{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nBased on the information provided, the abstract (PubMed ID"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "does not mention or describe the function of LINC00367. Instead, it focuses on a proteome-wide phosphoproteomic analysis comparing the effectiveness of multiple proteases (Lys-N, Lys-C, and trypsin) in identifying and characterizing nonredundant phosphopeptides. The study highlights how employing a multiprotease approach significantly increases the number of detected phosphorylation sites and shifts the identifiable phosphorylation motifs compared to using trypsin alone. As such, there is no relevant data in this abstract regarding LINC00367.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sharon Gauci, Andreas O Helbig, Monique Slijper, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Anal Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/ac9004309"}], "href": "https://doi.org/10.1021/ac9004309"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19413330"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19413330"}]}]}]}