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The baculovirus expression system is now a widely accepted tool for the expression of recombinant proteins with many features to recommend it. Selection of recombinants is rapid compared to mammalian expression systems, whereas the capacity to perform many posttranslational modifications necessary for the expression of authentic, functional proteins is retained. Examples of glycosylation (
1
), phosphorylation (
2
), myristilation (
3
), palmitoylation (
4
), and carboxy-methylation (
5
) are among the many modifications reported. In addition, coexpression of related proteins in the baculovirus system appears to provide an ideal medium for the study of protein-protein interactions (
6
–
8
) and the assembly of virus particles (
9
–
13
).