{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n CXorf51A is a small, 108–amino acid human protein that has recently been subjected to structural de‐orphanization to better understand its potential cellular roles. A combined approach using bioinformatics and nuclear magnetic resonance (NMR) spectroscopy has revealed that CXorf51A is an intrinsically disordered protein, as evidenced by comprehensive backbone and near–complete side‐chain chemical shift assignments (1). Its lack of a well–defined tertiary structure suggests that, rather than adopting a stable conformation, the protein may participate in cellular processes through transient or flexible interactions with other biomolecules. Although the precise biological function of CXorf51A remains to be elucidated, establishing its disordered nature constitutes a critical first step toward unraveling how this protein contributes to human cellular physiology (1)."}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christoph Wiedemann, Kingsley Benjamin Obika, Sandra Liebscher, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biomol NMR Assign (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s12104-021-10043-6"}], "href": "https://doi.org/10.1007/s12104-021-10043-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34415548"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34415548"}]}]}]}