) J. Mol. Biol. , vol.333 , pp. 47-58
    • Sackett, K.1    Shai, Y.2
  • 50
    • 0035210771 scopus 로고    scopus 로고
    • Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate
    • Meng, F. G., Zeng, X., Hong, Y. K., and Zhou, H. M. (2001) Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate, Biochimie 83, 953-956.
    • (2001) Biochimie , vol.83 , pp. 953-956
    • Meng, F.G.1    Zeng, X.2    Hong, Y.K.3    Zhou, H.M.4
  • 51
    • 0026795513 scopus 로고
    • Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils
    • Zhou, N. E., Kay, C. M., and Hodges, R. S. (1992) Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils, J. Biol. Chem. 267, 2664-2670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 52
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils
    • Lau, S. Y., Taneja, A. K., and Hodges, R. S. (1984) Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils, J. Biol. Chem. 259, 13253-13261.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.1    Taneja, A.K.2    Hodges, R.S.3
  • 53
    • 0034628898 scopus 로고    scopus 로고
    • Paramyxovirus F1 Protein Has Two Fusion Peptides: Implications for the Mechanism of Membrane Fusion
    • Peisajovich, S. G., Samuel, O., and Shai, Y. (2000) Paramyxovirus F1 Protein Has Two Fusion Peptides: Implications for the Mechanism of Membrane Fusion, J. Mol. Biol. 296, 1353-1365.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1353-1365
    • Peisajovich, S.G.1    Samuel, O.2    Shai, Y.3
  • 54
    • 0035814820 scopus 로고    scopus 로고
    • Participation of Two Fusion Peptides in Measles Virus-Induced Membrane Fusion: Emerging Similarity with Other Paramyxoviruses
    • Samuel, O., and Shai, Y. (2001) Participation of Two Fusion Peptides in Measles Virus-Induced Membrane Fusion: Emerging Similarity with Other Paramyxoviruses, Biochemistry 40, 1340-1349.
    • (2001) Biochemistry , vol.40 , pp. 1340-1349
    • Samuel, O.1    Shai, Y.2
  • 55
    • 0034714156 scopus 로고    scopus 로고
    • Membrane-induced Conformational Change during the Activation of HIV-1 gp41
    • Kliger, Y., Peisajovich, S. G., Blumenthal, R., and Shai, Y. (2000) Membrane-induced Conformational Change During the Activation of HIV-1 gp41, J. Mol. Biol. 301, 905-914.
    • (2000) J. Mol. Biol. , vol.301 , pp. 905-914
    • Kliger, Y.1    Peisajovich, S.G.2    Blumenthal, R.3    Shai, Y.4
  • 56
    • 0039182128 scopus 로고    scopus 로고
    • FTIR-Spectroscopy of multistranded coiled coil proteins
    • Heimburg, T., Schunemann, J., Weber, K., and Geisler, N. (1999) FTIR-Spectroscopy of multistranded coiled coil proteins, Biochemistry 38, 12727-12734.
    • (1999) Biochemistry , vol.38 , pp. 12727-12734
    • Heimburg, T.1    Schunemann, J.2    Weber, K.3    Geisler, N.4
  • 57
    • 2442559243 scopus 로고    scopus 로고
    • The C- and the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively
    • Shnaper, S., Sackett, K., Gallo, S. A., Blumenthal, R., and Shai, Y. (2004) The C- and the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively, J. Biol. Chem. 279, 18526-18534.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18526-18534
    • Shnaper, S.1    Sackett, K.2    Gallo, S.A.3    Blumenthal, R.4    Shai, Y.5
  • 58
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher, W. R. (1987) Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus, Cell 50, 327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 59
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport, D., Ovadia, M., and Shai, Y. (1995) A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses, EMBO J. 14, 5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 60
    • 0029964418 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • Shugars, D. C., Wild, C. T., Greenwell, T. K., and Matthews, T. J. (1996) Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41, J. Virol. 70, 2982-2991.
    • (1996) J. Virol. , vol.70 , pp. 2982-2991
    • Shugars, D.C.1    Wild, C.T.2    Greenwell, T.K.3    Matthews, T.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.