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It is of note that the common features surrounding O-GlcNAc modification sites described here and before [ 9], which are apparent in the primary structure of a protein, can also be achieved or constituted in the secondary structure of proteins by residues present distantly from each other.
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All substrates harbour an acidic region as well as a Ser-Gly sequence, which have been described previously for CS and HS modification sites [ 25, 26].
Kinetic analysis of modification sites was performed using a label-free quantitation approach we described previously.
Fig. 1 Modification sites based on compound 1.
Site annotations list any structurally/functionally important sites (molecule processing sites, binding sites, modification sites, etc).
The use of C-terminal cysteines to promote formation of covalent dimers and for the purpose of site-specific modification has been described previously.
All datasets used, including 24 modifications in H and IMR90, various sequence-specific transcription factors, and DNase-I hypersensitivity sites, were described previously (Rajagopal et al. 2013).
Similar modifications have been described for the Magdalenian sites of Le Placard (Charente, France) and Isturitz (Pyrénées-Atlantiques, France).
b The modification described in the text.
More than two dozens of site-specific histone modifications have been described [13], [14], and the acetylation and methylation of lysine residues in the tails of nucleosomal histones have been shown to exert crucial influences on chromatin packaging and gene expression [15], [16].
These modifications are described in detail.
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