메뉴 건너뛰기




Volumn 22, Issue 1, 2017, Pages 99-110.e7

Fusion Stage of HIV-1 Entry Depends on Virus-Induced Cell Surface Exposure of Phosphatidylserine

Author keywords

cell activation; cell signaling; gp120 CD4 coreceptor; hemifusion; HIV entry; lipid scramblase; membrane fusion; phosphatidylserine exposure; TMEM16F activity; viral entry

Indexed keywords

CALCIUM ION; CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; GLYCOPROTEIN; LACTADHERIN; LYSOPHOSPHATIDYLCHOLINE; N [4 [[[6,7 DIHYDRO 2 (4 METHYLPHENYL) 5H BENZOCYCLOHEPTEN 8 YL]CARBONYL]AMINO]BENZYL] N,N DIMETHYL 2H TETRAHYDROPYRAN 4 AMINIUM CHLORIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLSERINE; PLERIXAFOR; SHORT HAIRPIN RNA; AMIDE; ANO6 PROTEIN, HUMAN; ANOCTAMIN; CALCIUM; CCR5 PROTEIN, HUMAN; CXCR4 PROTEIN, HUMAN; HETEROCYCLIC COMPOUND; MONOCLONAL ANTIBODY; PHOSPHOLIPID TRANSFER PROTEIN; QUATERNARY AMMONIUM DERIVATIVE; VIRUS ENVELOPE PROTEIN;

EID: 85030456275     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2017.06.012     Document Type: Article
Times cited : (98)

References (58)
  • 1
    • 44949167779 scopus 로고    scopus 로고
    • Intracellular calcium signalling patterns reflect the differentiation status of human T cells
    • Arrol, H.P., Church, L.D., Bacon, P.A., Young, S.P., Intracellular calcium signalling patterns reflect the differentiation status of human T cells. Clin. Exp. Immunol. 153 (2008), 86–95.
    • (2008) Clin. Exp. Immunol. , vol.153 , pp. 86-95
    • Arrol, H.P.1    Church, L.D.2    Bacon, P.A.3    Young, S.P.4
  • 2
    • 84946606167 scopus 로고    scopus 로고
    • Binding of alphaherpesvirus glycoprotein H to surface α4β1-integrins activates calcium-signaling pathways and induces phosphatidylserine exposure on the plasma membrane
    • e01552–15
    • Azab, W., Gramatica, A., Herrmann, A., Osterrieder, N., Binding of alphaherpesvirus glycoprotein H to surface α4β1-integrins activates calcium-signaling pathways and induces phosphatidylserine exposure on the plasma membrane. MBio, 6, 2015 e01552–15.
    • (2015) MBio , vol.6
    • Azab, W.1    Gramatica, A.2    Herrmann, A.3    Osterrieder, N.4
  • 3
    • 0028173961 scopus 로고
    • Effects of CD45 on NF-kappa B. Implications for replication of HIV-1
    • Baur, A., Garber, S., Peterlin, B.M., Effects of CD45 on NF-kappa B. Implications for replication of HIV-1. J. Immunol. 152 (1994), 976–983.
    • (1994) J. Immunol. , vol.152 , pp. 976-983
    • Baur, A.1    Garber, S.2    Peterlin, B.M.3
  • 5
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley, J.M., Cayanan, C.S., Wiley, C., Schülke, N., Olson, W.C., Burton, D.R., Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77 (2003), 5678–5684.
    • (2003) J. Virol. , vol.77 , pp. 5678-5684
    • Binley, J.M.1    Cayanan, C.S.2    Wiley, C.3    Schülke, N.4    Olson, W.C.5    Burton, D.R.6
  • 6
    • 84870372472 scopus 로고    scopus 로고
    • HIV entry and envelope glycoprotein-mediated fusion
    • Blumenthal, R., Durell, S., Viard, M., HIV entry and envelope glycoprotein-mediated fusion. J. Biol. Chem. 287 (2012), 40841–40849.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40841-40849
    • Blumenthal, R.1    Durell, S.2    Viard, M.3
  • 8
    • 0036199093 scopus 로고    scopus 로고
    • Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions
    • Carneiro, F.A., Bianconi, M.L., Weissmüller, G., Stauffer, F., Da Poian, A.T., Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions. J. Virol. 76 (2002), 3756–3764.
    • (2002) J. Virol. , vol.76 , pp. 3756-3764
    • Carneiro, F.A.1    Bianconi, M.L.2    Weissmüller, G.3    Stauffer, F.4    Da Poian, A.T.5
  • 10
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: crossing a chasm in two leaps
    • Chernomordik, L.V., Kozlov, M.M., Membrane hemifusion: crossing a chasm in two leaps. Cell 123 (2005), 375–382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 11
    • 23844483178 scopus 로고    scopus 로고
    • Enhancement of enveloped virus entry by phosphatidylserine
    • Coil, D.A., Miller, A.D., Enhancement of enveloped virus entry by phosphatidylserine. J. Virol. 79 (2005), 11496–11500.
    • (2005) J. Virol. , vol.79 , pp. 11496-11500
    • Coil, D.A.1    Miller, A.D.2
  • 12
    • 27344433427 scopus 로고    scopus 로고
    • Phosphatidylserine treatment relieves the block to retrovirus infection of cells expressing glycosylated virus receptors
    • Coil, D.A., Miller, A.D., Phosphatidylserine treatment relieves the block to retrovirus infection of cells expressing glycosylated virus receptors. Retrovirology, 2, 2005, 49.
    • (2005) Retrovirology , vol.2 , pp. 49
    • Coil, D.A.1    Miller, A.D.2
  • 13
    • 33750608556 scopus 로고    scopus 로고
    • Paramyxovirus fusion: real-time measurement of parainfluenza virus 5 virus-cell fusion
    • Connolly, S.A., Lamb, R.A., Paramyxovirus fusion: real-time measurement of parainfluenza virus 5 virus-cell fusion. Virology 355 (2006), 203–212.
    • (2006) Virology , vol.355 , pp. 203-212
    • Connolly, S.A.1    Lamb, R.A.2
  • 14
    • 66149118152 scopus 로고    scopus 로고
    • Human immunodeficiency virus integrates directly into naive resting CD4+ T cells but enters naive cells less efficiently than memory cells
    • Dai, J., Agosto, L.M., Baytop, C., Yu, J.J., Pace, M.J., Liszewski, M.K., O'Doherty, U., Human immunodeficiency virus integrates directly into naive resting CD4+ T cells but enters naive cells less efficiently than memory cells. J. Virol. 83 (2009), 4528–4537.
    • (2009) J. Virol. , vol.83 , pp. 4528-4537
    • Dai, J.1    Agosto, L.M.2    Baytop, C.3    Yu, J.J.4    Pace, M.J.5    Liszewski, M.K.6    O'Doherty, U.7
  • 16
    • 34147124231 scopus 로고    scopus 로고
    • Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor
    • Deng, Y., Zheng, Q., Ketas, T.J., Moore, J.P., Lu, M., Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor. Biochemistry 46 (2007), 4360–4369.
    • (2007) Biochemistry , vol.46 , pp. 4360-4369
    • Deng, Y.1    Zheng, Q.2    Ketas, T.J.3    Moore, J.P.4    Lu, M.5
  • 17
    • 0030770546 scopus 로고    scopus 로고
    • Unwelcomed guests with master keys: how HIV uses chemokine receptors for cellular entry
    • Doms, R.W., Peiper, S.C., Unwelcomed guests with master keys: how HIV uses chemokine receptors for cellular entry. Virology 235 (1997), 179–190.
    • (1997) Virology , vol.235 , pp. 179-190
    • Doms, R.W.1    Peiper, S.C.2
  • 19
    • 70349898677 scopus 로고    scopus 로고
    • The ins and outs of phospholipid asymmetry in the plasma membrane: roles in health and disease
    • Fadeel, B., Xue, D., The ins and outs of phospholipid asymmetry in the plasma membrane: roles in health and disease. Crit. Rev. Biochem. Mol. Biol. 44 (2009), 264–277.
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 264-277
    • Fadeel, B.1    Xue, D.2
  • 20
    • 84876926824 scopus 로고    scopus 로고
    • LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus
    • Finkelshtein, D., Werman, A., Novick, D., Barak, S., Rubinstein, M., LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus. Proc. Natl. Acad. Sci. USA 110 (2013), 7306–7311.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7306-7311
    • Finkelshtein, D.1    Werman, A.2    Novick, D.3    Barak, S.4    Rubinstein, M.5
  • 21
    • 33845512042 scopus 로고    scopus 로고
    • Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells
    • Fischer, K., Voelkl, S., Berger, J., Andreesen, R., Pomorski, T., Mackensen, A., Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells. Blood 108 (2006), 4094–4101.
    • (2006) Blood , vol.108 , pp. 4094-4101
    • Fischer, K.1    Voelkl, S.2    Berger, J.3    Andreesen, R.4    Pomorski, T.5    Mackensen, A.6
  • 22
    • 0030065395 scopus 로고    scopus 로고
    • Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import
    • Gallay, P., Stitt, V., Mundy, C., Oettinger, M., Trono, D., Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 70 (1996), 1027–1032.
    • (1996) J. Virol. , vol.70 , pp. 1027-1032
    • Gallay, P.1    Stitt, V.2    Mundy, C.3    Oettinger, M.4    Trono, D.5
  • 23
    • 78349293747 scopus 로고    scopus 로고
    • V-fusion: a convenient, nontoxic method for cell fusion
    • Gottesman, A., Milazzo, J., Lazebnik, Y., V-fusion: a convenient, nontoxic method for cell fusion. Biotechniques 49 (2010), 747–750.
    • (2010) Biotechniques , vol.49 , pp. 747-750
    • Gottesman, A.1    Milazzo, J.2    Lazebnik, Y.3
  • 24
    • 59849112612 scopus 로고    scopus 로고
    • Use of human tissue explants to study human infectious agents
    • Grivel, J.C., Margolis, L., Use of human tissue explants to study human infectious agents. Nat. Protoc. 4 (2009), 256–269.
    • (2009) Nat. Protoc. , vol.4 , pp. 256-269
    • Grivel, J.C.1    Margolis, L.2
  • 25
    • 35448941978 scopus 로고    scopus 로고
    • Advances in methods for the production, purification, and characterization of HIV-1 Gag-Env pseudovirion vaccines
    • Hammonds, J., Chen, X., Zhang, X., Lee, F., Spearman, P., Advances in methods for the production, purification, and characterization of HIV-1 Gag-Env pseudovirion vaccines. Vaccine 25 (2007), 8036–8048.
    • (2007) Vaccine , vol.25 , pp. 8036-8048
    • Hammonds, J.1    Chen, X.2    Zhang, X.3    Lee, F.4    Spearman, P.5
  • 26
    • 50949123789 scopus 로고    scopus 로고
    • Induction of the Galpha(q) signaling cascade by the human immunodeficiency virus envelope is required for virus entry
    • Harmon, B., Ratner, L., Induction of the Galpha(q) signaling cascade by the human immunodeficiency virus envelope is required for virus entry. J. Virol. 82 (2008), 9191–9205.
    • (2008) J. Virol. , vol.82 , pp. 9191-9205
    • Harmon, B.1    Ratner, L.2
  • 27
    • 77954666282 scopus 로고    scopus 로고
    • Role of Abl kinase and the Wave2 signaling complex in HIV-1 entry at a post-hemifusion step
    • Harmon, B., Campbell, N., Ratner, L., Role of Abl kinase and the Wave2 signaling complex in HIV-1 entry at a post-hemifusion step. PLoS Pathog., 6, 2010, e1000956.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000956
    • Harmon, B.1    Campbell, N.2    Ratner, L.3
  • 29
  • 30
    • 0033919404 scopus 로고    scopus 로고
    • Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    • Kwong, P.D., Wyatt, R., Sattentau, Q.J., Sodroski, J., Hendrickson, W.A., Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74 (2000), 1961–1972.
    • (2000) J. Virol. , vol.74 , pp. 1961-1972
    • Kwong, P.D.1    Wyatt, R.2    Sattentau, Q.J.3    Sodroski, J.4    Hendrickson, W.A.5
  • 32
    • 0027531929 scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) fusion with model membranes: kinetic analysis and the role of lipid composition, pH and divalent cations
    • Larsen, C.E., Nir, S., Alford, D.R., Jennings, M., Lee, K.D., Düzgüneş, N., Human immunodeficiency virus type 1 (HIV-1) fusion with model membranes: kinetic analysis and the role of lipid composition, pH and divalent cations. Biochim. Biophys. Acta 1147 (1993), 223–236.
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 223-236
    • Larsen, C.E.1    Nir, S.2    Alford, D.R.3    Jennings, M.4    Lee, K.D.5    Düzgüneş, N.6
  • 35
    • 84877119843 scopus 로고    scopus 로고
    • Anionic lipids are required for vesicular stomatitis virus G protein-mediated single particle fusion with supported lipid bilayers
    • Matos, P.M., Marin, M., Ahn, B., Lam, W., Santos, N.C., Melikyan, G.B., Anionic lipids are required for vesicular stomatitis virus G protein-mediated single particle fusion with supported lipid bilayers. J. Biol. Chem. 288 (2013), 12416–12425.
    • (2013) J. Biol. Chem. , vol.288 , pp. 12416-12425
    • Matos, P.M.1    Marin, M.2    Ahn, B.3    Lam, W.4    Santos, N.C.5    Melikyan, G.B.6
  • 36
    • 33846837651 scopus 로고    scopus 로고
    • Physiological levels of virion-associated human immunodeficiency virus type 1 envelope induce coreceptor-dependent calcium flux
    • Melar, M., Ott, D.E., Hope, T.J., Physiological levels of virion-associated human immunodeficiency virus type 1 envelope induce coreceptor-dependent calcium flux. J. Virol. 81 (2007), 1773–1785.
    • (2007) J. Virol. , vol.81 , pp. 1773-1785
    • Melar, M.1    Ott, D.E.2    Hope, T.J.3
  • 37
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm
    • Melikyan, G.B., Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm. Retrovirology, 5, 2008, 111.
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 38
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi, K., Kim, Y., Latinovic, O., Morozov, V., Melikyan, G.B., HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137 (2009), 433–444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 40
    • 84857655202 scopus 로고    scopus 로고
    • Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition
    • Otzen, D.E., Blans, K., Wang, H., Gilbert, G.E., Rasmussen, J.T., Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition. Biochim. Biophys. Acta 1818 (2012), 1019–1027.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1019-1027
    • Otzen, D.E.1    Blans, K.2    Wang, H.3    Gilbert, G.E.4    Rasmussen, J.T.5
  • 42
    • 84878528694 scopus 로고    scopus 로고
    • Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design
    • Ping, L.H., Joseph, S.B., Anderson, J.A., Abrahams, M.R., Salazar-Gonzalez, J.F., Kincer, L.P., Treurnicht, F.K., Arney, L., Ojeda, S., Zhang, M., et al., CAPRISA Acute Infection Study and the Center for HIV-AIDS Vaccine Immunology Consortium. Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design. J. Virol. 87 (2013), 7218–7233.
    • (2013) J. Virol. , vol.87 , pp. 7218-7233
    • Ping, L.H.1    Joseph, S.B.2    Anderson, J.A.3    Abrahams, M.R.4    Salazar-Gonzalez, J.F.5    Kincer, L.P.6    Treurnicht, F.K.7    Arney, L.8    Ojeda, S.9    Zhang, M.10
  • 43
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt, E.J., Wehrly, K., Kuhmann, S.E., Chesebro, B., Kabat, D., Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J. Virol. 72 (1998), 2855–2864.
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 44
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt, E.J., Durnin, J.P., Kabat, D., Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J. Virol. 79 (2005), 4347–4356.
    • (2005) J. Virol. , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 45
    • 67749110262 scopus 로고    scopus 로고
    • Evidence that ecotropic murine leukemia virus contamination in TZM-bl cells does not affect the outcome of neutralizing antibody assays with human immunodeficiency virus type 1
    • Platt, E.J., Bilska, M., Kozak, S.L., Kabat, D., Montefiori, D.C., Evidence that ecotropic murine leukemia virus contamination in TZM-bl cells does not affect the outcome of neutralizing antibody assays with human immunodeficiency virus type 1. J. Virol. 83 (2009), 8289–8292.
    • (2009) J. Virol. , vol.83 , pp. 8289-8292
    • Platt, E.J.1    Bilska, M.2    Kozak, S.L.3    Kabat, D.4    Montefiori, D.C.5
  • 46
    • 77649171305 scopus 로고    scopus 로고
    • Rapid dissociation of HIV-1 from cultured cells severely limits infectivity assays, causes the inactivation ascribed to entry inhibitors, and masks the inherently high level of infectivity of virions
    • Platt, E.J., Kozak, S.L., Durnin, J.P., Hope, T.J., Kabat, D., Rapid dissociation of HIV-1 from cultured cells severely limits infectivity assays, causes the inactivation ascribed to entry inhibitors, and masks the inherently high level of infectivity of virions. J. Virol. 84 (2010), 3106–3110.
    • (2010) J. Virol. , vol.84 , pp. 3106-3110
    • Platt, E.J.1    Kozak, S.L.2    Durnin, J.P.3    Hope, T.J.4    Kabat, D.5
  • 47
    • 1842287973 scopus 로고    scopus 로고
    • Identification of a chemokine receptor encoded by human cytomegalovirus as a cofactor for HIV-1 entry
    • Pleskoff, O., Tréboute, C., Brelot, A., Heveker, N., Seman, M., Alizon, M., Identification of a chemokine receptor encoded by human cytomegalovirus as a cofactor for HIV-1 entry. Science 276 (1997), 1874–1878.
    • (1997) Science , vol.276 , pp. 1874-1878
    • Pleskoff, O.1    Tréboute, C.2    Brelot, A.3    Heveker, N.4    Seman, M.5    Alizon, M.6
  • 48
  • 49
    • 77956630038 scopus 로고    scopus 로고
    • Virus-induced Ca2+ influx extends survival of west nile virus-infected cells
    • Scherbik, S.V., Brinton, M.A., Virus-induced Ca2+ influx extends survival of west nile virus-infected cells. J. Virol. 84 (2010), 8721–8731.
    • (2010) J. Virol. , vol.84 , pp. 8721-8731
    • Scherbik, S.V.1    Brinton, M.A.2
  • 50
    • 82755163551 scopus 로고    scopus 로고
    • Constitutive exposure of phosphatidylserine on viable cells
    • Segawa, K., Suzuki, J., Nagata, S., Constitutive exposure of phosphatidylserine on viable cells. Proc. Natl. Acad. Sci. USA 108 (2011), 19246–19251.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 19246-19251
    • Segawa, K.1    Suzuki, J.2    Nagata, S.3
  • 51
    • 43749112983 scopus 로고    scopus 로고
    • Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif
    • Shao, C., Novakovic, V.A., Head, J.F., Seaton, B.A., Gilbert, G.E., Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif. J. Biol. Chem. 283 (2008), 7230–7241.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7230-7241
    • Shao, C.1    Novakovic, V.A.2    Head, J.F.3    Seaton, B.A.4    Gilbert, G.E.5
  • 53
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki, J., Umeda, M., Sims, P.J., Nagata, S., Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468 (2010), 834–838.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 56
    • 74549178998 scopus 로고    scopus 로고
    • Chemokine coreceptor signaling in HIV-1 infection and pathogenesis
    • Wu, Y., Yoder, A., Chemokine coreceptor signaling in HIV-1 infection and pathogenesis. PLoS Pathog., 5, 2009, e1000520.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000520
    • Wu, Y.1    Yoder, A.2
  • 57
    • 78449257072 scopus 로고    scopus 로고
    • Dengue virus ensures its fusion in late endosomes using compartment-specific lipids
    • Zaitseva, E., Yang, S.-T., Melikov, K., Pourmal, S., Chernomordik, L.V., Dengue virus ensures its fusion in late endosomes using compartment-specific lipids. PLoS Pathog., 6, 2010, e1001131.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001131
    • Zaitseva, E.1    Yang, S.-T.2    Melikov, K.3    Pourmal, S.4    Chernomordik, L.V.5
  • 58
    • 0035958043 scopus 로고    scopus 로고
    • Dantrolene inhibition of ryanodine receptor Ca2+ release channels. Molecular mechanism and isoform selectivity
    • Zhao, F., Li, P., Chen, S.R., Louis, C.F., Fruen, B.R., Dantrolene inhibition of ryanodine receptor Ca2+ release channels. Molecular mechanism and isoform selectivity. J. Biol. Chem. 276 (2001), 13810–13816.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13810-13816
    • Zhao, F.1    Li, P.2    Chen, S.R.3    Louis, C.F.4    Fruen, B.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.