메뉴 건너뛰기




Volumn 12, Issue 2, 2016, Pages

Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike

Author keywords

[No Author keywords available]

Indexed keywords

LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; RIBONUCLEOPROTEIN; VIRUS SPIKE PROTEIN; GLYCOPROTEIN; LAMP1 PROTEIN, HUMAN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; MULTIPROTEIN COMPLEX; PROTEIN BINDING; SIGNAL PEPTIDE; VIRUS ENVELOPE PROTEIN;

EID: 84959486075     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005418     Document Type: Article
Times cited : (105)

References (54)
  • 2
    • 0037434923 scopus 로고    scopus 로고
    • Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length
    • 12633879, .;:–
    • Eichler R, Lenz O, Strecker T, Garten W, Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length. FEBS Lett. 2003;538: 203–206. 12633879
    • (2003) FEBS Lett , vol.538 , pp. 203-206
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Garten, W.4
  • 3
    • 84055179004 scopus 로고    scopus 로고
    • X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation
    • ..;:–
    • Igonet S, Vaney M-C, Vonhrein C, Bricogne G, Stura EA, Hengartner H, et al. X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation. P Natl Acad Sci Usa. 2011;108: 19967–19972.
    • (2011) P Natl Acad Sci Usa , vol.108 , pp. 19967-19972
    • Igonet, S.1    Vaney, M.-C.2    Vonhrein, C.3    Bricogne, G.4    Stura, E.A.5    Hengartner, H.6
  • 4
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • .;:–
    • Lenz O, Meulen ter J, Klenk HD, Seidah NG, Garten W, The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. P Natl Acad Sci Usa. 2001;98: 12701–12705.
    • (2001) P Natl Acad Sci Usa , vol.98 , pp. 12701-12705
    • Lenz, O.1    Meulen ter, J.2    Klenk, H.D.3    Seidah, N.G.4    Garten, W.5
  • 5
    • 84887199856 scopus 로고    scopus 로고
    • Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 postfusion architecture with extensive glycosylation
    • 24049182, .;:–
    • Parsy M-L, Harlos K, Huiskonen JT, Bowden TA, Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 postfusion architecture with extensive glycosylation. J Virol. 2013;87: 13070–13075. doi: 10.1128/JVI.02298-1324049182
    • (2013) J Virol , vol.87 , pp. 13070-13075
    • Parsy, M.-L.1    Harlos, K.2    Huiskonen, J.T.3    Bowden, T.A.4
  • 6
    • 0346242739 scopus 로고    scopus 로고
    • Identification of Lassa virus glycoprotein signal peptide as a trans-acting maturation factor
    • 14555961, .;:–
    • Eichler R, Lenz O, Strecker T, Eickmann M, Klenk HD, Garten W, Identification of Lassa virus glycoprotein signal peptide as a trans-acting maturation factor. EMBO Rep. 2003;4: 1084–1088. 14555961
    • (2003) EMBO Rep , vol.4 , pp. 1084-1088
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 7
    • 4544266361 scopus 로고    scopus 로고
    • The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex
    • 15367645, .;:–
    • York J, Romanowski V, Lu M, Nunberg JH, The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex. J Virol. 2004;78: 10783–10792. 15367645
    • (2004) J Virol , vol.78 , pp. 10783-10792
    • York, J.1    Romanowski, V.2    Lu, M.3    Nunberg, J.H.4
  • 8
    • 84920911910 scopus 로고    scopus 로고
    • Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization
    • 25352624, .;:
    • Bederka LH, Bonhomme CJ, Ling EL, Buchmeier MJ, Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization. MBio. 2014;5: e02063. doi: 10.1128/mBio.02063-1425352624
    • (2014) MBio , vol.5 , pp. e02063
    • Bederka, L.H.1    Bonhomme, C.J.2    Ling, E.L.3    Buchmeier, M.J.4
  • 9
    • 73849123124 scopus 로고    scopus 로고
    • Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication
    • 19889753, .;:–
    • Schlie K, Maisa A, Lennartz F, Ströher U, Garten W, Strecker T, Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication. J Virol. 2010;84: 983–992. doi: 10.1128/JVI.02039-0919889753
    • (2010) J Virol , vol.84 , pp. 983-992
    • Schlie, K.1    Maisa, A.2    Lennartz, F.3    Ströher, U.4    Garten, W.5    Strecker, T.6
  • 11
    • 84903289135 scopus 로고    scopus 로고
    • Lassa virus entry requires a trigger-induced receptor switch
    • 24970085, ..;:–
    • Jae LT, Raaben M, Herbert AS, Kuehne AI, Wirchnianski AS, Soh TK, et al. Lassa virus entry requires a trigger-induced receptor switch. Science. 2014;344: 1506–1510. doi: 10.1126/science.125248024970085
    • (2014) Science , vol.344 , pp. 1506-1510
    • Jae, L.T.1    Raaben, M.2    Herbert, A.S.3    Kuehne, A.I.4    Wirchnianski, A.S.5    Soh, T.K.6
  • 12
    • 67749096150 scopus 로고    scopus 로고
    • Unusual molecular architecture of the machupo virus attachment glycoprotein
    • 19494008, ..;:–
    • Bowden TA, Crispin M, Graham SC, Harvey DJ, Grimes JM, Jones EY, et al. Unusual molecular architecture of the machupo virus attachment glycoprotein. J Virol. 2009;83: 8259–8265. doi: 10.1128/JVI.00761-0919494008
    • (2009) J Virol , vol.83 , pp. 8259-8265
    • Bowden, T.A.1    Crispin, M.2    Graham, S.C.3    Harvey, D.J.4    Grimes, J.M.5    Jones, E.Y.6
  • 13
    • 77950517857 scopus 로고    scopus 로고
    • Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses
    • 20208545, .;:–
    • Abraham J, Corbett KD, Farzan M, Choe H, Harrison SC, Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses. Nat Struct Mol Biol. 2010;17: 438–444. doi: 10.1038/nsmb.177220208545
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 438-444
    • Abraham, J.1    Corbett, K.D.2    Farzan, M.3    Choe, H.4    Harrison, S.C.5
  • 14
    • 33744935523 scopus 로고    scopus 로고
    • Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins
    • 16731928, .;:–
    • Eschli B, Quirin K, Wepf A, Weber J, Zinkernagel R, Hengartner H, Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins. J Virol. 2006;80: 5897–5907. 16731928
    • (2006) J Virol , vol.80 , pp. 5897-5907
    • Eschli, B.1    Quirin, K.2    Wepf, A.3    Weber, J.4    Zinkernagel, R.5    Hengartner, H.6
  • 15
    • 14744278960 scopus 로고    scopus 로고
    • Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis
    • 15731275, .;:–
    • Neuman BW, Adair BD, Burns JW, Milligan RA, Buchmeier MJ, Yeager M, Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis. J Virol. 2005;79: 3822–3830. 15731275
    • (2005) J Virol , vol.79 , pp. 3822-3830
    • Neuman, B.W.1    Adair, B.D.2    Burns, J.W.3    Milligan, R.A.4    Buchmeier, M.J.5    Yeager, M.6
  • 16
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • 24179160, ..;:–
    • Lyumkis D, Julien J-P, de Val N, Cupo A, Potter CS, Klasse P-J, et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science. 2013;342: 1484–1490. doi: 10.1126/science.124562724179160
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.-P.2    de Val, N.3    Cupo, A.4    Potter, C.S.5    Klasse, P.-J.6
  • 17
    • 84906346444 scopus 로고    scopus 로고
    • Spatial localization of the ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography
    • 25008940, ..;:–
    • Tran EEH, Simmons JA, Bartesaghi A, Shoemaker CJ, Nelson E, White JM, et al. Spatial localization of the ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography. J Virol. 2014;88: 10958–10962. doi: 10.1128/JVI.00870-1425008940
    • (2014) J Virol , vol.88 , pp. 10958-10962
    • Tran, E.E.H.1    Simmons, J.A.2    Bartesaghi, A.3    Shoemaker, C.J.4    Nelson, E.5    White, J.M.6
  • 18
    • 66149085621 scopus 로고    scopus 로고
    • Intersubunit interactions modulate pH-induced activation of membrane fusion by the Junin virus envelope glycoprotein GPC
    • 19224989, .;:–
    • York J, Nunberg JH, Intersubunit interactions modulate pH-induced activation of membrane fusion by the Junin virus envelope glycoprotein GPC. J Virol. 2009;83: 4121–4126. doi: 10.1128/JVI.02410-0819224989
    • (2009) J Virol , vol.83 , pp. 4121-4126
    • York, J.1    Nunberg, J.H.2
  • 19
    • 36048983549 scopus 로고    scopus 로고
    • Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity
    • 17804515, .;:–
    • Schrempf S, Froeschke M, Giroglou T, Laer von D, Dobberstein B, Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity. J Virol. 2007;81: 12515–12524. 17804515
    • (2007) J Virol , vol.81 , pp. 12515-12524
    • Schrempf, S.1    Froeschke, M.2    Giroglou, T.3    Laer von, D.4    Dobberstein, B.5
  • 20
    • 1842478088 scopus 로고    scopus 로고
    • Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region
    • 14709548, .;:–
    • Eichler R, Lenz O, Strecker T, Eickmann M, Klenk HD, Garten W, Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region. J Biol Chem. 2004;279: 12293–12299. 14709548
    • (2004) J Biol Chem , vol.279 , pp. 12293-12299
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 21
    • 34247118403 scopus 로고    scopus 로고
    • Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex
    • 17267481, .;:–
    • Agnihothram SS, York J, Trahey M, Nunberg JH, Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex. J Virol. 2007;81: 4331–4337. 17267481
    • (2007) J Virol , vol.81 , pp. 4331-4337
    • Agnihothram, S.S.1    York, J.2    Trahey, M.3    Nunberg, J.H.4
  • 22
    • 77949364631 scopus 로고    scopus 로고
    • Viral protein determinants of Lassa virus entry and release from polarized epithelial cells
    • 20071570, .;:–
    • Schlie K, Maisa A, Freiberg F, Groseth A, Strecker T, Garten W, Viral protein determinants of Lassa virus entry and release from polarized epithelial cells. J Virol. 2010;84: 3178–3188. doi: 10.1128/JVI.02240-0920071570
    • (2010) J Virol , vol.84 , pp. 3178-3188
    • Schlie, K.1    Maisa, A.2    Freiberg, F.3    Groseth, A.4    Strecker, T.5    Garten, W.6
  • 23
    • 84870595089 scopus 로고    scopus 로고
    • Multifunctional nature of the arenavirus RING finger protein Z
    • 23202512, .;:–
    • Fehling SK, Lennartz F, Strecker T, Multifunctional nature of the arenavirus RING finger protein Z. Viruses. 2012;4: 2973–3011. doi: 10.3390/v411297323202512
    • (2012) Viruses , vol.4 , pp. 2973-3011
    • Fehling, S.K.1    Lennartz, F.2    Strecker, T.3
  • 24
    • 34548170431 scopus 로고    scopus 로고
    • Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
    • 17581989, .;:–
    • Capul AA, Perez M, Burke E, Kunz S, Buchmeier MJ, la Torre de JC, Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains. J Virol. 2007;81: 9451–9460. 17581989
    • (2007) J Virol , vol.81 , pp. 9451-9460
    • Capul, A.A.1    Perez, M.2    Burke, E.3    Kunz, S.4    Buchmeier, M.J.5    la Torre de, J.C.6
  • 25
    • 0032509177 scopus 로고    scopus 로고
    • Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus
    • 9851928, ..;:–
    • Cao W, Henry MD, Borrow P, Yamada H, Elder JH, Ravkov EV, et al. Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. Science. 1998;282: 2079–2081. 9851928
    • (1998) Science , vol.282 , pp. 2079-2081
    • Cao, W.1    Henry, M.D.2    Borrow, P.3    Yamada, H.4    Elder, J.H.5    Ravkov, E.V.6
  • 26
    • 84857081598 scopus 로고    scopus 로고
    • Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry
    • 22156524, .;:–
    • Shimojima M, Ströher U, Ebihara H, Feldmann H, Kawaoka Y, Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry. J Virol. 2012;86: 2067–2078. doi: 10.1128/JVI.06451-1122156524
    • (2012) J Virol , vol.86 , pp. 2067-2078
    • Shimojima, M.1    Ströher, U.2    Ebihara, H.3    Feldmann, H.4    Kawaoka, Y.5
  • 27
    • 84886896855 scopus 로고    scopus 로고
    • Role of DC-SIGN in Lassa virus entry into human dendritic cells
    • 23966408, .;:–
    • Goncalves A-R, Moraz M-L, Pasquato A, Helenius A, Lozach P-Y, Kunz S, Role of DC-SIGN in Lassa virus entry into human dendritic cells. J Virol. 2013;87: 11504–11515. doi: 10.1128/JVI.01893-1323966408
    • (2013) J Virol , vol.87 , pp. 11504-11515
    • Goncalves, A.-R.1    Moraz, M.-L.2    Pasquato, A.3    Helenius, A.4    Lozach, P.-Y.5    Kunz, S.6
  • 28
    • 34547585371 scopus 로고    scopus 로고
    • Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity
    • 17622638, .;:–
    • Klewitz C, Klenk HD, Meulen ter J, Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity. J Gen Virol. 2007;88: 2320–2328. 17622638
    • (2007) J Gen Virol , vol.88 , pp. 2320-2328
    • Klewitz, C.1    Klenk, H.D.2    Meulen ter, J.3
  • 29
    • 84864761447 scopus 로고    scopus 로고
    • Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx
    • 22809326, .;:
    • Wilke S, Krausze J, Büssow K, Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx. BMC Biol. 2012;10: 62. doi: 10.1186/1741-7007-10-6222809326
    • (2012) BMC Biol , vol.10 , pp. 62
    • Wilke, S.1    Krausze, J.2    Büssow, K.3
  • 30
    • 79959923466 scopus 로고    scopus 로고
    • Cells under siege: viral glycoprotein interactions at the cell surface
    • 21440638, .;:–
    • Bowden TA, Jones EY, Stuart DI, Cells under siege: viral glycoprotein interactions at the cell surface. J Struct Biol. 2011;175: 120–126. doi: 10.1016/j.jsb.2011.03.01621440638
    • (2011) J Struct Biol , vol.175 , pp. 120-126
    • Bowden, T.A.1    Jones, E.Y.2    Stuart, D.I.3
  • 31
    • 80053437934 scopus 로고    scopus 로고
    • Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport
    • 21931550, .;:
    • Pasqual G, Rojek JM, Masin M, Chatton J-Y, Kunz S, Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport. PLoS Pathog. 2011;7: e1002232. doi: 10.1371/journal.ppat.100223221931550
    • (2011) PLoS Pathog , vol.7 , pp. e1002232
    • Pasqual, G.1    Rojek, J.M.2    Masin, M.3    Chatton, J.-Y.4    Kunz, S.5
  • 32
    • 77957993361 scopus 로고    scopus 로고
    • Lassa virus-like particles displaying all major immunological determinants as a vaccine candidate for Lassa hemorrhagic fever
    • 20961433, ..;:
    • Branco LM, Grove JN, Geske FJ, Boisen ML, Muncy IJ, Magliato SA, et al. Lassa virus-like particles displaying all major immunological determinants as a vaccine candidate for Lassa hemorrhagic fever. Virol J. 2010;7: 279. doi: 10.1186/1743-422X-7-27920961433
    • (2010) Virol J , vol.7 , pp. 279
    • Branco, L.M.1    Grove, J.N.2    Geske, F.J.3    Boisen, M.L.4    Muncy, I.J.5    Magliato, S.A.6
  • 33
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • 21124458, ..;:–
    • Voss JE, Vaney M-C, Duquerroy S, Vonrhein C, Girard-Blanc C, Crublet E, et al. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature. 2010;468: 709–712. doi: 10.1038/nature0955521124458
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1    Vaney, M.-C.2    Duquerroy, S.3    Vonrhein, C.4    Girard-Blanc, C.5    Crublet, E.6
  • 34
    • 84863583991 scopus 로고    scopus 로고
    • Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion
    • 22438561, .;:–
    • Messina EL, York J, Nunberg JH, Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion. J Virol. 2012;86: 6138–6145. doi: 10.1128/JVI.07241-1122438561
    • (2012) J Virol , vol.86 , pp. 6138-6145
    • Messina, E.L.1    York, J.2    Nunberg, J.H.3
  • 35
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • 18596815, .;:–
    • Harrison SC, Viral membrane fusion. Nat Struct Mol Biol. 2008;15: 690–698. doi: 10.1038/nsmb.145618596815
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1
  • 36
    • 84886893256 scopus 로고    scopus 로고
    • Isolation, identification, and characterization of novel arenaviruses, the etiological agents of boid inclusion body disease
    • 23926354, ..;:–
    • Hetzel U, Sironen T, Laurinmäki P, Liljeroos L, Patjas A, Henttonen H, et al. Isolation, identification, and characterization of novel arenaviruses, the etiological agents of boid inclusion body disease. J Virol. 2013;87: 10918–10935. doi: 10.1128/JVI.01123-1323926354
    • (2013) J Virol , vol.87 , pp. 10918-10935
    • Hetzel, U.1    Sironen, T.2    Laurinmäki, P.3    Liljeroos, L.4    Patjas, A.5    Henttonen, H.6
  • 37
    • 3142545672 scopus 로고    scopus 로고
    • The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor
    • 11208257, .;:
    • Gallaher WR, DiSimone C, Buchmeier MJ, The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor. BMC Microbiol. 2001;1: 1. 11208257
    • (2001) BMC Microbiol , vol.1 , pp. 1
    • Gallaher, W.R.1    DiSimone, C.2    Buchmeier, M.J.3
  • 38
    • 0034466514 scopus 로고    scopus 로고
    • Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein
    • 11070044, .;:–
    • Lenz O, Meulen ter J, Feldmann H, Klenk HD, Garten W, Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein. J Virol. 2000;74: 11418–11421. 11070044
    • (2000) J Virol , vol.74 , pp. 11418-11421
    • Lenz, O.1    Meulen ter, J.2    Feldmann, H.3    Klenk, H.D.4    Garten, W.5
  • 39
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • 17001101, .;:–
    • Aricescu AR, Lu W, Jones EY, A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr D Biol Crystallogr. 2006;62: 1243–1250. 17001101
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 40
    • 0025076063 scopus 로고
    • Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I
    • 2144287, .;:–
    • Elbein AD, Tropea JE, Mitchell M, Kaushal GP, Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I. J Biol Chem. 1990;265: 15599–15605. 2144287
    • (1990) J Biol Chem , vol.265 , pp. 15599-15605
    • Elbein, A.D.1    Tropea, J.E.2    Mitchell, M.3    Kaushal, G.P.4
  • 41
    • 52149100074 scopus 로고    scopus 로고
    • An improved cryogen for plunge freezing
    • 18793481, .;:–
    • Tivol WF, Briegel A, Jensen GJ, An improved cryogen for plunge freezing. Microsc Microanal. 2008;14: 375–379. doi: 10.1017/S143192760808078118793481
    • (2008) Microsc Microanal , vol.14 , pp. 375-379
    • Tivol, W.F.1    Briegel, A.2    Jensen, G.J.3
  • 42
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • 16182563, .;:–. 7
    • Mastronarde DN, Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol. 2005;152: 36–51. 7 16182563
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 43
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • 23644547, ..;:–
    • Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, Gubbens S, et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat Methods. 2013;10: 584–590. doi: 10.1038/nmeth.247223644547
    • (2013) Nat Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6
  • 44
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • 8742726, .;:–
    • Kremer J, Mastronarde D, McIntosh J, Computer visualization of three-dimensional image data using IMOD. J Struct Biol. 1996;116: 71–76. 8742726
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.1    Mastronarde, D.2    McIntosh, J.3
  • 45
    • 70350217328 scopus 로고    scopus 로고
    • CTF determination and correction for low dose tomographic tilt series
    • 19732834, .;:–
    • Xiong Q, Morphew MK, Schwartz CL, Hoenger AH, Mastronarde DN, CTF determination and correction for low dose tomographic tilt series. J Struct Biol. 2009;168: 378–387. doi: 10.1016/j.jsb.2009.08.01619732834
    • (2009) J Struct Biol , vol.168 , pp. 378-387
    • Xiong, Q.1    Morphew, M.K.2    Schwartz, C.L.3    Hoenger, A.H.4    Mastronarde, D.N.5
  • 46
    • 84860574289 scopus 로고    scopus 로고
    • Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments
    • 22245546, .;:–
    • Castaño-Díez D, Kudryashev M, Arheit M, Stahlberg H, Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J Struct Biol. 2012;178: 139–151. doi: 10.1016/j.jsb.2011.12.01722245546
    • (2012) J Struct Biol , vol.178 , pp. 139-151
    • Castaño-Díez, D.1    Kudryashev, M.2    Arheit, M.3    Stahlberg, H.4
  • 47
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • 17011211, .;:–
    • Heymann JB, Belnap DM, Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol. 2007;157: 3–18. 17011211
    • (2007) J Struct Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 48
    • 77951477375 scopus 로고    scopus 로고
    • Electron cryotomography of Tula hantavirus suggests a unique assembly paradigm for enveloped viruses
    • 20219926, ..;:–
    • Huiskonen JT, Hepojoki J, Laurinmäki P, Vaheri A, Lankinen H, Butcher SJ, et al. Electron cryotomography of Tula hantavirus suggests a unique assembly paradigm for enveloped viruses. J Virol. 2010;84: 4889–4897. doi: 10.1128/JVI.00057-1020219926
    • (2010) J Virol , vol.84 , pp. 4889-4897
    • Huiskonen, J.T.1    Hepojoki, J.2    Laurinmäki, P.3    Vaheri, A.4    Lankinen, H.5    Butcher, S.J.6
  • 49
    • 84878490025 scopus 로고    scopus 로고
    • Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike
    • 23696739, .;:
    • Bowden TA, Bitto D, McLees A, Yeromonahos C, Elliott RM, Huiskonen JT, Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike. PLoS Pathog. 2013;9: e1003374. doi: 10.1371/journal.ppat.100337423696739
    • (2013) PLoS Pathog , vol.9 , pp. e1003374
    • Bowden, T.A.1    Bitto, D.2    McLees, A.3    Yeromonahos, C.4    Elliott, R.M.5    Huiskonen, J.T.6
  • 50
    • 84908326020 scopus 로고    scopus 로고
    • Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo
    • Huiskonen JT, Parsy M-L, Li S, Bitto D, Renner M, Bowden TA, Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo. J Vis Exp. 2014.
    • (2014) J Vis Exp
    • Huiskonen, J.T.1    Parsy, M.-L.2    Li, S.3    Bitto, D.4    Renner, M.5    Bowden, T.A.6
  • 51
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • 25122622, .;:
    • Scheres SH, Beam-induced motion correction for sub-megadalton cryo-EM particles. Elife. 2014;3: e03665. doi: 10.7554/eLife.0366525122622
    • (2014) Elife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 52
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • 14568533, .;:–
    • Rosenthal PB, Henderson R, Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol. 2003;333: 721–745. 14568533
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 53
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • 20338243, .;:–
    • Pintilie GD, Zhang J, Goddard TD, Chiu W, Gossard DC, Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J Struct Biol. 2010;170: 427–438. doi: 10.1016/j.jsb.2010.03.00720338243
    • (2010) J Struct Biol , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 54
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • 16963278, .;:–
    • Goddard TD, Huang CC, Ferrin TE, Visualizing density maps with UCSF Chimera. J Struct Biol. 2007;157: 281–287. 16963278
    • (2007) J Struct Biol , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.