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Volumn 16, Issue 5, 2014, Pages 627-638

Structural insight into HIV-1 restriction by MxB

Author keywords

[No Author keywords available]

Indexed keywords

MYXOVIRUS RESISTANCE PROTEIN; MX2 PROTEIN, HUMAN;

EID: 84911448433     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2014.09.021     Document Type: Article
Times cited : (105)

References (45)
  • 3
    • 84897965284 scopus 로고    scopus 로고
    • HIV-1 uncoating: Connection to nuclear entry and regulation by host proteins
    • Z. Ambrose, and C. Aiken HIV-1 uncoating: connection to nuclear entry and regulation by host proteins Virology 454-455 2014 371 379
    • (2014) Virology , vol.454-455 , pp. 371-379
    • Ambrose, Z.1    Aiken, C.2
  • 5
    • 0000192748 scopus 로고
    • An automated-system for micro-batch protein crystallization and screening
    • N.E. Chayen, P.D.S. Stewart, D.L. Maeder, and D.M. Blow An automated-system for micro-batch protein crystallization and screening J. Appl. Cryst. 23 1990 297 302
    • (1990) J. Appl. Cryst. , vol.23 , pp. 297-302
    • Chayen, N.E.1    Stewart, P.D.S.2    Maeder, D.L.3    Blow, D.M.4
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 79952054310 scopus 로고    scopus 로고
    • Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module
    • O. Daumke, S. Gao, A. von der Malsburg, O. Haller, and G. Kochs Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module Small GTPases 1 2010 62 64
    • (2010) Small GTPases , vol.1 , pp. 62-64
    • Daumke, O.1    Gao, S.2    Von Der Malsburg, A.3    Haller, O.4    Kochs, G.5
  • 8
    • 0033527650 scopus 로고    scopus 로고
    • Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization
    • C. Di Paolo, H.P. Hefti, M. Meli, H. Landis, and J. Pavlovic Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization J. Biol. Chem. 274 1999 32071 32078
    • (1999) J. Biol. Chem. , vol.274 , pp. 32071-32078
    • Di Paolo, C.1    Hefti, H.P.2    Meli, M.3    Landis, H.4    Pavlovic, J.5
  • 12
    • 80755153638 scopus 로고    scopus 로고
    • Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function
    • S. Gao, A. von der Malsburg, A. Dick, K. Faelber, G.F. Schröder, O. Haller, G. Kochs, and O. Daumke Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function Immunity 35 2011 514 525
    • (2011) Immunity , vol.35 , pp. 514-525
    • Gao, S.1    Von Der Malsburg, A.2    Dick, A.3    Faelber, K.4    Schröder, G.F.5    Haller, O.6    Kochs, G.7    Daumke, O.8
  • 14
    • 84904861293 scopus 로고    scopus 로고
    • Transfer of the amino-terminal nuclear envelope targeting domain of human MX2 converts MX1 into an HIV-1 resistance factor
    • C. Goujon, O. Moncorgé, H. Bauby, T. Doyle, W.S. Barclay, and M.H. Malim Transfer of the amino-terminal nuclear envelope targeting domain of human MX2 converts MX1 into an HIV-1 resistance factor J. Virol. 88 2014 9017 9026
    • (2014) J. Virol. , vol.88 , pp. 9017-9026
    • Goujon, C.1    Moncorgé, O.2    Bauby, H.3    Doyle, T.4    Barclay, W.S.5    Malim, M.H.6
  • 15
    • 78651515640 scopus 로고    scopus 로고
    • Human MxA protein: An interferon-induced dynamin-like GTPase with broad antiviral activity
    • O. Haller, and G. Kochs Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity J. Interferon Cytokine Res. 31 2011 79 87
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 79-87
    • Haller, O.1    Kochs, G.2
  • 16
    • 77956268333 scopus 로고    scopus 로고
    • Dynamin-like MxA GTPase: Structural insights into oligomerization and implications for antiviral activity
    • O. Haller, S. Gao, A. von der Malsburg, O. Daumke, and G. Kochs Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity J. Biol. Chem. 285 2010 28419 28424
    • (2010) J. Biol. Chem. , vol.285 , pp. 28419-28424
    • Haller, O.1    Gao, S.2    Von Der Malsburg, A.3    Daumke, O.4    Kochs, G.5
  • 17
    • 0032775260 scopus 로고    scopus 로고
    • Human MxA protein protects mice lacking a functional alpha/beta interferon system against la crosse virus and other lethal viral infections
    • H.P. Hefti, M. Frese, H. Landis, C. Di Paolo, A. Aguzzi, O. Haller, and J. Pavlovic Human MxA protein protects mice lacking a functional alpha/beta interferon system against La crosse virus and other lethal viral infections J. Virol. 73 1999 6984 6991
    • (1999) J. Virol. , vol.73 , pp. 6984-6991
    • Hefti, H.P.1    Frese, M.2    Landis, H.3    Di Paolo, C.4    Aguzzi, A.5    Haller, O.6    Pavlovic, J.7
  • 18
    • 84893716884 scopus 로고    scopus 로고
    • In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects
    • M.S. Henning, B.N. Dubose, M.J. Burse, C. Aiken, and M. Yamashita In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects PLoS Pathog. 10 2014 e1003868
    • (2014) PLoS Pathog. , vol.10 , pp. 1003868
    • Henning, M.S.1    Dubose, B.N.2    Burse, M.J.3    Aiken, C.4    Yamashita, M.5
  • 20
    • 2942676463 scopus 로고    scopus 로고
    • Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB
    • M.C. King, G. Raposo, and M.A. Lemmon Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB Proc. Natl. Acad. Sci. USA 101 2004 8957 8962
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8957-8962
    • King, M.C.1    Raposo, G.2    Lemmon, M.A.3
  • 21
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae)
    • G. Kochs, and O. Haller GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae) J. Biol. Chem. 274 1999 4370 4376
    • (1999) J. Biol. Chem. , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 22
    • 0033514947 scopus 로고    scopus 로고
    • Interferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids
    • G. Kochs, and O. Haller Interferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids Proc. Natl. Acad. Sci. USA 96 1999 2082 2086
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2082-2086
    • Kochs, G.1    Haller, O.2
  • 23
    • 0037134425 scopus 로고    scopus 로고
    • Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers
    • G. Kochs, M. Haener, U. Aebi, and O. Haller Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers J. Biol. Chem. 277 2002 14172 14176
    • (2002) J. Biol. Chem. , vol.277 , pp. 14172-14176
    • Kochs, G.1    Haener, M.2    Aebi, U.3    Haller, O.4
  • 24
    • 0037022575 scopus 로고    scopus 로고
    • Antivirally active MxA protein sequesters la Crosse virus nucleocapsid protein into perinuclear complexes
    • G. Kochs, C. Janzen, H. Hohenberg, and O. Haller Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes Proc. Natl. Acad. Sci. USA 99 2002 3153 3158
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3153-3158
    • Kochs, G.1    Janzen, C.2    Hohenberg, H.3    Haller, O.4
  • 26
    • 84878285234 scopus 로고    scopus 로고
    • A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallization via compound-mediated dimerization
    • C.T. Lemke, S. Titolo, N. Goudreau, A.M. Faucher, S.W. Mason, and P. Bonneau A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallization via compound-mediated dimerization Acta Crystallogr. D Biol. Crystallogr. 69 2013 1115 1123
    • (2013) Acta Crystallogr. D Biol. Crystallogr. , vol.69 , pp. 1115-1123
    • Lemke, C.T.1    Titolo, S.2    Goudreau, N.3    Faucher, A.M.4    Mason, S.W.5    Bonneau, P.6
  • 27
    • 84893662498 scopus 로고    scopus 로고
    • Electron density sharpening as a general technique in crystallographic studies
    • C. Liu, and Y. Xiong Electron density sharpening as a general technique in crystallographic studies J. Mol. Biol. 426 2014 980 993
    • (2014) J. Mol. Biol. , vol.426 , pp. 980-993
    • Liu, C.1    Xiong, Y.2
  • 29
    • 84885138769 scopus 로고    scopus 로고
    • Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes
    • K.A. Matreyek, and A. Engelman Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes Viruses 5 2013 2483 2511
    • (2013) Viruses , vol.5 , pp. 2483-2511
    • Matreyek, K.A.1    Engelman, A.2
  • 30
    • 84885090088 scopus 로고    scopus 로고
    • Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity
    • K.A. Matreyek, S.S. Yücel, X. Li, and A. Engelman Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity PLoS Pathog. 9 2013 e1003693
    • (2013) PLoS Pathog. , vol.9 , pp. 1003693
    • Matreyek, K.A.1    Yücel, S.S.2    Li, X.3    Engelman, A.4
  • 32
    • 0031464185 scopus 로고    scopus 로고
    • Nuclear cotransport mechanism of cytoplasmic human MxB protein
    • K. Melén, and I. Julkunen Nuclear cotransport mechanism of cytoplasmic human MxB protein J. Biol. Chem. 272 1997 32353 32359
    • (1997) J. Biol. Chem. , vol.272 , pp. 32353-32359
    • Melén, K.1    Julkunen, I.2
  • 33
    • 0027101757 scopus 로고
    • Interferon-induced Mx proteins form oligomers and contain a putative leucine zipper
    • K. Melén, T. Ronni, B. Broni, R.M. Krug, C.H. von Bonsdorff, and I. Julkunen Interferon-induced Mx proteins form oligomers and contain a putative leucine zipper J. Biol. Chem. 267 1992 25898 25907
    • (1992) J. Biol. Chem. , vol.267 , pp. 25898-25907
    • Melén, K.1    Ronni, T.2    Broni, B.3    Krug, R.M.4    Von Bonsdorff, C.H.5    Julkunen, I.6
  • 34
    • 0029813449 scopus 로고    scopus 로고
    • Human MxB protein, an interferon-alpha-inducible GTPase, contains a nuclear targeting signal and is localized in the heterochromatin region beneath the nuclear envelope
    • K. Melén, P. Keskinen, T. Ronni, T. Sareneva, K. Lounatmaa, and I. Julkunen Human MxB protein, an interferon-alpha-inducible GTPase, contains a nuclear targeting signal and is localized in the heterochromatin region beneath the nuclear envelope J. Biol. Chem. 271 1996 23478 23486
    • (1996) J. Biol. Chem. , vol.271 , pp. 23478-23486
    • Melén, K.1    Keskinen, P.2    Ronni, T.3    Sareneva, T.4    Lounatmaa, K.5    Julkunen, I.6
  • 36
    • 0027722486 scopus 로고
    • Mx proteins: GTPases involved in the interferon-induced antiviral state
    • discussion 243-247
    • J. Pavlovic, A. Schröder, A. Blank, F. Pitossi, and P. Staeheli Mx proteins: GTPases involved in the interferon-induced antiviral state Ciba Found. Symp. 176 1993 233 243 discussion 243-247
    • (1993) Ciba Found. Symp. , vol.176 , pp. 233-243
    • Pavlovic, J.1    Schröder, A.2    Blank, A.3    Pitossi, F.4    Staeheli, P.5
  • 39
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • B. Prakash, G.J. Praefcke, L. Renault, A. Wittinghofer, and C. Herrmann Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins Nature 403 2000 567 571
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 41
    • 4744357399 scopus 로고    scopus 로고
    • Missorting of LaCrosse virus nucleocapsid protein by the interferon-induced MxA GTPase involves smooth ER membranes
    • M. Reichelt, S. Stertz, J. Krijnse-Locker, O. Haller, and G. Kochs Missorting of LaCrosse virus nucleocapsid protein by the interferon-induced MxA GTPase involves smooth ER membranes Traffic 5 2004 772 784
    • (2004) Traffic , vol.5 , pp. 772-784
    • Reichelt, M.1    Stertz, S.2    Krijnse-Locker, J.3    Haller, O.4    Kochs, G.5
  • 43
    • 0029036975 scopus 로고
    • Unexpected structural requirements for GTPase activity of the interferon-induced MxA protein
    • M. Schwemmle, M.F. Richter, C. Herrmann, N. Nassar, and P. Staeheli Unexpected structural requirements for GTPase activity of the interferon-induced MxA protein J. Biol. Chem. 270 1995 13518 13523
    • (1995) J. Biol. Chem. , vol.270 , pp. 13518-13523
    • Schwemmle, M.1    Richter, M.F.2    Herrmann, C.3    Nassar, N.4    Staeheli, P.5
  • 45
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • A. Vagin, and A. Teplyakov An approach to multi-copy search in molecular replacement Acta Crystallogr. D Biol. Crystallogr. 56 2000 1622 1624
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2


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