Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "This substrate (ELK1) could be phosphorylated to a stoichiometry of 3.3 mol of phosphate by incubation with homogeneous ERKI, consistent with the presence of at least four phosphorylation sites....Peptide B contained only one serine, thus pinpointing the phosphorylation site S389.....S324 and S422 are inferred as the phosphorylated sites in peptides D and E, respectively. These peptides were highly purified and each contained exclusively serine phosphate. C appeared to contain only one serine, thus strongly suggesting that S383 is also a site.....The phosphopeptide maps also demonstrate phosphorylation of T336, not identified previously by peptide sequencing." ?g. }

• _5 value "This substrate (ELK1) could be phosphorylated to a stoichiometry of 3.3 mol of phosphate by incubation with homogeneous ERKI, consistent with the presence of at least four phosphorylation sites....Peptide B contained only one serine, thus pinpointing the phosphorylation site S389.....S324 and S422 are inferred as the phosphorylated sites in peptides D and E, respectively. These peptides were highly purified and each contained exclusively serine phosphate. C appeared to contain only one serine, thus strongly suggesting that S383 is also a site.....The phosphopeptide maps also demonstrate phosphorylation of T336, not identified previously by peptide sequencing." provenance.
• _5 value "This substrate (ELK1) could be phosphorylated to a stoichiometry of 3.3 mol of phosphate by incubation with homogeneous ERKI, consistent with the presence of at least four phosphorylation sites....Peptide B contained only one serine, thus pinpointing the phosphorylation site S389.....S324 and S422 are inferred as the phosphorylated sites in peptides D and E, respectively. These peptides were highly purified and each contained exclusively serine phosphate. C appeared to contain only one serine, thus strongly suggesting that S383 is also a site.....The phosphopeptide maps also demonstrate phosphorylation of T336, not identified previously by peptide sequencing." provenance.
• _5 value "This substrate (ELK1) could be phosphorylated to a stoichiometry of 3.3 mol of phosphate by incubation with homogeneous ERKI, consistent with the presence of at least four phosphorylation sites....Peptide B contained only one serine, thus pinpointing the phosphorylation site S389.....S324 and S422 are inferred as the phosphorylated sites in peptides D and E, respectively. These peptides were highly purified and each contained exclusively serine phosphate. C appeared to contain only one serine, thus strongly suggesting that S383 is also a site.....The phosphopeptide maps also demonstrate phosphorylation of T336, not identified previously by peptide sequencing." provenance.
• _5 value "This substrate (ELK1) could be phosphorylated to a stoichiometry of 3.3 mol of phosphate by incubation with homogeneous ERKI, consistent with the presence of at least four phosphorylation sites....Peptide B contained only one serine, thus pinpointing the phosphorylation site S389.....S324 and S422 are inferred as the phosphorylated sites in peptides D and E, respectively. These peptides were highly purified and each contained exclusively serine phosphate. C appeared to contain only one serine, thus strongly suggesting that S383 is also a site.....The phosphopeptide maps also demonstrate phosphorylation of T336, not identified previously by peptide sequencing." provenance.