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Furthermore, if the enzymes can tolerate substrate analogs, it becomes possible to engineer chemically modified proteins in a site-specific fashion.
The present work significantly enlarges the number of N-terminally modified proteins in bacteria and confirms that these modifications are a general and fundamental process, not only restricted to eukaryotes.
Enolase1 is one of the most consistently up-regulated and oxidatively modified proteins in brain of subjects of early-onset AD [34].
It also even has the potential to produce modified proteins in a variety of cells.
Similarly, finding all modified proteins in a complex or reaction can be retrieved with predefined queries.
This likely underestimates the basal level of post-translationally modified proteins in samples not exposed to H2O2, but these levels are usually quite low.
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Query: 'Find all modified proteins in a pathway' —this query enables users to retrieve modified proteins associated with Reactome pathway(s) of interest for further analysis.
Moreover, CML-modified proteins in glyoxal-treated cells were shown to be substrates for ubiquitin conjugation, suggesting a potential mechanism by which these modified proteins may be marked for degradation [48].
The antibody CTD110.6 was used to detect O-GlcNAc-modified proteins in immunoprecipitates.
We detected O-GlcNAc-modified proteins in nonvernalized, vernalized and devernalized wheat plants using the monoclonal antibody CTD110.6 originally produced to specifically recognize Ser- or Thr-O-GlcNAc-modified proteins in animal cells [34].
The production of N-GlcNAc2-modified proteins in T24 and some cancer cell line cells may require the deprivation of sugar.
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