E
E.G. Westaway
Researcher at Monash University
Publications - 9
Citations - 360
E.G. Westaway is an academic researcher from Monash University. The author has contributed to research in topics: Glycoprotein & Mannose. The author has an hindex of 9, co-authored 9 publications receiving 359 citations.
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Journal ArticleDOI
Proteins specified by group B togaviruses in mammalian cells during productive infections
TL;DR: Seven nonstructural and two of the three virion proteins specified by each of Kunjin, dengue type 2, St. Louis encephalitis, and Japanese encephalopathy virus were labeled during replication in Vero and in PS cells which had been treated only with actinomycin.
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Strategy of the flavivirus genome: Evidence for multiple internal initiation of translation of proteins specified by Kunjin virus in mammalian cells
TL;DR: The results are interpreted as indicating that multiple internal initiation of translation occurs in flavivirus-infected cells.
Journal ArticleDOI
Replication of the flavivirus Kunjin: proteins, glycoproteins, and maturation associated with cell membranes.
R.W. Boulton,E.G. Westaway +1 more
TL;DR: Radioisotopic labeling experiments showed that virus-specific RNA and protein syntheses occur predominantly on smooth and rough membranes, respectively, and electrophoretic profiles of viral proteins were similar in all membrane fractions.
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Comparisons of togaviruses: Sindbis virus (group A) and Kunjin virus (group B)
R.W. Boulton,E.G. Westaway +1 more
TL;DR: Kunjin virus sedimented at three-quarters the rate of Sind Bis virus, but the cores obtained by deoxycholate treatment of Kunjin virions had properties similar to those reported for Sindbis virus cores (sedimentation coefficient, ribonuclease sensitivity, absence of phospholipid).
Journal ArticleDOI
Proteins and glycoproteins specified by the flavivirus Kunjin
E.G. Westaway,Marilyn Shew +1 more
TL;DR: Kunjin virus-specified proteins were readily resolved against a background of labeled host cell proteins in autoradiograms of slab gels after SDS-phosphate electrophoresis and unexpected complexity was observed among the glycoproteins.