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- W43977963 abstract "With the number of complete genome sequences increasing at an ever-faster pace, we are getting sequence data for the full complement of proteins or “proteome” (Wasinger et al. 1995; Wilkins et al. 1996), encoded by various organisms. To understand how the proteome confers specific properties to a host cell, one needs to obtain information regarding several parameters, including the level of expression of all proteins, their posttranslational modifications, their cellular localizations, and their interactions with different partners (proteins, nucleic acids, etc.). This task is often complicated by the wide variety of expression levels of different proteins in a given cell: The steady-state level of cellular proteins may differ by several orders of magnitude even though they are encoded by genes approximately equally represented in the genome (Gygi et al. 2000). In recent years, mass spectrometry has become a powerful tool for protein identification at an" @default.
- W43977963 created "2016-06-24" @default.
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- W43977963 date "2002-01-01" @default.
- W43977963 modified "2023-09-27" @default.
- W43977963 title "Tandem Affinity Purification to Enhance Interacting Protein Identification" @default.
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