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- W2477335912 abstract ".Within the biochemical approaches of proteomics, adistinction can be made between ‘expression proteomics’and ‘interaction proteomics’. In the former, the total pro-tein complement of a tissue, cell homogenate or bodyfluid is prepared in two physiological states (e.g. normaland diseased), separated by 2D gel electrophoresis andsurveyed for differences in protein expression by stainingand image analysis. Up- or downregulated proteins cansubsequently be identified by mass spectrometry (MS).Although expression proteomics holds the attraction ofmonitoring many cellular responses to a changed physio-logical state in parallel, there are several inherent disadvan-tages that limit its scope.The dynamic range (the variationin the abundance of proteins in total protein preparations)can exceed 10" @default.
- W2477335912 created "2016-08-23" @default.
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- W2477335912 date "2000-01-01" @default.
- W2477335912 modified "2023-09-27" @default.
- W2477335912 title "Protein-interaction mapping for functional proteomics Proteomics techniques aimed at identifying protein-protein interactions have been used successfully to characterize multiprotein complexes such as the spliceosome, the nuclear-pore complex and transient complexes in cell signaling. This has led to important biological insights. 'Interaction proteomics' is now ready for the large-scale, unbiased exploration of complexes, cellular structures and pathways." @default.
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