Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Fiona M. Pringle"'
Autor:
Cheryl T. Walter, Pablo de Felipe, Fiona M. Pringle, L. Andrew Ball, Martin D. Ryan, Ritah Nakayinga, Rosemary A. Dorrington
Publikováno v:
Journal of General Virology. 91:2826-2835
Providence virus (PrV) is a member of the family Tetraviridae, a family of small, positive-sense, ssRNA viruses that exclusively infect lepidopteran insects. PrV is the only known tetravirus that replicates in tissue culture. We have analysed the gen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5bb75a411837f7cd8ebd9e19952595a
https://doi.org/10.1099/vir.0.023796-0
https://doi.org/10.1099/vir.0.023796-0
Autor:
Padmaja Natarajan, L. Andrew Ball, Jeffrey A. Speir, Derek James Taylor, John E. Johnson, Fiona M. Pringle
Publikováno v:
Structure. 18(6):700-709
The T = 4 tetravirus and T = 3 nodavirus capsid proteins undergo closely similar autoproteolysis to produce the N-terminal beta and C-terminal, lipophilic gamma polypeptides. The gamma peptides and the N termini of beta also act as molecular switches
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef037c0acf220481b5e2574174d34fa
Autor:
L. A. Ball, Vijay S. Reddy, Fiona M. Pringle, John E. Johnson, Gino Cingolani, Jeffrey A. Speir, D. J. Taylor
Publikováno v:
Archives of Virology. 151:155-165
Providence Virus (PrV) is a non-envoloped, T = 4 icosahedral beta-tetravirus that undergoes autocatalytic cleavage of its coat protein precursor after capsid assembly. This is also a well characterized function of Nudaurelia capensis omega virus (Nom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::005eea0dd1d1a001491d41bcc312c19a
https://doi.org/10.1007/s00705-005-0637-3
https://doi.org/10.1007/s00705-005-0637-3
Publikováno v:
Virology. 306:359-370
We identified a new member of the Tetraviridae, Providence virus (PrV), persistently infecting a midgut cell line derived from the corn earworm (Helicoverpa zea). Virus purified from these cells also productively infected a H. zea fat body cell line,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a908b4804d506bf4b49db389a388dcd9
https://doi.org/10.1016/s0042-6822(02)00052-1
https://doi.org/10.1016/s0042-6822(02)00052-1
Autor:
Brian T. Luke, Terry N. Hanzlik, Jean Louis Zeddam, Fiona M. Pringle, James Kalmakoff, Vernon K. Ward, Craig E. Cameron, Alexander E. Gorbalenya, Karl H.J. Gordon
Publikováno v:
Journal of Molecular Biology
Template-dependent polynucleotide synthesis is catalyzed by enzymes whose core component includes a ubiquitous alphabeta palm subdomain comprising A, B and C sequence motifs crucial for catalysis. Due to its unique, universal conservation in all RNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3b1275320a8aa8104677d7acd26d960
https://doi.org/10.1016/s0022-2836(02)01033-1
https://doi.org/10.1016/s0022-2836(02)01033-1
Publikováno v:
The Journal of general virology. 82(Pt 1)
Thosea asignavirus (TaV), a putative member of the genusBetatetravirusof the familyTetraviridae, is predicted to have a novel capsid expression strategy compared with other characterized tetraviruses. The capsid precursor protein is cleaved twice to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d47560b84c737e8008bc7c033295bf9c
https://pubmed.ncbi.nlm.nih.gov/11125178
https://pubmed.ncbi.nlm.nih.gov/11125178
Autor:
Paul D. Scotti, Terry N. Hanzlik, Fiona M. Pringle, Karl H.J. Gordon, James Kalmakoff, Vernon K. Ward
Publikováno v:
The Journal of general virology. 80
This paper presents evidence that Thosea asigna virus (TaV) has a unique capsid expression strategy and is a member of the Nudaurelia beta-like genus of the Tetraviridae. Electron microscopy of TaV particles indicated a 38 nm, T = 4 icosahedral capsi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::783adc4743436c1b656c08065e265bf6
https://pubmed.ncbi.nlm.nih.gov/10423156
https://pubmed.ncbi.nlm.nih.gov/10423156