메뉴 건너뛰기




Volumn 105, Issue 3, 2013, Pages 657-666

Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; GLYCOPROTEIN GP 41; LENTIVIRAL LYTIC PEPTIDE TYPE 1, HUMAN IMMUNODEFICIENCY VIRUS 1; PEPTIDE FRAGMENT;

EID: 84881432603     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.06.042     Document Type: Article
Times cited : (22)

References (64)
  • 1
    • 38349181791 scopus 로고    scopus 로고
    • Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein
    • J.M. Costin, and J.M. Rausch W.C. Wimley Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein Virol. J. 4 2007 1 14
    • (2007) Virol. J. , vol.4 , pp. 1-14
    • Costin, J.M.1    Rausch, J.M.2    Wimley, W.C.3
  • 2
    • 0033545957 scopus 로고    scopus 로고
    • Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41
    • B.W. Koenig, J.A. Ferretti, and K. Gawrisch Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41 Biochemistry 38 1999 6327 6334
    • (1999) Biochemistry , vol.38 , pp. 6327-6334
    • Koenig, B.W.1    Ferretti, J.A.2    Gawrisch, K.3
  • 3
    • 33646672410 scopus 로고    scopus 로고
    • The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein
    • M.R. Moreno, M. Giudici, and J. Villalaín The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein Biochim. Biophys. Acta 1758 2006 111 123
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 111-123
    • Moreno, M.R.1    Giudici, M.2    Villalaín, J.3
  • 4
    • 0030969495 scopus 로고    scopus 로고
    • A leucine zipper-like sequence from the cytoplasmic tail of the HIV-1 envelope glycoprotein binds and perturbs lipid bilayers
    • Y. Kliger, and Y. Shai A leucine zipper-like sequence from the cytoplasmic tail of the HIV-1 envelope glycoprotein binds and perturbs lipid bilayers Biochemistry 36 1997 5157 5169
    • (1997) Biochemistry , vol.36 , pp. 5157-5169
    • Kliger, Y.1    Shai, Y.2
  • 5
    • 0034812854 scopus 로고    scopus 로고
    • Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41
    • S.S.L. Chen, S.F. Lee, and C.T. Wang Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41 J. Virol. 75 2001 9925 9938
    • (2001) J. Virol. , vol.75 , pp. 9925-9938
    • Chen, S.S.L.1    Lee, S.F.2    Wang, C.T.3
  • 6
    • 0025055304 scopus 로고
    • The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glycoprotein 41
    • D. Eisenberg, and M. Wesson The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glycoprotein 41 Biopolymers 29 1990 171 177
    • (1990) Biopolymers , vol.29 , pp. 171-177
    • Eisenberg, D.1    Wesson, M.2
  • 7
    • 0034602736 scopus 로고    scopus 로고
    • The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions
    • T. Murakami, and E.O. Freed The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions Proc. Natl. Acad. Sci. USA 97 2000 343 348
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 8
    • 0026741425 scopus 로고
    • Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product
    • T. Wilk, T. Pfeiffer, and V. Bosch Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product Virology 189 1992 167 177
    • (1992) Virology , vol.189 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3
  • 9
    • 84871950126 scopus 로고    scopus 로고
    • The tale of the long tail: The cytoplasmic domain of HIV-1 gp41
    • T.S. Postler, and R.C. Desrosiers The tale of the long tail: the cytoplasmic domain of HIV-1 gp41 J. Virol. 87 2013 2 15
    • (2013) J. Virol. , vol.87 , pp. 2-15
    • Postler, T.S.1    Desrosiers, R.C.2
  • 10
    • 0037334568 scopus 로고    scopus 로고
    • Rational site-directed mutations of the LLP-1 and LLP-2 lentivirus lytic peptide domains in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 indicate common functions in cell-cell fusion but distinct roles in virion envelope incorporation
    • V. Kalia, and S. Sarkar R.C. Montelaro Rational site-directed mutations of the LLP-1 and LLP-2 lentivirus lytic peptide domains in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 indicate common functions in cell-cell fusion but distinct roles in virion envelope incorporation J. Virol. 77 2003 3634 3646
    • (2003) J. Virol. , vol.77 , pp. 3634-3646
    • Kalia, V.1    Sarkar, S.2    Montelaro, R.C.3
  • 11
    • 13444291135 scopus 로고    scopus 로고
    • Antibody neutralization escape mediated by point mutations in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41
    • V. Kalia, and S. Sarkar R.C. Montelaro Antibody neutralization escape mediated by point mutations in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 J. Virol. 79 2005 2097 2107
    • (2005) J. Virol. , vol.79 , pp. 2097-2107
    • Kalia, V.1    Sarkar, S.2    Montelaro, R.C.3
  • 12
    • 37649031391 scopus 로고    scopus 로고
    • Diffuse scattering provides material parameters and electron density profiles of biomembranes
    • (R)
    • Y.F. Liu, and J.F. Nagle Diffuse scattering provides material parameters and electron density profiles of biomembranes Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 69 2004 040901 040904 (R)
    • (2004) Phys. Rev. e Stat. Nonlin. Soft Matter Phys. , vol.69 , pp. 040901-040904
    • Liu, Y.F.1    Nagle, J.F.2
  • 13
    • 22144486884 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using X-ray scattering from oriented multilamellar arrays and from unilamellar vesicles
    • N. Kučerka, and Y.F. Liu J.F. Nagle Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using X-ray scattering from oriented multilamellar arrays and from unilamellar vesicles Biophys. J. 88 2005 2626 2637
    • (2005) Biophys. J. , vol.88 , pp. 2626-2637
    • Kučerka, N.1    Liu, Y.F.2    Nagle, J.F.3
  • 14
    • 47749087009 scopus 로고    scopus 로고
    • Order parameters and areas in fluid-phase oriented lipid membranes using wide angle X-ray scattering
    • T.T. Mills, and G.E.S. Toombes J.F. Nagle Order parameters and areas in fluid-phase oriented lipid membranes using wide angle X-ray scattering Biophys. J. 95 2008 669 681
    • (2008) Biophys. J. , vol.95 , pp. 669-681
    • Mills, T.T.1    Toombes, G.E.S.2    Nagle, J.F.3
  • 17
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • R. Chan, and P.D. Uchil M.R. Wenk Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides J. Virol. 82 2008 11228 11238
    • (2008) J. Virol. , vol.82 , pp. 11228-11238
    • Chan, R.1    Uchil, P.D.2    Wenk, M.R.3
  • 18
    • 40949163797 scopus 로고    scopus 로고
    • CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol
    • A.I. Greenwood, and J.J. Pan S. Tristram-Nagle CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol Biochim. Biophys. Acta 1778 2008 1120 1130
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1120-1130
    • Greenwood, A.I.1    Pan, J.J.2    Tristram-Nagle, S.3
  • 19
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • H. Li, and V. Papadopoulos Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern Endocrinology 139 1998 4991 4997
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 20
    • 0346220015 scopus 로고    scopus 로고
    • Peptide-induced formation of cholesterol-rich domains
    • R.M. Epand, B.G. Sayer, and R.F. Epand Peptide-induced formation of cholesterol-rich domains Biochemistry 42 2003 14677 14689
    • (2003) Biochemistry , vol.42 , pp. 14677-14689
    • Epand, R.M.1    Sayer, B.G.2    Epand, R.F.3
  • 21
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • I. Rousso, and M.B. Mixon P.S. Kim Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity Proc. Natl. Acad. Sci. USA 97 2000 13523 13525
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Kim, P.S.3
  • 22
    • 0028784818 scopus 로고
    • The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated
    • C.L. Yang, C.P. Spies, and R.W. Compans The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated Proc. Natl. Acad. Sci. USA 92 1995 9871 9875
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9871-9875
    • Yang, C.L.1    Spies, C.P.2    Compans, R.W.3
  • 23
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • E.G. Bligh, and W.J. Dyer A rapid method of total lipid extraction and purification Can. J. Biochem. Physiol. 37 1959 911 917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 24
    • 78650164019 scopus 로고    scopus 로고
    • Topology of the C-terminal tail of HIV-1 gp41: Differential exposure of the Kennedy epitope on cell and viral membranes
    • J.D. Steckbeck, and C.Q. Sun R.C. Montelaro Topology of the C-terminal tail of HIV-1 gp41: differential exposure of the Kennedy epitope on cell and viral membranes PLoS ONE 5 2010 e15261
    • (2010) PLoS ONE , vol.5 , pp. 15261
    • Steckbeck, J.D.1    Sun, C.Q.2    Montelaro, R.C.3
  • 25
    • 36549088496 scopus 로고    scopus 로고
    • Preparation of oriented, fully hydrated lipid samples for structure determination using X-ray scattering
    • S.A. Tristram-Nagle Preparation of oriented, fully hydrated lipid samples for structure determination using X-ray scattering Methods Mol. Biol. 400 2007 63 75
    • (2007) Methods Mol. Biol. , vol.400 , pp. 63-75
    • Tristram-Nagle, S.A.1
  • 26
    • 84859608897 scopus 로고    scopus 로고
    • Structure and elasticity of lipid membranes with genistein and daidzein bioflavinoids using X-ray scattering and MD simulations
    • M. Raghunathan, and Y. Zubovski S. Tristram-Nagle Structure and elasticity of lipid membranes with genistein and daidzein bioflavinoids using X-ray scattering and MD simulations J. Phys. Chem. B 116 2012 3918 3927
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3918-3927
    • Raghunathan, M.1    Zubovski, Y.2    Tristram-Nagle, S.3
  • 27
    • 51649129838 scopus 로고    scopus 로고
    • Lipid bilayer structure determined by the simultaneous analysis of neutron and X-ray scattering data
    • N. Kučerka, and J.F. Nagle J. Katsaras Lipid bilayer structure determined by the simultaneous analysis of neutron and X-ray scattering data Biophys. J. 95 2008 2356 2367
    • (2008) Biophys. J. , vol.95 , pp. 2356-2367
    • Kučerka, N.1    Nagle, J.F.2    Katsaras, J.3
  • 28
    • 0024615072 scopus 로고
    • Relations for lipid bilayers. Connection of electron density profiles to other structural quantities
    • J.F. Nagle, and M.C. Wiener Relations for lipid bilayers. Connection of electron density profiles to other structural quantities Biophys. J. 55 1989 309 313
    • (1989) Biophys. J. , vol.55 , pp. 309-313
    • Nagle, J.F.1    Wiener, M.C.2
  • 29
    • 3142723209 scopus 로고    scopus 로고
    • Determination of bilayer thickness and lipid surface area in unilamellar dimyristoylphosphatidylcholine vesicles from small-angle neutron scattering curves: A comparison of evaluation methods
    • N. Kučerka, M.A. Kiselev, and P. Balgavý Determination of bilayer thickness and lipid surface area in unilamellar dimyristoylphosphatidylcholine vesicles from small-angle neutron scattering curves: a comparison of evaluation methods Eur. Biophys. J. 33 2004 328 334
    • (2004) Eur. Biophys. J. , vol.33 , pp. 328-334
    • Kučerka, N.1    Kiselev, M.A.2    Balgavý, P.3
  • 30
    • 47749126522 scopus 로고    scopus 로고
    • Liquid-liquid domains in bilayers detected by wide angle X-ray scattering
    • T.T. Mills, and S. Tristram-Nagle G.W. Feigenson Liquid-liquid domains in bilayers detected by wide angle X-ray scattering Biophys. J. 95 2008 682 690
    • (2008) Biophys. J. , vol.95 , pp. 682-690
    • Mills, T.T.1    Tristram-Nagle, S.2    Feigenson, G.W.3
  • 31
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Y. Wu, H.W. Huang, and G.A. Olah Method of oriented circular dichroism Biophys. J. 57 1990 797 806
    • (1990) Biophys. J. , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 32
    • 33244472850 scopus 로고    scopus 로고
    • Directed assembly of surface-supported bilayers with transmembrane helices
    • M. Merzlyakov, E. Li, and K. Hristova Directed assembly of surface-supported bilayers with transmembrane helices Langmuir 22 2006 1247 1253
    • (2006) Langmuir , vol.22 , pp. 1247-1253
    • Merzlyakov, M.1    Li, E.2    Hristova, K.3
  • 33
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, and B.A. Wallace DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra Bioinformatics 18 2002 211 212
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 34
    • 79958139475 scopus 로고    scopus 로고
    • A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy
    • A. Abdul-Gader, A.J. Miles, and B.A. Wallace A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy Bioinformatics 27 2011 1630 1636
    • (2011) Bioinformatics , vol.27 , pp. 1630-1636
    • Abdul-Gader, A.1    Miles, A.J.2    Wallace, B.A.3
  • 35
    • 10644275071 scopus 로고
    • Unbinding transition of a biological model membrane
    • M. Mutz, and W. Helfrich Unbinding transition of a biological model membrane Phys. Rev. Lett. 62 1989 2881 2884
    • (1989) Phys. Rev. Lett. , vol.62 , pp. 2881-2884
    • Mutz, M.1    Helfrich, W.2
  • 36
    • 0001554189 scopus 로고
    • Intrinsic bending force in anisotropic membranes made of chiral molecules
    • W. Helfrich, and J. Prost Intrinsic bending force in anisotropic membranes made of chiral molecules Phys. Rev. A 38 1988 3065 3068
    • (1988) Phys. Rev. A , vol.38 , pp. 3065-3068
    • Helfrich, W.1    Prost, J.2
  • 37
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • N. Kučerka, S. Tristram-Nagle, and J.F. Nagle Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains J. Membr. Biol. 208 2005 193 202
    • (2005) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kučerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 38
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • W. Rawicz, and K.C. Olbrich E. Evans Effect of chain length and unsaturation on elasticity of lipid bilayers Biophys. J. 79 2000 328 339
    • (2000) Biophys. J. , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    Evans, E.3
  • 39
    • 34548726186 scopus 로고    scopus 로고
    • HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates
    • S. Tristram-Nagle, and J.F. Nagle HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates Biophys. J. 93 2007 2048 2055
    • (2007) Biophys. J. , vol.93 , pp. 2048-2055
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 40
    • 84869217910 scopus 로고    scopus 로고
    • HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes
    • R.A. Dick, and S.L. Goh V.M. Vogt HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes Proc. Natl. Acad. Sci. USA 109 2012 18761 18766
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 18761-18766
    • Dick, R.A.1    Goh, S.L.2    Vogt, V.M.3
  • 41
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • R.S. Cantor Lipid composition and the lateral pressure profile in bilayers Biophys. J. 76 1999 2625 2639
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 42
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • L. Shang, L. Yue, and E. Hunter Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection J. Virol. 82 2008 5417 5428
    • (2008) J. Virol. , vol.82 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 43
    • 0034801792 scopus 로고    scopus 로고
    • Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity
    • J.T. West, and P.B. Johnston E. Hunter Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity J. Virol. 75 2001 9601 9612
    • (2001) J. Virol. , vol.75 , pp. 9601-9612
    • West, J.T.1    Johnston, P.B.2    Hunter, E.3
  • 44
    • 77952000064 scopus 로고    scopus 로고
    • Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain
    • N. Kondo, and K. Miyauchi Z. Matsuda Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain J. Biol. Chem. 285 2010 14681 14688
    • (2010) J. Biol. Chem. , vol.285 , pp. 14681-14688
    • Kondo, N.1    Miyauchi, K.2    Matsuda, Z.3
  • 45
    • 0025471152 scopus 로고
    • Bilayer membrane bending stiffness by tether formation from mixed PC-PS lipid vesicles
    • J. Song, and R.E. Waugh Bilayer membrane bending stiffness by tether formation from mixed PC-PS lipid vesicles J. Biomech. Eng. 112 1990 235 240
    • (1990) J. Biomech. Eng. , vol.112 , pp. 235-240
    • Song, J.1    Waugh, R.E.2
  • 46
    • 3042773847 scopus 로고    scopus 로고
    • Experimental evidence of the electrostatic contribution to membrane rigidity
    • A.C. Rowat, P.L. Hansen, and J.H. Ipsen Experimental evidence of the electrostatic contribution to membrane rigidity Europhys. Lett. 67 2004 144 149
    • (2004) Europhys. Lett. , vol.67 , pp. 144-149
    • Rowat, A.C.1    Hansen, P.L.2    Ipsen, J.H.3
  • 47
    • 58149355792 scopus 로고    scopus 로고
    • The Gaussian curvature elastic energy of intermediates in membrane fusion
    • D.P. Siegel The Gaussian curvature elastic energy of intermediates in membrane fusion Biophys. J. 95 2008 5200 5215
    • (2008) Biophys. J. , vol.95 , pp. 5200-5215
    • Siegel, D.P.1
  • 48
    • 33847777367 scopus 로고    scopus 로고
    • A stiffness switch in human immunodeficiency virus
    • N. Kol, and Y. Shi I. Rousso A stiffness switch in human immunodeficiency virus Biophys. J. 92 2007 1777 1783
    • (2007) Biophys. J. , vol.92 , pp. 1777-1783
    • Kol, N.1    Shi, Y.2    Rousso, I.3
  • 49
    • 43849089443 scopus 로고    scopus 로고
    • Cholesterol perturbs lipid bilayers nonuniversally
    • J.J. Pan, and T.T. Mills J.F. Nagle Cholesterol perturbs lipid bilayers nonuniversally Phys. Rev. Lett. 100 2008 198103
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 198103
    • Pan, J.J.1    Mills, T.T.2    Nagle, J.F.3
  • 50
    • 70349153375 scopus 로고    scopus 로고
    • Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation
    • J.J. Pan, S. Tristram-Nagle, and J.F. Nagle Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation Phys. Rev. E 80 2009 021931
    • (2009) Phys. Rev. e , vol.80 , pp. 021931
    • Pan, J.J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 51
    • 79961008478 scopus 로고    scopus 로고
    • Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: Implications for functions in viral replication
    • J.D. Steckbeck, and J.K. Craigo R.C. Montelaro Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication J. Biol. Chem. 286 2011 27156 27166
    • (2011) J. Biol. Chem. , vol.286 , pp. 27156-27166
    • Steckbeck, J.D.1    Craigo, J.K.2    Montelaro, R.C.3
  • 53
    • 0034717055 scopus 로고    scopus 로고
    • Multimerization potential of the cytoplasmic domain of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41
    • S.F. Lee, and C.T. Wang S.S.L. Chen Multimerization potential of the cytoplasmic domain of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 J. Biol. Chem. 275 2000 15809 15819
    • (2000) J. Biol. Chem. , vol.275 , pp. 15809-15819
    • Lee, S.F.1    Wang, C.T.2    Chen, S.S.L.3
  • 54
    • 35648979561 scopus 로고    scopus 로고
    • Characterization of replication defects induced by mutations in the basic domain and C-terminus of HIV-1 matrix
    • A.K. Bhatia, and N. Campbell L. Ratner Characterization of replication defects induced by mutations in the basic domain and C-terminus of HIV-1 matrix Virology 369 2007 47 54
    • (2007) Virology , vol.369 , pp. 47-54
    • Bhatia, A.K.1    Campbell, N.2    Ratner, L.3
  • 55
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • E.O. Freed, and M.A. Martin Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions J. Virol. 70 1996 341 351
    • (1996) J. Virol. , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 56
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • E.O. Freed, and J.M. Orenstein M.A. Martin Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production J. Virol. 68 1994 5311 5320
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Martin, M.A.3
  • 57
    • 0034632924 scopus 로고    scopus 로고
    • Identification of the glycoprotein 41(TM) cytoplasmic tail domains of human immunodeficiency virus type 1 that interact with Pr55Gag particles
    • C. Hourioux, and D. Brand P. Roingeard Identification of the glycoprotein 41(TM) cytoplasmic tail domains of human immunodeficiency virus type 1 that interact with Pr55Gag particles AIDS Res. Hum. Retroviruses 16 2000 1141 1147
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1141-1147
    • Hourioux, C.1    Brand, D.2    Roingeard, P.3
  • 58
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • A. Ono, and E.O. Freed Plasma membrane rafts play a critical role in HIV-1 assembly and release Proc. Natl. Acad. Sci. USA 98 2001 13925 13930
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 59
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • O.W. Lindwasser, and M.D. Resh Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains J. Virol. 75 2001 7913 7924
    • (2001) J. Virol. , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 60
    • 27644522295 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: Use of a novel Gag multimerization assay
    • A. Ono, and A.A. Waheed E.O. Freed Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assay J. Virol. 79 2005 14131 14140
    • (2005) J. Virol. , vol.79 , pp. 14131-14140
    • Ono, A.1    Waheed, A.A.2    Freed, E.O.3
  • 61
    • 76949095696 scopus 로고    scopus 로고
    • Evidence that Gag facilitates HIV-1 envelope association both in GPI-enriched plasma membrane and detergent resistant membranes and facilitates envelope incorporation onto virions in primary CD4+ T cells
    • A. Patil, A. Gautam, and J. Bhattacharya Evidence that Gag facilitates HIV-1 envelope association both in GPI-enriched plasma membrane and detergent resistant membranes and facilitates envelope incorporation onto virions in primary CD4+ T cells Virol. J. 7 2010 1 5
    • (2010) Virol. J. , vol.7 , pp. 1-5
    • Patil, A.1    Gautam, A.2    Bhattacharya, J.3
  • 62
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • J.S. Saad, and J. Miller M.F. Summers Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly Proc. Natl. Acad. Sci. USA 103 2006 11364 11369
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Summers, M.F.3
  • 63
    • 25144488199 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail
    • S. Wyss, and A.S. Dimitrov J.A. Hoxie Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail J. Virol. 79 2005 12231 12241
    • (2005) J. Virol. , vol.79 , pp. 12231-12241
    • Wyss, S.1    Dimitrov, A.S.2    Hoxie, J.A.3
  • 64
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation
    • M.A. Checkley, B.G. Luttge, and E.O. Freed HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation J. Mol. Biol. 410 2011 582 608
    • (2011) J. Mol. Biol. , vol.410 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.