메뉴 건너뛰기




Volumn 174, Issue 3, 2018, Pages 659-671.e14

HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation

Author keywords

adaptor protein; clathrin; cryo EM; HIV; HIV Nef; trafficking

Indexed keywords

BONE MARROW STROMAL ANTIGEN 2; GLUTATHIONE TRANSFERASE; NEF PROTEIN; TRANSCRIPTION FACTOR AP 1; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CLATHRIN; NEF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 85050095137     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2018.07.004     Document Type: Article
Times cited : (38)

References (70)
  • 2
    • 84959080555 scopus 로고    scopus 로고
    • EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy
    • Barad, B.A., Echols, N., Wang, R.Y.R., Cheng, Y., DiMaio, F., Adams, P.D., Fraser, J.S., EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat. Methods 12 (2015), 943–946.
    • (2015) Nat. Methods , vol.12 , pp. 943-946
    • Barad, B.A.1    Echols, N.2    Wang, R.Y.R.3    Cheng, Y.4    DiMaio, F.5    Adams, P.D.6    Fraser, J.S.7
  • 3
    • 0035890324 scopus 로고    scopus 로고
    • Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs)
    • Boehm, M., Aguilar, R.C., Bonifacino, J.S., Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO J. 20 (2001), 6265–6276.
    • (2001) EMBO J. , vol.20 , pp. 6265-6276
    • Boehm, M.1    Aguilar, R.C.2    Bonifacino, J.S.3
  • 4
    • 84864023846 scopus 로고    scopus 로고
    • Feline tetherin is characterized by a short N-terminal region and is counteracted by the feline immunodeficiency virus envelope glycoprotein
    • Celestino, M., Calistri, A., Del Vecchio, C., Salata, C., Chiuppesi, F., Pistello, M., Borsetti, A., Palù G., Parolin, C., Feline tetherin is characterized by a short N-terminal region and is counteracted by the feline immunodeficiency virus envelope glycoprotein. J. Virol. 86 (2012), 6688–6700.
    • (2012) J. Virol. , vol.86 , pp. 6688-6700
    • Celestino, M.1    Calistri, A.2    Del Vecchio, C.3    Salata, C.4    Chiuppesi, F.5    Pistello, M.6    Borsetti, A.7    Palù, G.8    Parolin, C.9
  • 5
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • Chaudhuri, R., Lindwasser, O.W., Smith, W.J., Hurley, J.H., Bonifacino, J.S., Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J. Virol. 81 (2007), 3877–3890.
    • (2007) J. Virol. , vol.81 , pp. 3877-3890
    • Chaudhuri, R.1    Lindwasser, O.W.2    Smith, W.J.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 6
    • 85001093586 scopus 로고    scopus 로고
    • Antagonism of BST-2/Tetherin Is a Conserved Function of the Env Glycoprotein of Primary HIV-2 Isolates
    • Chen, C.Y., Shingai, M., Welbourn, S., Martin, M.A., Borrego, P., Taveira, N., Strebel, K., Antagonism of BST-2/Tetherin Is a Conserved Function of the Env Glycoprotein of Primary HIV-2 Isolates. J. Virol. 90 (2016), 11062–11074.
    • (2016) J. Virol. , vol.90 , pp. 11062-11074
    • Chen, C.Y.1    Shingai, M.2    Welbourn, S.3    Martin, M.A.4    Borrego, P.5    Taveira, N.6    Strebel, K.7
  • 7
    • 30844435721 scopus 로고    scopus 로고
    • HIV-1 Nef stabilizes AP-1 on membranes without inducing ARF1-independent de novo attachment
    • Coleman, S.H., Hitchin, D., Noviello, C.M., Guatelli, J.C., HIV-1 Nef stabilizes AP-1 on membranes without inducing ARF1-independent de novo attachment. Virology 345 (2006), 148–155.
    • (2006) Virology , vol.345 , pp. 148-155
    • Coleman, S.H.1    Hitchin, D.2    Noviello, C.M.3    Guatelli, J.C.4
  • 8
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • Collins, B.M., McCoy, A.J., Kent, H.M., Evans, P.R., Owen, D.J., Molecular architecture and functional model of the endocytic AP2 complex. Cell 109 (2002), 523–535.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 13
    • 34248198351 scopus 로고    scopus 로고
    • The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site
    • Doray, B., Lee, I., Knisely, J., Bu, G., Kornfeld, S., The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site. Mol. Biol. Cell 18 (2007), 1887–1896.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1887-1896
    • Doray, B.1    Lee, I.2    Knisely, J.3    Bu, G.4    Kornfeld, S.5
  • 14
    • 66149099203 scopus 로고    scopus 로고
    • Suppression of Tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network
    • Dubé M., Roy, B.B., Guiot-Guillain, P., Mercier, J., Binette, J., Leung, G., Cohen, E.A., Suppression of Tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network. J. Virol. 83 (2009), 4574–4590.
    • (2009) J. Virol. , vol.83 , pp. 4574-4590
    • Dubé, M.1    Roy, B.B.2    Guiot-Guillain, P.3    Mercier, J.4    Binette, J.5    Leung, G.6    Cohen, E.A.7
  • 16
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen, J.R., Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal. Chem. 81 (2009), 7870–7875.
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 17
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander, S.W., Hydrogen exchange and mass spectrometry: A historical perspective. J. Am. Soc. Mass Spectrom. 17 (2006), 1481–1489.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 18
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia, J.V., Miller, A.D., Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 350 (1991), 508–511.
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 23
    • 84946554121 scopus 로고    scopus 로고
    • Localized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes
    • Ilca, S.L., Kotecha, A., Sun, X., Poranen, M.M., Stuart, D.I., Huiskonen, J.T., Localized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes. Nat. Commun., 6, 2015, 8843.
    • (2015) Nat. Commun. , vol.6 , pp. 8843
    • Ilca, S.L.1    Kotecha, A.2    Sun, X.3    Poranen, M.M.4    Stuart, D.I.5    Huiskonen, J.T.6
  • 24
    • 77953884976 scopus 로고    scopus 로고
    • A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex
    • Jackson, L.P., Kelly, B.T., McCoy, A.J., Gaffry, T., James, L.C., Collins, B.M., Höning, S., Evans, P.R., Owen, D.J., A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell 141 (2010), 1220–1229.
    • (2010) Cell , vol.141 , pp. 1220-1229
    • Jackson, L.P.1    Kelly, B.T.2    McCoy, A.J.3    Gaffry, T.4    James, L.C.5    Collins, B.M.6    Höning, S.7    Evans, P.R.8    Owen, D.J.9
  • 27
    • 84899819636 scopus 로고    scopus 로고
    • Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1
    • Jia, X., Weber, E., Tokarev, A., Lewinski, M., Rizk, M., Suarez, M., Guatelli, J., Xiong, Y., Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1. eLife, 3, 2014, e02362.
    • (2014) eLife , vol.3 , pp. e02362
    • Jia, X.1    Weber, E.2    Tokarev, A.3    Lewinski, M.4    Rizk, M.5    Suarez, M.6    Guatelli, J.7    Xiong, Y.8
  • 30
    • 57749196168 scopus 로고    scopus 로고
    • A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex
    • Kelly, B.T., McCoy, A.J., Späte, K., Miller, S.E., Evans, P.R., Höning, S., Owen, D.J., A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex. Nature 456 (2008), 976–979.
    • (2008) Nature , vol.456 , pp. 976-979
    • Kelly, B.T.1    McCoy, A.J.2    Späte, K.3    Miller, S.E.4    Evans, P.R.5    Höning, S.6    Owen, D.J.7
  • 31
    • 85009208040 scopus 로고    scopus 로고
    • Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
    • Kimanius, D., Forsberg, B.O., Scheres, S.H.W., Lindahl, E., Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2. eLife, 5, 2016, e18722.
    • (2016) eLife , vol.5 , pp. e18722
    • Kimanius, D.1    Forsberg, B.O.2    Scheres, S.H.W.3    Lindahl, E.4
  • 32
    • 77958182786 scopus 로고    scopus 로고
    • Immune evasion and counteraction of restriction factors by HIV-1 and other primate lentiviruses
    • Kirchhoff, F., Immune evasion and counteraction of restriction factors by HIV-1 and other primate lentiviruses. Cell Host Microbe 8 (2010), 55–67.
    • (2010) Cell Host Microbe , vol.8 , pp. 55-67
    • Kirchhoff, F.1
  • 34
    • 84940771694 scopus 로고    scopus 로고
    • Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors
    • Kueck, T., Foster, T.L., Weinelt, J., Sumner, J.C., Pickering, S., Neil, S.J.D., Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors. PLoS Pathog, 11, 2015, e1005141.
    • (2015) PLoS Pathog , vol.11 , pp. e1005141
    • Kueck, T.1    Foster, T.L.2    Weinelt, J.3    Sumner, J.C.4    Pickering, S.5    Neil, S.J.D.6
  • 35
    • 84861209115 scopus 로고    scopus 로고
    • A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction
    • Kueck, T., Neil, S.J.D., A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction. PLoS Pathog, 8, 2012, e1002609.
    • (2012) PLoS Pathog , vol.8 , pp. e1002609
    • Kueck, T.1    Neil, S.J.D.2
  • 36
    • 70350266393 scopus 로고    scopus 로고
    • Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein
    • Le Tortorec, A., Neil, S.J., Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein. J. Virol. 83 (2009), 11966–11978.
    • (2009) J. Virol. , vol.83 , pp. 11966-11978
    • Le Tortorec, A.1    Neil, S.J.2
  • 37
    • 34548510349 scopus 로고    scopus 로고
    • HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2
    • Lubben, N.B., Sahlender, D.A., Motley, A.M., Lehner, P.J., Benaroch, P., Robinson, M.S., HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2. Mol. Biol. Cell 18 (2007), 3351–3365.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3351-3365
    • Lubben, N.B.1    Sahlender, D.A.2    Motley, A.M.3    Lehner, P.J.4    Benaroch, P.5    Robinson, M.S.6
  • 38
    • 84894577734 scopus 로고    scopus 로고
    • Feline immunodeficiency virus envelope glycoproteins antagonize tetherin through a distinctive mechanism that requires virion incorporation
    • Morrison, J.H., Guevara, R.B., Marcano, A.C., Saenz, D.T., Fadel, H.J., Rogstad, D.K., Poeschla, E.M., Feline immunodeficiency virus envelope glycoproteins antagonize tetherin through a distinctive mechanism that requires virion incorporation. J. Virol. 88 (2014), 3255–3272.
    • (2014) J. Virol. , vol.88 , pp. 3255-3272
    • Morrison, J.H.1    Guevara, R.B.2    Marcano, A.C.3    Saenz, D.T.4    Fadel, H.J.5    Rogstad, D.K.6    Poeschla, E.M.7
  • 39
    • 85029639811 scopus 로고    scopus 로고
    • Measuring the effects of particle orientation to improve the efficiency of electron cryomicroscopy
    • Naydenova, K., Russo, C.J., Measuring the effects of particle orientation to improve the efficiency of electron cryomicroscopy. Nat. Commun., 8, 2017, 629.
    • (2017) Nat. Commun. , vol.8 , pp. 629
    • Naydenova, K.1    Russo, C.J.2
  • 40
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil, S.J.D., Zang, T., Bieniasz, P.D., Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451 (2008), 425–430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Bieniasz, P.D.3
  • 41
    • 38349127341 scopus 로고    scopus 로고
    • Cooperative binding of the class I major histocompatibility complex cytoplasmic domain and human immunodeficiency virus type 1 Nef to the endosomal AP-1 complex via its mu subunit
    • Noviello, C.M., Benichou, S., Guatelli, J.C., Cooperative binding of the class I major histocompatibility complex cytoplasmic domain and human immunodeficiency virus type 1 Nef to the endosomal AP-1 complex via its mu subunit. J. Virol. 82 (2008), 1249–1258.
    • (2008) J. Virol. , vol.82 , pp. 1249-1258
    • Noviello, C.M.1    Benichou, S.2    Guatelli, J.C.3
  • 43
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D.J., Evans, P.R., A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282 (1998), 1327–1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 45
    • 85011645437 scopus 로고    scopus 로고
    • cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
    • Punjani, A., Rubinstein, J.L., Fleet, D.J., Brubaker, M.A., cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14 (2017), 290–296.
    • (2017) Nat. Methods , vol.14 , pp. 290-296
    • Punjani, A.1    Rubinstein, J.L.2    Fleet, D.J.3    Brubaker, M.A.4
  • 46
    • 84874033425 scopus 로고    scopus 로고
    • Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1
    • Ren, X., Farías, G.G., Canagarajah, B.J., Bonifacino, J.S., Hurley, J.H., Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell 152 (2013), 755–767.
    • (2013) Cell , vol.152 , pp. 755-767
    • Ren, X.1    Farías, G.G.2    Canagarajah, B.J.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 47
    • 84898733948 scopus 로고    scopus 로고
    • How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4
    • Ren, X., Park, S.Y., Bonifacino, J.S., Hurley, J.H., How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4. eLife, 3, 2014, e01754.
    • (2014) eLife , vol.3 , pp. e01754
    • Ren, X.1    Park, S.Y.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 48
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • Roeth, J.F., Williams, M., Kasper, M.R., Filzen, T.M., Collins, K.L., HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J. Cell Biol. 167 (2004), 903–913.
    • (2004) J. Cell Biol. , vol.167 , pp. 903-913
    • Roeth, J.F.1    Williams, M.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 51
    • 77951898650 scopus 로고    scopus 로고
    • Tetherin: holding on and letting go
    • Sauter, D., Specht, A., Kirchhoff, F., Tetherin: holding on and letting go. Cell 141 (2010), 392–398.
    • (2010) Cell , vol.141 , pp. 392-398
    • Sauter, D.1    Specht, A.2    Kirchhoff, F.3
  • 54
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H.W., RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180 (2012), 519–530.
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 55
    • 84855187526 scopus 로고    scopus 로고
    • HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction
    • e00036–e11
    • Schmidt, S., Fritz, J.V., Bitzegeio, J., Fackler, O.T., Keppler, O.T., HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction. MBio, 2, 2011 e00036–e11.
    • (2011) MBio , vol.2
    • Schmidt, S.1    Fritz, J.V.2    Bitzegeio, J.3    Fackler, O.T.4    Keppler, O.T.5
  • 56
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz, O., Maréchal, V., Le Gall, S., Lemonnier, F., Heard, J.M., Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat. Med. 2 (1996), 338–342.
    • (1996) Nat. Med. , vol.2 , pp. 338-342
    • Schwartz, O.1    Maréchal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 57
    • 84884769542 scopus 로고    scopus 로고
    • Tetherin/BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis
    • Serra-Moreno, R., Zimmermann, K., Stern, L.J., Evans, D.T., Tetherin/BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis. PLoS Pathog, 9, 2013, e1003487.
    • (2013) PLoS Pathog , vol.9 , pp. e1003487
    • Serra-Moreno, R.1    Zimmermann, K.2    Stern, L.J.3    Evans, D.T.4
  • 58
    • 84944755225 scopus 로고    scopus 로고
    • HIV-1 Nef hijacks clathrin coats by stabilizing AP-1:Arf1 polygons
    • Shen, Q.T., Ren, X., Zhang, R., Lee, I.H., Hurley, J.H., HIV-1 Nef hijacks clathrin coats by stabilizing AP-1:Arf1 polygons. Science, 350, 2015, aac5137.
    • (2015) Science , vol.350 , pp. aac5137
    • Shen, Q.T.1    Ren, X.2    Zhang, R.3    Lee, I.H.4    Hurley, J.H.5
  • 59
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes, M.A., Rothman, J.E., The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73 (1993), 999–1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 61
    • 84862636093 scopus 로고    scopus 로고
    • Misdirection of membrane trafficking by HIV-1 Vpu and Nef: Keys to viral virulence and persistence
    • Tokarev, A., Guatelli, J., Misdirection of membrane trafficking by HIV-1 Vpu and Nef: Keys to viral virulence and persistence. Cell. Logist. 1 (2011), 90–102.
    • (2011) Cell. Logist. , vol.1 , pp. 90-102
    • Tokarev, A.1    Guatelli, J.2
  • 63
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • Traub, L.M., Ostrom, J.A., Kornfeld, S., Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123 (1993), 561–573.
    • (1993) J. Cell Biol. , vol.123 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 64
    • 84944110470 scopus 로고    scopus 로고
    • SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef
    • Usami, Y., Wu, Y., Göttlinger, H.G., SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef. Nature 526 (2015), 218–223.
    • (2015) Nature , vol.526 , pp. 218-223
    • Usami, Y.1    Wu, Y.2    Göttlinger, H.G.3
  • 65
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme, N., Goff, D., Katsura, C., Jorgenson, R.L., Mitchell, R., Johnson, M.C., Stephens, E.B., Guatelli, J., The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3 (2008), 245–252.
    • (2008) Cell Host Microbe , vol.3 , pp. 245-252
    • Van Damme, N.1    Goff, D.2    Katsura, C.3    Jorgenson, R.L.4    Mitchell, R.5    Johnson, M.C.6    Stephens, E.B.7    Guatelli, J.8
  • 68
    • 79958024908 scopus 로고    scopus 로고
    • SIV Nef proteins recruit the AP-2 complex to antagonize tetherin and facilitate virion release
    • Zhang, F.W., Landford, W.N., Ng, M., McNatt, M.W., Bieniasz, P.D., Hatziioannou, T., SIV Nef proteins recruit the AP-2 complex to antagonize tetherin and facilitate virion release. PLoS Pathog, 7, 2011, e1002039.
    • (2011) PLoS Pathog , vol.7 , pp. e1002039
    • Zhang, F.W.1    Landford, W.N.2    Ng, M.3    McNatt, M.W.4    Bieniasz, P.D.5    Hatziioannou, T.6
  • 69
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • Zhang, K., Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193 (2016), 1–12.
    • (2016) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 70
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S.Q., Palovcak, E., Armache, J.P., Verba, K.A., Cheng, Y., Agard, D.A., MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14 (2017), 331–332.
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1    Palovcak, E.2    Armache, J.P.3    Verba, K.A.4    Cheng, Y.5    Agard, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.