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http://hdl.handle.net/10261/39210
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Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Illana, Belén | - |
dc.contributor.author | Zaballos, Ángel | - |
dc.contributor.author | Blanco, Luis | - |
dc.contributor.author | Salas, Margarita | - |
dc.date.accessioned | 2011-09-01T12:51:02Z | - |
dc.date.available | 2011-09-01T12:51:02Z | - |
dc.date.issued | 1998-08-15 | - |
dc.identifier.citation | Virology 248(1): 12-19 (1980) | es_ES |
dc.identifier.issn | 0042-6822 | - |
dc.identifier.uri | http://hdl.handle.net/10261/39210 | - |
dc.description.abstract | The RGD (Arg-Gly-Asp) motif functions as a recognition site for adhesive proteins responsible for a number of cell–cell interactions. Certain viruses use this sequence as a receptor-binding site by interaction with cellular integrins. To elucidate the role of the RGD sequence of the ø29 terminal protein (TP), seven modified TPs were generated by site-directed mutagenesis. Most of the TP mutants were not efficiently used as primers, leading to a reduction of the TP-dAMP complex formation in the presence of the ø29 TP-DNA template. Moreover, these mutant TPs were poorly deoxyadenylylated by ø29 DNA polymerase in the absence of template. Analysis of primer TP/DNA polymerase complex formation showed that the modified TPs were affected in the formation of the heterodimeric complex. These results indicate that the RGD sequence present in ø29 TP is primarily involved in interaction with the viral DNA polymerase. | es_ES |
dc.description.sponsorship | This investigation was supported by research grant 5RO1 GM27242–18 from the National Institutes of Health, by grant No. PB93– 0173 from the Direccio´n General de Investigacio´n Cientı´fica y Te´cnica, by grant CHRX-CT 93–0248 from the European Economic Community, and by an institutional grant from Fundacio´n Ramo´n Areces. B.I. was recipient of a predoctoral fellowship from Ministerio de Educacio´ n y Ciencia. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Elsevier | es_ES |
dc.rights | closedAccess | es_ES |
dc.title | The "RGD" sequence in phage ø29 terminal protein is required for interaction with ø29 DNA polymerase | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1006/viro.1998.9276 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1006/viro.1998.9276 | es_ES |
dc.contributor.funder | National Institutes of Health (US) | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.contributor.funder | European Commission | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.contributor.funder | Ministerio de Educación y Ciencia (España) | - |
dc.identifier.funder | http://dx.doi.org/10.13039/100000002 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000780 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
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