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- W2110441489 endingPage "749" @default.
- W2110441489 startingPage "730" @default.
- W2110441489 abstract "SUMMARY Studies of the functional proteins encoded by the poxvirus genome provide information about the composition of the virus as well as individual virus-virus protein and virus-host protein interactions, which provides insight into viral pathogenesis and drug discovery. Widely used proteomic techniques to identify and characterize specific protein-protein interactions include yeast two-hybrid studies and coimmunoprecipitations. Recently, various mass spectrometry techniques have been employed to identify viral protein components of larger complexes. These methods, combined with structural studies, can provide new information about the putative functions of viral proteins as well as insights into virus-host interaction dynamics. For viral proteins of unknown function, identification of either viral or host binding partners provides clues about their putative function. In this review, we discuss poxvirus proteomics, including the use of proteomic methodologies to identify viral components and virus-host protein interactions. High-throughput global protein expression studies using protein chip technology as well as new methods for validating putative protein-protein interactions are also discussed." @default.
- W2110441489 created "2016-06-24" @default.
- W2110441489 creator A5003839855 @default.
- W2110441489 creator A5005895051 @default.
- W2110441489 creator A5040591138 @default.
- W2110441489 creator A5047577001 @default.
- W2110441489 creator A5051810842 @default.
- W2110441489 creator A5076953309 @default.
- W2110441489 creator A5090031793 @default.
- W2110441489 date "2009-12-01" @default.
- W2110441489 modified "2023-10-16" @default.
- W2110441489 title "Poxvirus Proteomics and Virus-Host Protein Interactions" @default.
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