메뉴 건너뛰기




Volumn 7, Issue 5, 2011, Pages

Correction to: Structural Insights into Viral Determinants of Nematode Mediated Grapevine fanleaf virus Transmission (PLoS Pathogens, (2011), 7, 5, (e1002034), 10.1371/journal.ppat.1002034);Structural insights into viral determinants of nematode mediated grapevine fanleaf virus transmission

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CAPSID PROTEIN; GLYCINE; VIRUS RNA;

EID: 79958068763     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1006268     Document Type: Erratum
Times cited : (43)

References (67)
  • 1
    • 40349114934 scopus 로고    scopus 로고
    • Dengue virus-mosquito interactions
    • Halstead SB, (2008) Dengue virus-mosquito interactions. Annu Rev Entomol 53: 273-291.
    • (2008) Annu Rev Entomol , vol.53 , pp. 273-291
    • Halstead, S.B.1
  • 2
    • 50849098592 scopus 로고    scopus 로고
    • Global Spread and Persistence of Dengue
    • Kyle JL, Harris E, (2008) Global Spread and Persistence of Dengue. Annu Rev Microbiol 62: 71-92.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 71-92
    • Kyle, J.L.1    Harris, E.2
  • 4
    • 74449092224 scopus 로고    scopus 로고
    • Present and future arboviral threats
    • Weaver SC, Reisen WK, (2010) Present and future arboviral threats. Antiviral Res 85: 328-345.
    • (2010) Antiviral Res , vol.85 , pp. 328-345
    • Weaver, S.C.1    Reisen, W.K.2
  • 5
    • 29244454317 scopus 로고    scopus 로고
    • Transmission specificity of plant viruses by vectors
    • Andret-Link P, Fuchs M, (2005) Transmission specificity of plant viruses by vectors. J Plant Pathol 87: 153-165.
    • (2005) J Plant Pathol , vol.87 , pp. 153-165
    • Andret-Link, P.1    Fuchs, M.2
  • 7
    • 33748945418 scopus 로고    scopus 로고
    • Virus-vector interactions mediating nonpersistent and semipersistent transmission of plant viruses
    • Ng JCK, Falk BW, (2006) Virus-vector interactions mediating nonpersistent and semipersistent transmission of plant viruses. Annu Rev Phytopathol 44: 183-212.
    • (2006) Annu Rev Phytopathol , vol.44 , pp. 183-212
    • Ng, J.C.K.1    Falk, B.W.2
  • 8
    • 33947585383 scopus 로고    scopus 로고
    • Virus transmission - Getting out and in
    • Blanc S, (2007) Virus transmission- Getting out and in. Plant Cell Monogr 7: 1-28.
    • (2007) Plant Cell Monogr , vol.7 , pp. 1-28
    • Blanc, S.1
  • 9
    • 0025141014 scopus 로고
    • A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus
    • Atreya CD, Raccah B, Pirone TP, (1990) A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus. Virology 178: 161-165.
    • (1990) Virology , vol.178 , pp. 161-165
    • Atreya, C.D.1    Raccah, B.2    Pirone, T.P.3
  • 10
    • 0344577901 scopus 로고    scopus 로고
    • Context of the coat protein DAG motif affects potyvirus transmissibility by aphids
    • Lopez-Moya JJ, Wang RY, Pirone TP, (1999) Context of the coat protein DAG motif affects potyvirus transmissibility by aphids. J Gen Virol 80: 3281-3288.
    • (1999) J Gen Virol , vol.80 , pp. 3281-3288
    • Lopez-Moya, J.J.1    Wang, R.Y.2    Pirone, T.P.3
  • 11
    • 0032029737 scopus 로고    scopus 로고
    • Amino acid changes in the coat protein of cucumber mosaic virus differentially affect transmission by the aphids Myzus persicae and Aphis gossypii
    • Perry KL, Zhang L, Palukaitis P, (1998) Amino acid changes in the coat protein of cucumber mosaic virus differentially affect transmission by the aphids Myzus persicae and Aphis gossypii. Virology 242: 204-210.
    • (1998) Virology , vol.242 , pp. 204-210
    • Perry, K.L.1    Zhang, L.2    Palukaitis, P.3
  • 12
    • 0034997956 scopus 로고    scopus 로고
    • Identification of specific cucumber necrosis virus coat protein amino acids affecting fungus transmission and zoospore attachment
    • Kakani K, Sgro JY, Rochon D, (2001) Identification of specific cucumber necrosis virus coat protein amino acids affecting fungus transmission and zoospore attachment. J Virol 75: 5576-5583.
    • (2001) J Virol , vol.75 , pp. 5576-5583
    • Kakani, K.1    Sgro, J.Y.2    Rochon, D.3
  • 13
    • 33747065592 scopus 로고    scopus 로고
    • The roles and mechanisms of helper component proteins encoded by potyviruses and caulimoviruses
    • Syller J, (2006) The roles and mechanisms of helper component proteins encoded by potyviruses and caulimoviruses. Physiol Mol Plant Pathol 67: 119-130.
    • (2006) Physiol Mol Plant Pathol , vol.67 , pp. 119-130
    • Syller, J.1
  • 14
    • 0031925390 scopus 로고    scopus 로고
    • Mutations in the HC-Pro gene of zucchini yellow mosaic potyvirus: effects on aphid transmission and binding to purified virions
    • Peng YH, Kadoury D, Gal-On A, Huet H, Wang Y, et al. (1998) Mutations in the HC-Pro gene of zucchini yellow mosaic potyvirus: effects on aphid transmission and binding to purified virions. J Gen Virol 79: 897-904.
    • (1998) J Gen Virol , vol.79 , pp. 897-904
    • Peng, Y.H.1    Kadoury, D.2    Gal-On, A.3    Huet, H.4    Wang, Y.5
  • 15
    • 0032408632 scopus 로고    scopus 로고
    • Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets
    • Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, et al. (1998) Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol 79: 3119-3122.
    • (1998) J Gen Virol , vol.79 , pp. 3119-3122
    • Blanc, S.1    Ammar, E.D.2    Garcia-Lampasona, S.3    Dolja, V.V.4    Llave, C.5
  • 16
    • 0028236450 scopus 로고
    • Mutations in the helper component protease gene of zucchini yellow mosaic virus affect its ability to mediate aphid transmissibility
    • Huet H, Gal-On A, Meir E, Lecoq H, Raccah B, (1994) Mutations in the helper component protease gene of zucchini yellow mosaic virus affect its ability to mediate aphid transmissibility. J Gen Virol 75: 1407-1414.
    • (1994) J Gen Virol , vol.75 , pp. 1407-1414
    • Huet, H.1    Gal-On, A.2    Meir, E.3    Lecoq, H.4    Raccah, B.5
  • 17
    • 0025270788 scopus 로고
    • Cucumovirus transmission by the aphid Myzus persicae is determined solely by the viral coat protein
    • Chen B, Francki RI, (1990) Cucumovirus transmission by the aphid Myzus persicae is determined solely by the viral coat protein. J Gen Virol 71: 939-944.
    • (1990) J Gen Virol , vol.71 , pp. 939-944
    • Chen, B.1    Francki, R.I.2
  • 18
    • 0036776323 scopus 로고    scopus 로고
    • A Conserved Capsid Protein Surface Domain of Cucumber Mosaic Virus Is Essential for Efficient Aphid Vector Transmission
    • Liu S, He X, Park G, Josefsson C, Perry KL, (2002) A Conserved Capsid Protein Surface Domain of Cucumber Mosaic Virus Is Essential for Efficient Aphid Vector Transmission. J Virol 76: 9756-9762.
    • (2002) J Virol , vol.76 , pp. 9756-9762
    • Liu, S.1    He, X.2    Park, G.3    Josefsson, C.4    Perry, K.L.5
  • 19
    • 12344334262 scopus 로고    scopus 로고
    • Virion stability and aphid vector transmissibility of Cucumber mosaic virus mutants
    • Ng JC, Josefsson C, Clark AJ, Franz AW, Perry KL, (2005) Virion stability and aphid vector transmissibility of Cucumber mosaic virus mutants. Virology 332: 397-405.
    • (2005) Virology , vol.332 , pp. 397-405
    • Ng, J.C.1    Josefsson, C.2    Clark, A.J.3    Franz, A.W.4    Perry, K.L.5
  • 20
    • 0034751126 scopus 로고    scopus 로고
    • Interaction between the open reading frame III product and the coat protein is required for transmission of cauliflower mosaic virus by aphids
    • Leh V, Jacquot E, Geldreich A, Haas M, Blanc S, et al. (2001) Interaction between the open reading frame III product and the coat protein is required for transmission of cauliflower mosaic virus by aphids. J Virol 75: 100-106.
    • (2001) J Virol , vol.75 , pp. 100-106
    • Leh, V.1    Jacquot, E.2    Geldreich, A.3    Haas, M.4    Blanc, S.5
  • 21
    • 77950797958 scopus 로고    scopus 로고
    • Structural insights into the molecular mechanisms of Cauliflower mosaic virus transmission by its insect vector
    • Hoh F, Uzest M, Drucker M, Plisson-Chastang C, Bron P, et al. (2010) Structural insights into the molecular mechanisms of Cauliflower mosaic virus transmission by its insect vector. J Virol pp. 4706-4713.
    • (2010) J Virol , pp. 4706-4713
    • Hoh, F.1    Uzest, M.2    Drucker, M.3    Plisson-Chastang, C.4    Bron, P.5
  • 22
    • 0033572949 scopus 로고    scopus 로고
    • Aphid transmission of cauliflower mosaic virus requires the viral PIII protein
    • Leh V, Jacquot E, Geldreich A, Hermann T, Leclerc D, et al. (1999) Aphid transmission of cauliflower mosaic virus requires the viral PIII protein. EMBO J 18: 7077-7085.
    • (1999) EMBO J , vol.18 , pp. 7077-7085
    • Leh, V.1    Jacquot, E.2    Geldreich, A.3    Hermann, T.4    Leclerc, D.5
  • 23
    • 63349111174 scopus 로고    scopus 로고
    • A role for plant microtubules in the formation of transmission-specific inclusion bodies of Cauliflower mosaic virus
    • Martinière A, Gargani D, Uzest M, Lautredou N, Blanc S, et al. (2009) A role for plant microtubules in the formation of transmission-specific inclusion bodies of Cauliflower mosaic virus. Plant J 58: 135-146.
    • (2009) Plant J , vol.58 , pp. 135-146
    • Martinière, A.1    Gargani, D.2    Uzest, M.3    Lautredou, N.4    Blanc, S.5
  • 24
    • 36749101892 scopus 로고    scopus 로고
    • A protein key to plant virus transmission at the tip of the insect vector stylet
    • Uzest M, Gargani D, Drucker M, Hebrard E, Garzo E, et al. (2007) A protein key to plant virus transmission at the tip of the insect vector stylet. Proc Natl Acad Sci USA 104: 17959-17964.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17959-17964
    • Uzest, M.1    Gargani, D.2    Drucker, M.3    Hebrard, E.4    Garzo, E.5
  • 26
    • 0031034052 scopus 로고    scopus 로고
    • Transmission of tobacco rattle virus isolate PpK20 by its nematode vector requires one of the two non-structural genes in the viral RNA 2
    • Hernandez C, Visser PB, Brown DJ, Bol JF, (1997) Transmission of tobacco rattle virus isolate PpK20 by its nematode vector requires one of the two non-structural genes in the viral RNA 2. J Gen Virol 78: 465-467.
    • (1997) J Gen Virol , vol.78 , pp. 465-467
    • Hernandez, C.1    Visser, P.B.2    Brown, D.J.3    Bol, J.F.4
  • 27
    • 0029941143 scopus 로고    scopus 로고
    • Multiple virus genes involved in the nematode transmission of pea early browning virus
    • MacFarlane SA, Wallis CV, Brown DJ, (1996) Multiple virus genes involved in the nematode transmission of pea early browning virus. Virology 219: 417-422.
    • (1996) Virology , vol.219 , pp. 417-422
    • MacFarlane, S.A.1    Wallis, C.V.2    Brown, D.J.3
  • 28
  • 29
    • 1542270892 scopus 로고    scopus 로고
    • The specific transmission of Grapevine fanleaf virus by its nematode vector Xiphinema index is solely determined by the viral coat protein
    • Andret-Link P, Schmitt-Keichinger C, Demangeat G, Komar V, Fuchs M, (2004) The specific transmission of Grapevine fanleaf virus by its nematode vector Xiphinema index is solely determined by the viral coat protein. Virology 320: 12-22.
    • (2004) Virology , vol.320 , pp. 12-22
    • Andret-Link, P.1    Schmitt-Keichinger, C.2    Demangeat, G.3    Komar, V.4    Fuchs, M.5
  • 31
    • 0032520212 scopus 로고    scopus 로고
    • The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily
    • Chandrasekar V, Johnson JE, (1998) The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily. Structure 6: 157-171.
    • (1998) Structure , vol.6 , pp. 157-171
    • Chandrasekar, V.1    Johnson, J.E.2
  • 32
    • 77954978513 scopus 로고    scopus 로고
    • A stretch of 11 amino acids in the ßB-ßC loop of the coat protein of grapevine fanleaf virus is essential for transmission by the nematode Xiphinema index
    • Schellenberger P, Andret-Link P, Schmitt-Keichinger C, Bergdoll M, Marmonier A, et al. (2010) A stretch of 11 amino acids in the ßB-ßC loop of the coat protein of grapevine fanleaf virus is essential for transmission by the nematode Xiphinema index. J Virol 84: 7924-7933.
    • (2010) J Virol , vol.84 , pp. 7924-7933
    • Schellenberger, P.1    Andret-Link, P.2    Schmitt-Keichinger, C.3    Bergdoll, M.4    Marmonier, A.5
  • 33
    • 32944473016 scopus 로고    scopus 로고
    • Virus Entry: Open Sesame
    • Marsh M, Helenius A, (2006) Virus Entry: Open Sesame. Cell 124: 729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 34
    • 1542284426 scopus 로고
    • Souches de virus à haute aggressivité isolées de vignes atteintes de dégenerescence infectieuse
    • Vuittenez M, Munck MC, Kuszala J, (1964) Souches de virus à haute aggressivité isolées de vignes atteintes de dégenerescence infectieuse. Etudes Virol Appliquée 5: 69-78.
    • (1964) Etudes Virol Appliquée , vol.5 , pp. 69-78
    • Vuittenez, M.1    Munck, M.C.2    Kuszala, J.3
  • 35
    • 0027404463 scopus 로고
    • Biologically active transcripts from cloned cDNA of genomic Grapevine fanleaf nepovirus RNAs
    • Viry M, Serghini MA, Hans F, Ritzenthaler C, Pinck M, et al. (1993) Biologically active transcripts from cloned cDNA of genomic Grapevine fanleaf nepovirus RNAs. J Gen Virol 74: 169-174.
    • (1993) J Gen Virol , vol.74 , pp. 169-174
    • Viry, M.1    Serghini, M.A.2    Hans, F.3    Ritzenthaler, C.4    Pinck, M.5
  • 36
    • 79954415294 scopus 로고    scopus 로고
    • Strategies for the crystallization of viruses: Using phase diagrams and gels to produced 3D crystals of Grapevine fanleaf virus
    • Schellenberger P, Demangeat G, Lemaire O, Ritzenthaler C, Bergdoll M, et al. (2011) Strategies for the crystallization of viruses: Using phase diagrams and gels to produced 3D crystals of Grapevine fanleaf virus. J Struct Biol 174: 344-351.
    • (2011) J Struct Biol , vol.174 , pp. 344-351
    • Schellenberger, P.1    Demangeat, G.2    Lemaire, O.3    Ritzenthaler, C.4    Bergdoll, M.5
  • 37
    • 1442359308 scopus 로고    scopus 로고
    • Structures of Picorna-Like Plant Viruses: Implications and Applications
    • Lin T, Johnson JE, (2003) Structures of Picorna-Like Plant Viruses: Implications and Applications. Adv Virus Research 62: 167-239.
    • (2003) Adv Virus Research , vol.62 , pp. 167-239
    • Lin, T.1    Johnson, J.E.2
  • 38
    • 0346412376 scopus 로고
    • Efficiency of Xiphinema americanum as a vector of tobacco ringspot virus
    • McGuire JM, (1964) Efficiency of Xiphinema americanum as a vector of tobacco ringspot virus. Phytopathol 54: 799-801.
    • (1964) Phytopathol , vol.54 , pp. 799-801
    • McGuire, J.M.1
  • 39
    • 0000522291 scopus 로고
    • Distribution of viruses and their nematode vectors
    • In: Harris K, editors, New York, Springer-Verlag
    • Martelli GP, Taylor CE, (1990) Distribution of viruses and their nematode vectors. In: Harris K, editors. Advances in Disease Vector Research New York Springer-Verlag pp. 151-189.
    • (1990) Advances in Disease Vector Research , pp. 151-189
    • Martelli, G.P.1    Taylor, C.E.2
  • 40
    • 0000470490 scopus 로고
    • Protein coats of two strains of Cucumber mosaic virus affect transmission by Aphis gossypii
    • Gera A, Loebenstein G, Raccah B, (1979) Protein coats of two strains of Cucumber mosaic virus affect transmission by Aphis gossypii. Phytopathology 69: 396-399.
    • (1979) Phytopathology , vol.69 , pp. 396-399
    • Gera, A.1    Loebenstein, G.2    Raccah, B.3
  • 41
    • 0001237424 scopus 로고
    • Aphid Transmission of a nonaphid-transmissible strain of Tobacco etch Virus
    • Simons JN, (1976) Aphid Transmission of a nonaphid-transmissible strain of Tobacco etch Virus. Phytopathology 66: 652-654.
    • (1976) Phytopathology , vol.66 , pp. 652-654
    • Simons, J.N.1
  • 42
    • 0031582634 scopus 로고    scopus 로고
    • A cucumber necrosis virus variant deficient in fungal transmissibility contains an altered coat protein shell domain
    • Robbins MA, Reade RD, Rochon DM, (1997) A cucumber necrosis virus variant deficient in fungal transmissibility contains an altered coat protein shell domain. Virology 234: 138-146.
    • (1997) Virology , vol.234 , pp. 138-146
    • Robbins, M.A.1    Reade, R.D.2    Rochon, D.M.3
  • 43
    • 27144506977 scopus 로고    scopus 로고
    • A single amino acid position in the helper component of cauliflower mosaic virus can change the spectrum of transmitting vector species
    • Moreno A, Hebrard E, Uzest M, Blanc S, Fereres A, (2005) A single amino acid position in the helper component of cauliflower mosaic virus can change the spectrum of transmitting vector species. J Virol 79: 13587-13593.
    • (2005) J Virol , vol.79 , pp. 13587-13593
    • Moreno, A.1    Hebrard, E.2    Uzest, M.3    Blanc, S.4    Fereres, A.5
  • 44
    • 43349101478 scopus 로고    scopus 로고
    • Picornavirales, a proposed order of positive-sense single-stranded RNA viruses with a pseudo-T = 3 virion architecture
    • Le Gall O, Christian P, Fauquet CM, King AM, Knowles NJ, et al. (2008) Picornavirales, a proposed order of positive-sense single-stranded RNA viruses with a pseudo-T = 3 virion architecture. Arch Virol 153: 715-727.
    • (2008) Arch Virol , vol.153 , pp. 715-727
    • Le Gall, O.1    Christian, P.2    Fauquet, C.M.3    King, A.M.4    Knowles, N.J.5
  • 45
    • 56349152646 scopus 로고    scopus 로고
    • The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups
    • Koonin EV, Wolf YI, Nagasaki K, Dolja VV, (2008) The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups. Nat Rev Micro 6: 925-939.
    • (2008) Nat Rev Micro , vol.6 , pp. 925-939
    • Koonin, E.V.1    Wolf, Y.I.2    Nagasaki, K.3    Dolja, V.V.4
  • 46
    • 0024310096 scopus 로고
    • Protein-RNA interactions in an icosahedral virus at 3.0 A resolution
    • Chen Stauffacher ZC, Li Y, Schmidt T, Bomu W, Kamer G, et al. (1989) Protein-RNA interactions in an icosahedral virus at 3.0 A resolution. Science 245: 154-159.
    • (1989) Science , vol.245 , pp. 154-159
    • Chen Stauffacher, Z.C.1    Li, Y.2    Schmidt, T.3    Bomu, W.4    Kamer, G.5
  • 47
    • 84899947371 scopus 로고    scopus 로고
    • Nepovirus
    • In: Mahy BWJ, van Regenmortel MHV, editors, Oxford, Elsevier
    • Sanfaçon H, (2008) Nepovirus. In: Mahy BWJ, van Regenmortel MHV, editors. Encyclopedia of Virology Oxford Elsevier pp. 405-413.
    • (2008) Encyclopedia of Virology , pp. 405-413
    • Sanfaçon, H.1
  • 48
    • 0025867217 scopus 로고
    • Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus
    • Atreya PL, Atreya CD, Pirone TP, (1991) Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus. Proc Natl Acad Sci U S A 88: 7887-7891.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7887-7891
    • Atreya, P.L.1    Atreya, C.D.2    Pirone, T.P.3
  • 49
    • 77955279752 scopus 로고    scopus 로고
    • Genetic structure and molecular variability of Grapevine fanleaf virus populations
    • Oliver JE, Vigne E, Fuchs M, (2010) Genetic structure and molecular variability of Grapevine fanleaf virus populations. Virus Res 152: 30-40.
    • (2010) Virus Res , vol.152 , pp. 30-40
    • Oliver, J.E.1    Vigne, E.2    Fuchs, M.3
  • 50
    • 0033081979 scopus 로고    scopus 로고
    • The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex
    • Fry EE, Lea SM, Jackson T, Newman JWI, Ellard FM, et al. (1999) The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. EMBO J 18: 543-554.
    • (1999) EMBO J , vol.18 , pp. 543-554
    • Fry, E.E.1    Lea, S.M.2    Jackson, T.3    Newman, J.W.I.4    Ellard, F.M.5
  • 51
    • 21444433508 scopus 로고    scopus 로고
    • Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation
    • Fry EE, Newman JWI, Curry S, Najjam S, Jackson T, et al. (2005) Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation. J Gen Virol 86: 1909-1920.
    • (2005) J Gen Virol , vol.86 , pp. 1909-1920
    • Fry, E.E.1    Newman, J.W.I.2    Curry, S.3    Najjam, S.4    Jackson, T.5
  • 52
    • 0032977608 scopus 로고    scopus 로고
    • The nine C-terminal residues of the Grapevine fanleaf nepovirus movement protein are critical for systemic virus spread
    • Belin C, Schmitt C, Gaire F, Walter B, Demangeat G, et al. (1999) The nine C-terminal residues of the Grapevine fanleaf nepovirus movement protein are critical for systemic virus spread. J Gen Virol 80: 1347-1356.
    • (1999) J Gen Virol , vol.80 , pp. 1347-1356
    • Belin, C.1    Schmitt, C.2    Gaire, F.3    Walter, B.4    Demangeat, G.5
  • 54
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera
    • Ritzenthaler C, Nebenfuhr A, Movafeghi A, Stussi-Garaud C, Behnia L, et al. (2002) Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera. Plant Cell 14: 237-261.
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1    Nebenfuhr, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5
  • 55
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N, (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142: 334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 56
    • 0033372028 scopus 로고    scopus 로고
    • Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution
    • Conway J, Steven A, (1999) Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution. J Struct Biol 128: 106-118.
    • (1999) J Struct Biol , vol.128 , pp. 106-118
    • Conway, J.1    Steven, A.2
  • 57
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker TS, Cheng RH, (1996) A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J Struct Biol 116: 120-130.
    • (1996) J Struct Biol , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 58
    • 0022734418 scopus 로고
    • Resolution criteria for three dimensional reconstruction
    • van Heel M, Harauz G, (1986) Resolution criteria for three dimensional reconstruction. Optik (Jena) 73: 119-122.
    • (1986) Optik (Jena) , vol.73 , pp. 119-122
    • van Heel, M.1    Harauz, G.2
  • 60
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J, (1994) AMoRe: an automated package for molecular replacement. Acta Cryst 50: 157-163.
    • (1994) Acta Cryst , vol.50 , pp. 157-163
    • Navaza, J.1
  • 61
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt GJ, (1996) Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr D Biol Crystallogr 52: 842-857.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 62
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt GJ, Jones TA, (1999) Software for handling macromolecular envelopes. Acta Cryst D 55: 941-944.
    • (1999) Acta Cryst D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 63
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: generation and refinement of homology-based protein structure models
    • Fiser A, Sali A, (2003) Modeller: generation and refinement of homology-based protein structure models. Meth Enzymol 374: 461-491.
    • (2003) Meth Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 65
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 66
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: an efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC, (1996) Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38: 305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.