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Volumn 26, Issue 11, 2012, Pages 4628-4636

Sphingopeptides: Dihydrosphingosine-based fusion inhibitors against wild-type and enfuvirtide-resistant HIV-1

Author keywords

Sphingolipids; Viral envelope protein

Indexed keywords

ANTIRETROVIRUS AGENT; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; CHOLESTEROL; ENFUVIRTIDE; FATTY ACID; SPHINGANINE N17; SPHINGOSINE; SPHINGOSINE C16 N17; TOCOPHEROL; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 84868297922     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-215111     Document Type: Article
Times cited : (35)

References (56)
  • 1
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. M. (1990) Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52, 675-697
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 3
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen, D. H., and Hildreth, J. E. (2000) Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 74, 3264-3272
    • (2000) J. Virol. , vol.74
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 4
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in hiv-1 assembly and release
    • Ono, A., and Freed, E. O. (2001) Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. U. S. A. 98, 13925-13930
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 6
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipidbinding domain in alzheimer, prion, and hiv-1 proteins
    • Mahfoud, R., Garmy, N., Maresca, M., Yahi, N., Puigserver, A., and Fantini, J. (2002) Identification of a common sphingolipidbinding domain in Alzheimer, prion, and HIV-1 proteins. J. Biol. Chem. 277, 11292-11296
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 7
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda, M., Leser, G. P., Russell, C. J., and Lamb, R. A. (2003) Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. U. S. A. 100, 14610-14617
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 8
    • 22544463108 scopus 로고    scopus 로고
    • Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release
    • Choi, K. S., Aizaki, H., and Lai, M. M. (2005) Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release. J. Virol. 79, 9862-9871
    • (2005) J. Virol. , Issue.79 , pp. 9862-9871
    • Choi, K.S.1    Aizaki, H.2    Lai, M.M.3
  • 9
    • 43949122204 scopus 로고    scopus 로고
    • West nile virus entry requires cholesterol-rich membrane microdomains and is independent of V 3 integrin
    • Medigeshi, G. R., Hirsch, A. J., Streblow, D. N., Nikolich-Zugich, J., and Nelson, J. A. (2008) West Nile virus entry requires cholesterol-rich membrane microdomains and is independent of v 3 integrin. J. Virol. 82, 5212-5219
    • (2008) J. Virol. , vol.82 , pp. 5212-5219
    • Medigeshi, G.R.1    Hirsch, A.J.2    Streblow, D.N.3    Nikolich-Zugich, J.4    Nelson, J.A.5
  • 11
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387, 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 12
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons, K., and Gerl, M. J. (2010) Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 11, 688-699
    • (2010) Nat. Rev. Mol. Cell Biol. , Issue.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 13
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as hiv-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger, E. A., Murphy, P. M., and Farber, J. M. (1999) Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17, 657-700
    • (1999) Annu. Rev. Immunol. , Issue.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 14
    • 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
  • 16
    • 42049118274 scopus 로고    scopus 로고
    • The function of coreceptor as a basis for the kinetic dissection of hiv type 1 envelope protein-mediated cell fusion
    • Chien, M. P., Jiang, S., and Chang, D. K. (2008) The function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope protein-mediated cell fusion. FASEB J. 22, 1179-1192
    • (2008) FASEB J. , vol.22 , pp. 1179-1192
    • Chien, M.P.1    Jiang, S.2    Chang, D.K.3
  • 17
    • 77749329921 scopus 로고    scopus 로고
    • Topological layers in the hiv-1 gp120 inner domain regulate gp41 interaction and cd4-triggered conformational transitions
    • Finzi, A., Xiang, S. H., Pacheco, B., Wang, L., Haight, J., Kassa, A., Danek, B., Pancera, M., Kwong, P. D., and Sodroski, J. (2010) Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol. Cell 37, 656-667
    • (2010) Mol. Cell , vol.37 , pp. 656-667
    • Finzi, A.1    Xiang, S.H.2    Pacheco, B.3    Wang, L.4    Haight, J.5    Kassa, A.6    Danek, B.7    Pancera, M.8    Kwong, P.D.9    Sodroski, J.10
  • 19
    • 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. , Issue.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 20
    • 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
  • 21
    • 33645230933 scopus 로고    scopus 로고
    • Membrane-Anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion
    • Melikyan, G. B., Egelhofer, M., and von Laer, D. (2006) Membrane-Anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion. J. Virol. 80, 3249-3258
    • (2006) J. Virol , vol.80 , pp. 3249-3258
    • Melikyan, G.B.1    Egelhofer, M.2    Von Laer, D.3
  • 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
    • 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. , Issue.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 24
    • 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
  • 26
    • 3142510881 scopus 로고    scopus 로고
    • Intracellular and viral membrane fusion: A uniting mechanism
    • Sollner, T. H. (2004) Intracellular and viral membrane fusion: a uniting mechanism. Curr. Opin. Cell Biol. 16, 429-435
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 429-435
    • Sollner, T.H.1
  • 27
    • 33845346790 scopus 로고    scopus 로고
    • Biophysics of sphingolipids i. Membrane properties of sphingosine, ceramides and other simple sphingolipids
    • Goni, F. M., and Alonso, A. (2006) Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids. Biochim. Biophys. Acta 1758, 1902-1921
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1902-1921
    • Goni, F.M.1    Alonso, A.2
  • 28
    • 20444363393 scopus 로고    scopus 로고
    • The ins and outs of sphingolipid synthesis
    • Futerman, A. H., and Riezman, H. (2005) The ins and outs of sphingolipid synthesis. Trends Cell Biol. 15, 312-318
    • (2005) Trends Cell Biol. , vol.15 , pp. 312-318
    • Futerman, A.H.1    Riezman, H.2
  • 29
    • 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
  • 30
    • 78649829342 scopus 로고    scopus 로고
    • Virus-cell and cell-cell fusion mediated by the hiv-1 envelope glycoprotein is inhibited by short gp41 n-terminal membrane-Anchored peptides lacking the critical pocket domain
    • Wexler-Cohen, Y., Ashkenazi, A., Viard, M., Blumenthal, R., and Shai, Y. (2010) Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-Anchored peptides lacking the critical pocket domain. FASEB J. 24, 4196-4202
    • (2010) FASEB J. , Issue.24 , pp. 4196-4202
    • Wexler-Cohen, Y.1    Ashkenazi, A.2    Viard, M.3    Blumenthal, R.4    Shai, Y.5
  • 31
    • 34447121955 scopus 로고    scopus 로고
    • Site-specific mutations in hiv-1 gp41 reveal a correlation between hiv-1-mediated bystander apoptosis and fusion/hemifusion
    • Garg, H., Joshi, A., Freed, E. O., and Blumenthal, R. (2007) Site-specific mutations in HIV-1 gp41 reveal a correlation between HIV-1-mediated bystander apoptosis and fusion/hemifusion. J. Biol. Chem. 282, 16899-16906
    • (2007) J. Biol. Chem. , vol.282 , pp. 16899-16906
    • Garg, H.1    Joshi, A.2    Freed, E.O.3    Blumenthal, R.4
  • 32
    • 35348957822 scopus 로고    scopus 로고
    • Fatty acids can substitute the hiv fusion peptide in lipid merging and fusion: An analogy between viral and palmitoylated eukaryotic fusion proteins
    • Lev, N., and Shai, Y. (2007) Fatty acids can substitute the HIV fusion peptide in lipid merging and fusion: an analogy between viral and palmitoylated eukaryotic fusion proteins. J. Mol. Biol. 374, 220-230
    • (2007) J. Mol. Biol. , vol.374 , pp. 220-230
    • Lev, N.1    Shai, Y.2
  • 33
    • 0034142044 scopus 로고    scopus 로고
    • Androctonin, a hydrophilic disulphide-bridged nonhaemolytic anti-microbial peptide: A plausible mode of action
    • Hetru, C., Letellier, L., Oren, Z., Hoffmann, J. A., and Shai, Y. (2000) Androctonin, a hydrophilic disulphide-bridged nonhaemolytic anti-microbial peptide: a plausible mode of action. Biochem. J. 345(Pt. 3), 653-664
    • (2000) Biochem. J. , vol.345 , Issue.PART. 3 , pp. 653-664
    • Hetru, C.1    Letellier, L.2    Oren, Z.3    Hoffmann, J.A.4    Shai, Y.5
  • 34
    • 0027394475 scopus 로고
    • Spectroscopic and functional characterization of the putative transmembrane segment of the mink potassium channel
    • Ben-Efraim, I., Bach, D., and Shai, Y. (1993) Spectroscopic and functional characterization of the putative transmembrane segment of the minK potassium channel. Biochemistry 32, 2371-2377
    • (1993) Biochemistry , vol.32 , pp. 2371-2377
    • Ben-Efraim, I.1    Bach, D.2    Shai, Y.3
  • 35
    • 35348926466 scopus 로고    scopus 로고
    • Amino acid conservation in the gp41 transmembrane protein and natural polymorphisms associated with enfuvirtide resistance across hiv-1 variants
    • Holguin, A., De Arellano, E. R., and Soriano, V. (2007) Amino acid conservation in the gp41 transmembrane protein and natural polymorphisms associated with enfuvirtide resistance across HIV-1 variants. AIDS Res. Hum. Retroviruses 23, 1067-1074
    • (2007) AIDS Res. Hum. Retroviruses , vol.23 , pp. 1067-1074
    • Holguin, A.1    De Arellano, E.R.2    Soriano, V.3
  • 36
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of hiv type 1 gp41 is an attractive drug target
    • 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. U. S. A. 95, 15613-15617
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 37
    • 70049117718 scopus 로고    scopus 로고
    • Membrane-Anchored hiv-1 n-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action
    • Wexler-Cohen, Y., and Shai, Y. (2009) Membrane-Anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action. PLoS Pathog. 5, e1000509
    • (2009) PLoS Pathog. , vol.5
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 38
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of hiv-1 entry from the gp41 n-peptide region
    • Eckert, D. M., and Kim, P. S. (2001) Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc. Natl. Acad. Sci. U. S. A. 98, 11187-11192
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 39
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of hiv fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley, C. A., Louis, J. M., Ghirlando, R., and Clore, G. M. (2002) Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277, 14238-14245
    • (2002) J. Biol. Chem. , Issue.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 40
    • 7644236011 scopus 로고    scopus 로고
    • Emergence of a drugdependent human immunodeficiency virus type 1 variant during therapy with the t20 fusion inhibitor
    • Baldwin, C. E., Sanders, R. W., Deng, Y., Jurriaans, S., Lange, J. M., Lu, M., and Berkhout, B. (2004) Emergence of a drugdependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor. J. Virol. 78, 12428-12437
    • (2004) J. Virol , vol.78 , pp. 12428-12437
    • Baldwin, C.E.1    Sanders, R.W.2    Deng, Y.3    Jurriaans, S.4    Lange, J.M.5    Lu, M.6    Berkhout, B.7
  • 41
    • 35948978102 scopus 로고    scopus 로고
    • Demonstrating the c-terminal boundary of the hiv 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition
    • Wexler-Cohen, Y., and Shai, Y. (2007) Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition. FASEB J. 21, 3677-3684
    • (2007) FASEB J. , vol.21 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 42
    • 15744393651 scopus 로고    scopus 로고
    • Different from the hiv fusion inhibitor c34, the anti-hiv drug fuzeon (t-20) inhibits hiv-1 entry by targeting multiple sites in gp41 and gp120
    • Liu, S., Lu, H., Niu, J., Xu, Y., Wu, S., and Jiang, S. (2005) Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120. J. Biol. Chem. 280, 11259-11273
    • (2005) J. Biol. Chem. , vol.280 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 43
    • 0034834457 scopus 로고    scopus 로고
    • Lipid rafts and hiv pathogenesis: Host membrane cholesterol is required for infection by hiv type 1
    • Liao, Z., Cimakasky, L. M., Hampton, R., Nguyen, D. H., and Hildreth, J. E. (2001) Lipid rafts and HIV pathogenesis: host membrane cholesterol is required for infection by HIV type 1. AIDS Res. Hum. Retroviruses 17, 1009-1019
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1009-1019
    • Liao, Z.1    Cimakasky, L.M.2    Hampton, R.3    Nguyen, D.H.4    Hildreth, J.E.5
  • 44
    • 28244464389 scopus 로고    scopus 로고
    • Sphingolipids: Modulators of hiv-1 infection and pathogenesis
    • Rawat, S. S., Johnson, B. T., and Puri, A. (2005) Sphingolipids: modulators of HIV-1 infection and pathogenesis. Biosci. Rep. 25, 329-343
    • (2005) Biosci. Rep. , vol.25 , pp. 329-343
    • Rawat, S.S.1    Johnson, B.T.2    Puri, A.3
  • 45
    • 33846642714 scopus 로고    scopus 로고
    • The role of cholesterol and sphingolipids in chemokine receptor function and hiv-1 envelope glycoprotein-mediated fusion
    • Ablan, S., Rawat, S. S., Viard, M., Wang, J. M., Puri, A., and Blumenthal, R. (2006) The role of cholesterol and sphingolipids in chemokine receptor function and HIV-1 envelope glycoprotein-mediated fusion. Virol. J. 3, 104
    • (2006) Virol. J. , vol.3 , pp. 104
    • Ablan, S.1    Rawat, S.S.2    Viard, M.3    Wang, J.M.4    Puri, A.5    Blumenthal, R.6
  • 49
    • 0035033848 scopus 로고    scopus 로고
    • Membrane properties of d-erythro-n-Acyl sphingomyelins and their corresponding dihydro species
    • Kuikka, M., Ramstedt, B., Ohvo-Rekila, H., Tuuf, J., and Slotte, J. P. (2001) Membrane properties of d-erythro-N-Acyl sphingomyelins and their corresponding dihydro species. Biophys. J. 80, 2327-2337
    • (2001) Biophys. J. , vol.80 , pp. 2327-2337
    • Kuikka, M.1    Ramstedt, B.2    Ohvo-Rekila, H.3    Tuuf, J.4    Slotte, J.P.5
  • 50
    • 0038637713 scopus 로고    scopus 로고
    • Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes
    • Epand, R. M. (2003) Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes. Biophys. J. 84, 3102-3110
    • (2003) Biophys. J. , vol.84 , pp. 3102-3110
    • Epand, R.M.1
  • 51
    • 2642678478 scopus 로고    scopus 로고
    • Specific interaction of hiv-1 and hiv-2 surface envelope glycoproteins with monolayers of galactosylceramide and ganglioside gm3
    • Hammache, D., Pieroni, G., Yahi, N., Delezay, O., Koch, N., Lafont, H., Tamalet, C., and Fantini, J. (1998) Specific interaction of HIV-1 and HIV-2 surface envelope glycoproteins with monolayers of galactosylceramide and ganglioside GM3. J. Biol. Chem. 273, 7967-7971
    • (1998) J. Biol. Chem. , vol.273 , pp. 7967-7971
    • Hammache, D.1    Pieroni, G.2    Yahi, N.3    Delezay, O.4    Koch, N.5    Lafont, H.6    Tamalet, C.7    Fantini, J.8
  • 52
    • 34248343803 scopus 로고    scopus 로고
    • Sphingomyelinase restricts the lateral diffusion of cd4 and inhibits human immunodeficiency virus fusion
    • Finnegan, C. M., Rawat, S. S., Cho, E. H., Guiffre, D. L., Lockett, S., Merrill, A. H., Jr., and Blumenthal, R. (2007) Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion. J. Virol. 81, 5294-5304
    • (2007) J. Virol. , vol.81
    • Finnegan, C.M.1    Rawat, S.S.2    Cho, E.H.3    Guiffre, D.L.4    Lockett, S.5    Merrill Jr., A.6    Blumenthal, R.7
  • 53
    • 33646587391 scopus 로고    scopus 로고
    • Sphingolipids, cholesterol, and hiv-1: A paradigm in viral fusion
    • Rawat, S. S., Viard, M., Gallo, S. A., Blumenthal, R., and Puri, A. (2006) Sphingolipids, cholesterol, and HIV-1: a paradigm in viral fusion. Glycoconj. J. 23, 189-197
    • (2006) Glycoconj. J. , vol.23 , pp. 189-197
    • Rawat, S.S.1    Viard, M.2    Gallo, S.A.3    Blumenthal, R.4    Puri, A.5
  • 54
    • 0035873475 scopus 로고    scopus 로고
    • Secretory iga specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of hiv-1
    • Alfsen, A., Iniguez, P., Bouguyon, E., and Bomsel, M. (2001) Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1. J. Immunol. 166, 6257-6265
    • (2001) J. Immunol. , vol.166 , pp. 6257-6265
    • Alfsen, A.1    Iniguez, P.2    Bouguyon, E.3    Bomsel, M.4
  • 56
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of hiv-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon, V., Natrajan, G., Schibli, D., Campelo, F., Kozlov, M. M., and Weissenhorn, W. (2010) Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 6, e1000880
    • (2010) PLoS Pathog. , Issue.6
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.