FEBS Letters · 1999 · 28 citations · 27 references
Life SciencesBiochemistryMolecular BiologyMembrane BiochemistryMolecular VirologyVirologyViral InfectionsViral PathogenesisViral Protein ProcessingViral StructureVirus MorphologyVirus StructureStructural VirologyViral Envelope GlycoproteinsViral Envelope ProteinsViral Envelope StructureViral GlycoproteinsViral Surface ProteinsVirus-host Membrane InteractionsVirus-like Particles
An anti-ubiquitin cross-reactive protein which migrates more slowly (6.5 kDa) by SDS-PAGE than ubiquitin was identified in African swine fever virus particles. This protein was extracted into the detergent phase in Triton X-114 phase separations, showing that it is hydrophobic, and was radiolabelled with both [3H]palmitic acid and [32P]orthophosphate. This indicates that the protein has a similar structure to the membrane associated phosphatidyl ubiquitin described in baculovirus particles. A similar molecule was found in vaccinia virus and herpes simplex virus particles, suggesting that it may be a component of uninfected cell membranes, which is incorporated into membrane layers in virions during morphogenesis.
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Degradation of CFTR by the ubiquitin-proteasome pathway
Cristina L. Ward, Satoshi ŌMURA, Ron R. Kopito · Cell · 1995 · 1.3K citations · Full text
The Complete DNA Sequence of Autographa californica Nuclear Polyhedrosis Virus
Martin D. Ayres, Stephen C. Howard, John Kuzio et al. · Virology · 1994 · 964 citations