-
2
-
-
0032054113
-
Filamentous phage structure, infection and assembly
-
Marvin DA Filamentous phage structure, infection and assembly. Curr Opin Struct Biol. 8:1998;150-158.
-
(1998)
Curr Opin Struct Biol
, vol.8
, pp. 150-158
-
-
Marvin, D.A.1
-
3
-
-
0031588020
-
Quasi-equivalent viruses: A paradigm for protein assemblies
-
Johnson JE, Speir JA Quasi-equivalent viruses: a paradigm for protein assemblies. J Mol Biol. 269:1997;665-675.
-
(1997)
J Mol Biol
, vol.269
, pp. 665-675
-
-
Johnson, J.E.1
Speir, J.A.2
-
4
-
-
0031606857
-
Bacteriophage HK97 head assembly: A protein ballet
-
Hendrix RW, Duda RL Bacteriophage HK97 head assembly: a protein ballet. Adv Virus Res. 50:1998;235-288.
-
(1998)
Adv Virus Res
, vol.50
, pp. 235-288
-
-
Hendrix, R.W.1
Duda, R.L.2
-
5
-
-
0030586070
-
Poliovirus: New insights from an old paradigm
-
Wien MW, Chow M, Hogle JM Poliovirus: new insights from an old paradigm. Structure. 4:1996;763-767.
-
(1996)
Structure
, vol.4
, pp. 763-767
-
-
Wien, M.W.1
Chow, M.2
Hogle, J.M.3
-
6
-
-
0343773443
-
Orbivirus structure and assembly
-
Roy P Orbivirus structure and assembly. Virology. 216:1996;1-11.
-
(1996)
Virology
, vol.216
, pp. 1-11
-
-
Roy, P.1
-
7
-
-
0032520212
-
The structure of tobacco ringspot virus: A link in the evolution of icosahedral capsids in the picornavirus superfamily
-
This paper describes the crystal structure of a representative of a new group of plant viruses that are related to comoviruses and belong to the picornavirus family. The 60 coat protein molecules each have three β-sandwich-type domains connected by linker segments. The similar coat protein molecules of picornaviruses, like poliovirus, are synthesized as polyproteins, which are cleaved by a viral protease before assembly, but in the tobacco ringspot virus, no cleavage occurs.
-
Chandrasekar V, Johnson JE The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily. Structure. 6:1998;157-171. This paper describes the crystal structure of a representative of a new group of plant viruses that are related to comoviruses and belong to the picornavirus family. The 60 coat protein molecules each have three β-sandwich-type domains connected by linker segments. The similar coat protein molecules of picornaviruses, like poliovirus, are synthesized as polyproteins, which are cleaved by a viral protease before assembly, but in the tobacco ringspot virus, no cleavage occurs.
-
(1998)
Structure
, vol.6
, pp. 157-171
-
-
Chandrasekar, V.1
Johnson, J.E.2
-
8
-
-
0031554914
-
The crystal structure of bacteriophage GA and a comparison of bacteriophages belonging to the major groups of Escherichia coli leviviruses
-
The authors report the structure of an RNA phage and compare related phage structures in a search for the features that determine subunit packing in these viruses.
-
Tars K, Bundule M, Fridborg K, Liljas L The crystal structure of bacteriophage GA and a comparison of bacteriophages belonging to the major groups of Escherichia coli leviviruses. J Mol Biol. 271:1997;759-773. The authors report the structure of an RNA phage and compare related phage structures in a search for the features that determine subunit packing in these viruses.
-
(1997)
J Mol Biol
, vol.271
, pp. 759-773
-
-
Tars, K.1
Bundule, M.2
Fridborg, K.3
Liljas, L.4
-
9
-
-
12644284498
-
Structure of poliovirus type 2 Lansing complexed with antiviral agent SCH48973: Comparison of the structural and biological properties of three poliovirus serotypes
-
Lentz KN, Smith AD, Geisler SC, Cox S, Buontempo P, Skelton A, DeMartino J, Rozhon E, Schwartz J, Girijavallabhan Vet al. Structure of poliovirus type 2 Lansing complexed with antiviral agent SCH48973: comparison of the structural and biological properties of three poliovirus serotypes. Structure. 5:1997;961-978.
-
(1997)
Structure
, vol.5
, pp. 961-978
-
-
Lentz, K.N.1
Smith, A.D.2
Geisler, S.C.3
Cox, S.4
Buontempo, P.5
Skelton, A.6
Demartino, J.7
Rozhon, E.8
Schwartz, J.9
Girijavallabhan, V.10
-
10
-
-
0032526711
-
Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry
-
Chen XS, Stehle T, Harrison SC Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry. EMBO J. 17:1998;3233-3240.
-
(1998)
EMBO J
, vol.17
, pp. 3233-3240
-
-
Chen, X.S.1
Stehle, T.2
Harrison, S.C.3
-
11
-
-
0030890291
-
Structure of Semliki Forest virus core protein
-
Choi HK, Lu G, Lee S, Wengler G, Rossmann MG Structure of Semliki Forest virus core protein. Proteins. 27:1997;345-359.
-
(1997)
Proteins
, vol.27
, pp. 345-359
-
-
Choi, H.K.1
Lu, G.2
Lee, S.3
Wengler, G.4
Rossmann, M.G.5
-
12
-
-
0032189765
-
The atomic structure of the bluetongue virus core
-
The crystal structure at 3.5 Å resolution of bluetongue virus cores. The core structure comprises the inner two protein layers of the three layers in the intact virions. This is the largest object (the protein shell has 900 protein subunits with a total molecular weight of 42 MDa) to have been solved to a resolution allowing an atomic model to be built.
-
Grimes JM, Burroughs JN, Gouet P, Diprose JM, Malby R, Zientara S, Mertens PP, Stuart DI The atomic structure of the bluetongue virus core. Nature. 395:1998;470-478. The crystal structure at 3.5 Å resolution of bluetongue virus cores. The core structure comprises the inner two protein layers of the three layers in the intact virions. This is the largest object (the protein shell has 900 protein subunits with a total molecular weight of 42 MDa) to have been solved to a resolution allowing an atomic model to be built.
-
(1998)
Nature
, vol.395
, pp. 470-478
-
-
Grimes, J.M.1
Burroughs, J.N.2
Gouet, P.3
Diprose, J.M.4
Malby, R.5
Zientara, S.6
Mertens, P.P.7
Stuart, D.I.8
-
13
-
-
0031570687
-
Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
-
Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure. 5:1997;789-798.
-
(1997)
Structure
, vol.5
, pp. 789-798
-
-
Tao, Y.1
Strelkov, S.V.2
Mesyanzhinov, V.V.3
Rossmann, M.G.4
-
14
-
-
0032939173
-
Crystallographically identical virus capsids display different properties in solution
-
in press. Crystal structures of intact Flock House virus virions and virus-like particles formed by coat proteins from an expression system show no significant differences. This paper shows that such particles have widely different properties regarding susceptibility to proteases, which demonstrates that the crystal structures might have little relevance for understanding the flexibility of viral capsids.
-
Bothner B, Schneemann A, Marshall D, Reddy V, Johnson JE, Siuzdak G Crystallographically identical virus capsids display different properties in solution. Nat Struct Biol. 1999;. in press. Crystal structures of intact Flock House virus virions and virus-like particles formed by coat proteins from an expression system show no significant differences. This paper shows that such particles have widely different properties regarding susceptibility to proteases, which demonstrates that the crystal structures might have little relevance for understanding the flexibility of viral capsids.
-
(1999)
Nat Struct Biol
-
-
Bothner, B.1
Schneemann, A.2
Marshall, D.3
Reddy, V.4
Johnson, J.E.5
Siuzdak, G.6
-
16
-
-
0031213649
-
The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions
-
The crystal structures of two complexes between protein capsids and specifically bound RNA stem-loops show that the higher binding affinity is due to an internal hydrogen bond within the RNA molecule.
-
Valegård K, Murray JB, Stonehouse NJ, van den Worm S, Stockley PG, Liljas L The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J Mol Biol. 270:1997;724-738. The crystal structures of two complexes between protein capsids and specifically bound RNA stem-loops show that the higher binding affinity is due to an internal hydrogen bond within the RNA molecule.
-
(1997)
J Mol Biol
, vol.270
, pp. 724-738
-
-
Valegård, K.1
Murray, J.B.2
Stonehouse, N.J.3
Van Den Worm, S.4
Stockley, P.G.5
Liljas, L.6
-
17
-
-
0032030291
-
Crystal structures of MS2 coat protein mutant in complex with wild-type RNA operator fragments
-
van den Worm S, Stonehouse NJ, Valegård K, Murray JB, Walton C, Stockley PG, Liljas L Crystal structures of MS2 coat protein mutant in complex with wild-type RNA operator fragments. Nucleic Acids Res. 26:1998;1345-1351.
-
(1998)
Nucleic Acids Res
, vol.26
, pp. 1345-1351
-
-
Van Den Worm, S.1
Stonehouse, N.J.2
Valegård, K.3
Murray, J.B.4
Walton, C.5
Stockley, P.G.6
Liljas, L.7
-
18
-
-
0031903417
-
Binding of the human immunodeficiency virus type 1 Gag protein to the viral RNA encapsidation signal in the yeast three-hybrid system
-
Bacharach E, Goff SP Binding of the human immunodeficiency virus type 1 Gag protein to the viral RNA encapsidation signal in the yeast three-hybrid system. J Virol. 72:1998;6944-6949.
-
(1998)
J Virol
, vol.72
, pp. 6944-6949
-
-
Bacharach, E.1
Goff, S.P.2
-
19
-
-
0031820377
-
Encapsidation studies of poliovirus subgenomic replicons
-
Barclay W, Li Q, Hutchinson G, Moon D, Richardson A, Percy N, Almond JW, Evans DJ Encapsidation studies of poliovirus subgenomic replicons. J Gen Virol. 79:1998;1725-1734.
-
(1998)
J Gen Virol
, vol.79
, pp. 1725-1734
-
-
Barclay, W.1
Li, Q.2
Hutchinson, G.3
Moon, D.4
Richardson, A.5
Percy, N.6
Almond, J.W.7
Evans, D.J.8
-
20
-
-
0032565360
-
Mutational analysis of stem-loops in the RNA packaging signal of the Moloney murine leukemia virus
-
Fisher J, Goff SP Mutational analysis of stem-loops in the RNA packaging signal of the Moloney murine leukemia virus. Virology. 244:1998;133-145.
-
(1998)
Virology
, vol.244
, pp. 133-145
-
-
Fisher, J.1
Goff, S.P.2
-
21
-
-
0031662095
-
Trans-encapsidation of a poliovirus replicon by different picornavirus capsid proteins
-
Jia XY, Van Eden M, Busch MG, Ehrenfeld E, Summers DF Trans-encapsidation of a poliovirus replicon by different picornavirus capsid proteins. J Virol. 72:1998;7972-7977.
-
(1998)
J Virol
, vol.72
, pp. 7972-7977
-
-
Jia, X.Y.1
Van Eden, M.2
Busch, M.G.3
Ehrenfeld, E.4
Summers, D.F.5
-
22
-
-
0032579846
-
Demonstration of the specificity of poliovirus encapsidation using a novel replicon which encodes enzymatically active firefly luciferase
-
Porter DC, Ansardi DC, Wang J, McPherson S, Moldoveanu Z, Morrow CD Demonstration of the specificity of poliovirus encapsidation using a novel replicon which encodes enzymatically active firefly luciferase. Virology. 243:1998;1-11.
-
(1998)
Virology
, vol.243
, pp. 1-11
-
-
Porter, D.C.1
Ansardi, D.C.2
Wang, J.3
McPherson, S.4
Moldoveanu, Z.5
Morrow, C.D.6
-
23
-
-
0031694398
-
In vivo selection of Rous sarcoma virus mutants with randomized sequences in the packaging signal
-
Doria-Rose NA, Vogt VM In vivo selection of Rous sarcoma virus mutants with randomized sequences in the packaging signal. J Virol. 72:1998;8073-8082.
-
(1998)
J Virol
, vol.72
, pp. 8073-8082
-
-
Doria-Rose, N.A.1
Vogt, V.M.2
-
24
-
-
0032169944
-
Deletions in the conserved amino-terminal basic arm of cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement
-
Schmitz I, Rao AL Deletions in the conserved amino-terminal basic arm of cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement. Virology. 248:1998;323-331.
-
(1998)
Virology
, vol.248
, pp. 323-331
-
-
Schmitz, I.1
Rao, A.L.2
-
25
-
-
0031658922
-
Specific encapsidation of nodavirus RNAs is mediated through the C terminus of capsid precursor protein alpha
-
Mutants of Flock House virus are shown to form apparently normal particles, but they lack the viral capability for packaging the viral RNA. Three phenylalanine residues are shown to be important for the specific recognition of the viral RNA. These are found in the γ peptide, which is formed at the maturation cleavage.
-
Schneemann A, Marshall D Specific encapsidation of nodavirus RNAs is mediated through the C terminus of capsid precursor protein alpha. J Virol. 72:1998;8738-8746. Mutants of Flock House virus are shown to form apparently normal particles, but they lack the viral capability for packaging the viral RNA. Three phenylalanine residues are shown to be important for the specific recognition of the viral RNA. These are found in the γ peptide, which is formed at the maturation cleavage.
-
(1998)
J Virol
, vol.72
, pp. 8738-8746
-
-
Schneemann, A.1
Marshall, D.2
-
26
-
-
0032549663
-
Refined structure of satellite tobacco mosaic virus at 1.8 Å resolution
-
The 1.8 Å resolution structure of satellite tobacco mosaic virus, a small T = 1 virus, shows the arrangement of a large proportion of the viral RNA as double-stranded segments interacting with the protein at all equivalent positions of the icosahedral capsid.
-
Larson SB, Day J, Greenwood A, McPherson A Refined structure of satellite tobacco mosaic virus at 1.8 Å resolution. J Mol Biol. 277:1998;37-59. The 1.8 Å resolution structure of satellite tobacco mosaic virus, a small T = 1 virus, shows the arrangement of a large proportion of the viral RNA as double-stranded segments interacting with the protein at all equivalent positions of the icosahedral capsid.
-
(1998)
J Mol Biol
, vol.277
, pp. 37-59
-
-
Larson, S.B.1
Day, J.2
Greenwood, A.3
McPherson, A.4
-
27
-
-
0030792944
-
Structural adaptations in the specialized bacteriophage T4 cochaperonin gp31 expand the size of the Anfinsen cage
-
The folding of the capsid protein of bacteriophage T4 requires the presence of the gp31 protein, which replaces bacterial GroES in the complex with chaperonin GroEL. The crystal structure shows that gp31 is similar to GroES, but the gp31-GroEL complex can accommodate the T4 coat protein, which is larger than the proteins that are folded with the assistance of the GroEL-GroES bacterial complex.
-
Hunt JF, van der Vies SM, Henry L, Deisenhofer J Structural adaptations in the specialized bacteriophage T4 cochaperonin gp31 expand the size of the Anfinsen cage. Cell. 90:1997;361-371. The folding of the capsid protein of bacteriophage T4 requires the presence of the gp31 protein, which replaces bacterial GroES in the complex with chaperonin GroEL. The crystal structure shows that gp31 is similar to GroES, but the gp31-GroEL complex can accommodate the T4 coat protein, which is larger than the proteins that are folded with the assistance of the GroEL-GroES bacterial complex.
-
(1997)
Cell
, vol.90
, pp. 361-371
-
-
Hunt, J.F.1
Van Der Vies, S.M.2
Henry, L.3
Deisenhofer, J.4
-
28
-
-
0031018112
-
Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
-
Hu J, Toft DO, Seeger C Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J. 16:1997;59-68.
-
(1997)
EMBO J
, vol.16
, pp. 59-68
-
-
Hu, J.1
Toft, D.O.2
Seeger, C.3
-
29
-
-
0031961961
-
Energetics of quasiequivalence: Computational analysis of protein-protein interactions in icosahedral viruses
-
Association energies calculated using CHARMM were used to find likely assembly pathways for the black beetle virus, southern bean mosaic virus and human rhinovirus 14. The contributions of individual residues were calculated, allowing the possibility of testing the prediction by mutagenesis.
-
Reddy VS, Giesing HA, Morton RT, Kumar A, Post CB, Brooks CL III, Johnson JE Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses. Biophys J. 74:1998;546-558. Association energies calculated using CHARMM were used to find likely assembly pathways for the black beetle virus, southern bean mosaic virus and human rhinovirus 14. The contributions of individual residues were calculated, allowing the possibility of testing the prediction by mutagenesis.
-
(1998)
Biophys J
, vol.74
, pp. 546-558
-
-
Reddy, V.S.1
Giesing, H.A.2
Morton, R.T.3
Kumar, A.4
Post, C.B.5
Brooks C.L. III6
Johnson, J.E.7
-
30
-
-
73649156890
-
Physical principles in the construction of regular viruses
-
Caspar DLD, Klug A Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol. 27:1962;1-24.
-
(1962)
Cold Spring Harb Symp Quant Biol
, vol.27
, pp. 1-24
-
-
Caspar, D.L.D.1
Klug, A.2
-
31
-
-
0032563227
-
Bacteriophage DNA packaging: RNA gears in a DNA transport machine
-
Hendrix RW Bacteriophage DNA packaging: RNA gears in a DNA transport machine. Cell. 94:1998;147-150.
-
(1998)
Cell
, vol.94
, pp. 147-150
-
-
Hendrix, R.W.1
-
32
-
-
0032582665
-
Assembly of a tailed bacterial virus and its genome release studied in three dimensions
-
Three-dimensional reconstructions of phage F29 from electron micrographs of isometric heads with icosahedral symmetry, and prolate heads and complete virions with lower symmetry.
-
Tao Y, Olson NH, Xu W, Anderson DL, Rossmann MG, Baker TS Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell. 95:1998;431-437. Three-dimensional reconstructions of phage F29 from electron micrographs of isometric heads with icosahedral symmetry, and prolate heads and complete virions with lower symmetry.
-
(1998)
Cell
, vol.95
, pp. 431-437
-
-
Tao, Y.1
Olson, N.H.2
Xu, W.3
Anderson, D.L.4
Rossmann, M.G.5
Baker, T.S.6
-
33
-
-
0343811707
-
The bacteriophage F29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution
-
In this paper, the new atomic force microscopy technique is applied to the study of viral components. Two-dimensional crystals of phage Φ29 connectors are shown to possess the expected 12-fold symmetry.
-
Müller DJ, Engel A, Carrascosa JL, Velez M The bacteriophage F29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution. EMBO J. 16:1997;2547-2553. In this paper, the new atomic force microscopy technique is applied to the study of viral components. Two-dimensional crystals of phage Φ29 connectors are shown to possess the expected 12-fold symmetry.
-
(1997)
EMBO J
, vol.16
, pp. 2547-2553
-
-
Müller, D.J.1
Engel, A.2
Carrascosa, J.L.3
Velez, M.4
-
34
-
-
0030839256
-
High-resolution structure of a polyomavirus VP1-oligosaccharide complex: Implications for assembly and receptor binding
-
The crystal structure of polyomavirus VP1 pentamers shows the arrangement of the segments involved in the switching mechanism when the viral capsids form.
-
Stehle T, Harrison SC High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 16:1997;5139-5148. The crystal structure of polyomavirus VP1 pentamers shows the arrangement of the segments involved in the switching mechanism when the viral capsids form.
-
(1997)
EMBO J
, vol.16
, pp. 5139-5148
-
-
Stehle, T.1
Harrison, S.C.2
-
35
-
-
0031776460
-
Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus
-
The removal of a peptide segment that is ordered in the 'flat' subunit contact leads to the production of normal T = 3 particles (and irregular structures), indicating that this segment is not required for correct subunit packing.
-
Dong XF, Natarajan P, Tihova M, Johnson JE, Schneemann A Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus. J Virol. 72:1998;6024-6033. The removal of a peptide segment that is ordered in the 'flat' subunit contact leads to the production of normal T = 3 particles (and irregular structures), indicating that this segment is not required for correct subunit packing.
-
(1998)
J Virol
, vol.72
, pp. 6024-6033
-
-
Dong, X.F.1
Natarajan, P.2
Tihova, M.3
Johnson, J.E.4
Schneemann, A.5
-
36
-
-
0032530131
-
Structure of phage fr capsids with a deletion in the FG loop: Implications for viral assembly
-
The small (T = 3) RNA phages have no obvious order/disorder switches to control their assembly. A loop forming contacts at fivefold and quasi-sixfold axes has widely different conformations that are dependent upon its position. This paper describes the crystal structure of a mutant of a small RNA phage, in which a significant portion of this loop has been removed without any effects on the subunit packing, suggesting that this loop is not crucial for assembly.
-
Axblom C, Tars K, Fridborg K, Orna L, Bundule M, Liljas L Structure of phage fr capsids with a deletion in the FG loop: implications for viral assembly. Virology. 249:1998;80-88. The small (T = 3) RNA phages have no obvious order/disorder switches to control their assembly. A loop forming contacts at fivefold and quasi-sixfold axes has widely different conformations that are dependent upon its position. This paper describes the crystal structure of a mutant of a small RNA phage, in which a significant portion of this loop has been removed without any effects on the subunit packing, suggesting that this loop is not crucial for assembly.
-
(1998)
Virology
, vol.249
, pp. 80-88
-
-
Axblom, C.1
Tars, K.2
Fridborg, K.3
Orna, L.4
Bundule, M.5
Liljas, L.6
-
37
-
-
0030963813
-
Structure of a viral procapsid with molecular scaffolding
-
The crystal structure of a procapsid-like particle of the DNA bacteriophage ΦX-174 showing, for the first time, the conformation and arrangement of scaffolding proteins in atomic detail.
-
Dokland T, McKenna R, Ilag LL, Bowman BR, Incardona NL, Fane BA, Rossmann MG Structure of a viral procapsid with molecular scaffolding. Nature. 389:1997;308-313. The crystal structure of a procapsid-like particle of the DNA bacteriophage ΦX-174 showing, for the first time, the conformation and arrangement of scaffolding proteins in atomic detail.
-
(1997)
Nature
, vol.389
, pp. 308-313
-
-
Dokland, T.1
McKenna, R.2
Ilag, L.L.3
Bowman, B.R.4
Incardona, N.L.5
Fane, B.A.6
Rossmann, M.G.7
-
38
-
-
0031982564
-
Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures
-
This cryoelectron microscopy study of P22 procapsids of a normal and small size (without scaffolding protein) shows similar pentons and hexons. Models for the function of the scaffolding protein are presented.
-
Thuman-Commike PA, Greene B, Malinski JA, King J, Chiu W Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures. Biophys J. 74:1998;559-568. This cryoelectron microscopy study of P22 procapsids of a normal and small size (without scaffolding protein) shows similar pentons and hexons. Models for the function of the scaffolding protein are presented.
-
(1998)
Biophys J
, vol.74
, pp. 559-568
-
-
Thuman-Commike, P.A.1
Greene, B.2
Malinski, J.A.3
King, J.4
Chiu, W.5
-
39
-
-
0032493694
-
A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein
-
Tuma R, Parker MH, Weigele P, Sampson L, Sun Y, Krishna NR, Casjens S, Thomas GJ Jr., Prevelige PE Jr. A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein. J Mol Biol. 281:1998;81-94.
-
(1998)
J Mol Biol
, vol.281
, pp. 81-94
-
-
Tuma, R.1
Parker, M.H.2
Weigele, P.3
Sampson, L.4
Sun, Y.5
Krishna, N.R.6
Casjens, S.7
Thomas G.J., Jr.8
Prevelige P.E., Jr.9
-
40
-
-
18744429919
-
Bacteriophage P22 scaffolding protein forms oligomers in solution
-
Parker MH, Stafford WF III, Prevelige PE Jr. Bacteriophage P22 scaffolding protein forms oligomers in solution. J Mol Biol. 268:1997;655-665.
-
(1997)
J Mol Biol
, vol.268
, pp. 655-665
-
-
Parker, M.H.1
Stafford W.F. III2
Prevelige P.E., Jr.3
-
41
-
-
0032493783
-
Functional domains of bacteriophage P22 scaffolding protein
-
Parker MH, Casjens S, Prevelige PE Jr. Functional domains of bacteriophage P22 scaffolding protein. J Mol Biol. 281:1998;69-79.
-
(1998)
J Mol Biol
, vol.281
, pp. 69-79
-
-
Parker, M.H.1
Casjens, S.2
Prevelige P.E., Jr.3
-
42
-
-
0030780581
-
Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: The structure of empty capsids of foot-and-mouth disease virus
-
Crystal structures of empty capsids of a foot-and-mouth disease virus strain suggest that the mechanism leading to the cleavage of VP0 into VP4 and VP2 is similar to that suggested for poliovirus.
-
Curry S, Fry E, Blakemore W, Abu-Ghazaleh R, Jackson T, King A, Lea S, Newman J, Stuart D Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus. J Virol. 71:1997;9743-9752. Crystal structures of empty capsids of a foot-and-mouth disease virus strain suggest that the mechanism leading to the cleavage of VP0 into VP4 and VP2 is similar to that suggested for poliovirus.
-
(1997)
J Virol
, vol.71
, pp. 9743-9752
-
-
Curry, S.1
Fry, E.2
Blakemore, W.3
Abu-Ghazaleh, R.4
Jackson, T.5
King, A.6
Lea, S.7
Newman, J.8
Stuart, D.9
-
44
-
-
0031569393
-
The refined structure of human rhinovirus 16 at 2.15 Å resolution: Implications for the viral life cycle
-
Hadfield AT, Lee W, Zhao R, Oliveira MA, Minor I, Rueckert RR, Rossmann MG The refined structure of human rhinovirus 16 at 2.15 Å resolution: implications for the viral life cycle. Structure. 5:1997;427-441.
-
(1997)
Structure
, vol.5
, pp. 427-441
-
-
Hadfield, A.T.1
Lee, W.2
Zhao, R.3
Oliveira, M.A.4
Minor, I.5
Rueckert, R.R.6
Rossmann, M.G.7
-
46
-
-
0031936604
-
Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly
-
Li M, Beard P, Estes PA, Lyon MK, Garcea RL Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly. J Virol. 72:1998;2160-2167.
-
(1998)
J Virol
, vol.72
, pp. 2160-2167
-
-
Li, M.1
Beard, P.2
Estes, P.A.3
Lyon, M.K.4
Garcea, R.L.5
-
47
-
-
0031974862
-
Quantitative disassembly and reassembly of human papillomavirus type 11 virus-like particles in vitro
-
McCarthy MP, White WI, Palmer-Hill F, Koenig S, Suzich JA Quantitative disassembly and reassembly of human papillomavirus type 11 virus-like particles in vitro. J Virol. 72:1998;32-41.
-
(1998)
J Virol
, vol.72
, pp. 32-41
-
-
McCarthy, M.P.1
White, W.I.2
Palmer-Hill, F.3
Koenig, S.4
Suzich, J.A.5
-
48
-
-
0031777693
-
Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines
-
Sapp M, Fligge C, Petzak I, Harris JR, Streeck RE Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines. J Virol. 72:1998;6186-6189.
-
(1998)
J Virol
, vol.72
, pp. 6186-6189
-
-
Sapp, M.1
Fligge, C.2
Petzak, I.3
Harris, J.R.4
Streeck, R.E.5
-
49
-
-
0032536896
-
Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
-
The authors describe mutational analysis that suggests that local conformational changes might control assembly into spherical shells or conical structures
-
von Schwedler UK, Stemmler TL, Klishko VY, Li S, Albertine KH, Davis DR, Sundquist WI Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J. 17:1998;1555-1568. The authors describe mutational analysis that suggests that local conformational changes might control assembly into spherical shells or conical structures.
-
(1998)
EMBO J
, vol.17
, pp. 1555-1568
-
-
Von Schwedler, U.K.1
Stemmler, T.L.2
Klishko, V.Y.3
Li, S.4
Albertine, K.H.5
Davis, D.R.6
Sundquist, W.I.7
-
50
-
-
0031954466
-
N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
-
Gross I, Hohenberg H, Huckhagel C, Krausslich HG N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J Virol. 72:1998;4798-4810.
-
(1998)
J Virol
, vol.72
, pp. 4798-4810
-
-
Gross, I.1
Hohenberg, H.2
Huckhagel, C.3
Krausslich, H.G.4
-
51
-
-
0030937751
-
Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
-
Conway JF, Cheng N, Zlotnick A, Wingfield PT, Stahl SJ, Steven AC Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:1997;91-94.
-
(1997)
Nature
, vol.386
, pp. 91-94
-
-
Conway, J.F.1
Cheng, N.2
Zlotnick, A.3
Wingfield, P.T.4
Stahl, S.J.5
Steven, A.C.6
-
52
-
-
0031571162
-
An atomic model of the outer layer of the bluetongue virus core derived from X-ray crystallography and electron cryomicroscopy
-
Grimes JM, Jakana J, Ghosh M, Basak AK, Roy P, Chiu W, Stuart DI, Prasad BV An atomic model of the outer layer of the bluetongue virus core derived from X-ray crystallography and electron cryomicroscopy. Structure. 5:1997;885-893.
-
(1997)
Structure
, vol.5
, pp. 885-893
-
-
Grimes, J.M.1
Jakana, J.2
Ghosh, M.3
Basak, A.K.4
Roy, P.5
Chiu, W.6
Stuart, D.I.7
Prasad, B.V.8
-
53
-
-
1842409555
-
Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
-
Böttcher B, Wynne SA, Crowther RA Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91.
-
(1997)
Nature
, vol.386
, pp. 88-91
-
-
Böttcher, B.1
Wynne, S.A.2
Crowther, R.A.3
-
54
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis PJ MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
-
(1991)
J Appl Crystallogr
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
|