FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W255468937> ?p ?o ?g. }

• W255468937 abstract "Ascovirus infection of lepidopteran larvae leads to an accumulation of virion- containing vesicles in the hemolymph turning it opaque white. The unusual feature of the formation of virion-filled vesicles by these large, complex, double-stranded DNA viruses results from a process similar to apoptosis, but one modified to rescue the developing apoptotic bodies for viral reproduction and virion dissemination. Another unusual feature of these viruses is their dependence on transmission by endoparasitic wasps that deposit their eggs in a lepidopteran host. Four species of ascoviruses have been sequenced and reveal a range of genes involved in apoptosis, RNA metabolism, and lipid metabolism. In the present dissertation, the research focuses on characterization of a novel type of DNA binding protein, P64 along with its homologs, responsible for condensing viral genomic DNA as part of the process of virion assembly. Proteomic, electron microscopic, and biochemical studies demonstrated that P64 is a major virion protein which bound to and condensed DNA prior to virion core formation and envelopment. Mobility shift assays, bioinformatics, and additional electron microscopy data provided strong evidence that P64 and its homologs constitute a novel family of DNA condensing proteins. The combination of P64's highly basic nature, its large size relative to known viral/eukaryotic genome condensing proteins, its non-specific DNA binding activity, and the presence of two distinct and unique domains suggest that these proteins evolved in certain complex DNA viruses to condense and assist the packaging of newly synthesized viral genomes as part of the assembly of progeny virions. Preliminary data suggest that P64 might associate with other virion structural proteins once it has bound to condensed DNA. Finally, phylogenetic analyses and results of binding studies showed that P64 is related to DNA binding proteins from viruses of the closely related Iridoviridae family, which provided additional evidence that the ascoviruses evolved from iridoviruses." @default.
• W255468937 created "2016-06-24" @default.
• W255468937 creator A5048722087 @default.
• W255468937 date "2010-01-01" @default.
• W255468937 modified "2023-09-27" @default.
• W255468937 title "Molecular Characterization of a Novel Class of DNA Binding Proteins" @default.
• W255468937 hasPublicationYear "2010" @default.
• W255468937 type Work @default.
• W255468937 sameAs 255468937 @default.
• W255468937 citedByCount "0" @default.
• W255468937 crossrefType "journal-article" @default.
• W255468937 hasAuthorship W255468937A5048722087 @default.
• W255468937 hasConcept C104317684 @default.
• W255468937 hasConcept C141231307 @default.
• W255468937 hasConcept C54355233 @default.
• W255468937 hasConcept C552990157 @default.
• W255468937 hasConcept C70721500 @default.
• W255468937 hasConcept C86803240 @default.
• W255468937 hasConcept C95444343 @default.
• W255468937 hasConceptScore W255468937C104317684 @default.
• W255468937 hasConceptScore W255468937C141231307 @default.
• W255468937 hasConceptScore W255468937C54355233 @default.
• W255468937 hasConceptScore W255468937C552990157 @default.
• W255468937 hasConceptScore W255468937C70721500 @default.
• W255468937 hasConceptScore W255468937C86803240 @default.
• W255468937 hasConceptScore W255468937C95444343 @default.
• W255468937 hasLocation W2554689371 @default.
• W255468937 hasOpenAccess W255468937 @default.
• W255468937 hasPrimaryLocation W2554689371 @default.
• W255468937 hasRelatedWork W1501428507 @default.
• W255468937 hasRelatedWork W1775400131 @default.
• W255468937 hasRelatedWork W1946658043 @default.
• W255468937 hasRelatedWork W1963733416 @default.
• W255468937 hasRelatedWork W1977801631 @default.
• W255468937 hasRelatedWork W1983507701 @default.
• W255468937 hasRelatedWork W2068100213 @default.
• W255468937 hasRelatedWork W2075579583 @default.
• W255468937 hasRelatedWork W2094061221 @default.
• W255468937 hasRelatedWork W2138803959 @default.
• W255468937 hasRelatedWork W2154947282 @default.
• W255468937 hasRelatedWork W2158159622 @default.
• W255468937 hasRelatedWork W2161725266 @default.
• W255468937 hasRelatedWork W2440495642 @default.
• W255468937 hasRelatedWork W2514377229 @default.
• W255468937 hasRelatedWork W2604714425 @default.
• W255468937 hasRelatedWork W2765364193 @default.
• W255468937 hasRelatedWork W3049542845 @default.
• W255468937 hasRelatedWork W3087182845 @default.
• W255468937 hasRelatedWork W70589615 @default.
• W255468937 isParatext "false" @default.
• W255468937 isRetracted "false" @default.
• W255468937 magId "255468937" @default.
• W255468937 workType "article" @default.