{'fraction_non_alphanumeric': 0.033235581622678395, 'fraction_numerical': 0.0, 'mean_word_length': 6.062068965517241, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
System Metaglycomes: Mapping Dynamic Cell Surface N‐glycome, O‐glycome and Glycolipidome by Mass Spectrometry

Mammalian cell surface membranes are coated with a vast repertoire of glycan chains attached to proteins and lipids that play key roles in almost all biological processes involving cell‐cell adhesion, recognition, signaling, and growth. Aberrant expression of glycan moieties has been implicated in numerous congenital and acquired human diseases. Despite its potential for biomarker discovery, analysis of cell surface glycomes is challenging owing to the structural complexity and variety of glycan structures. Moreover, glycan structures and their spatial and temporal distribution of normal human and animal model tissues (e.g.: rodents) remain largely unknown. In this work, we developed a mass spectrometry‐based multimethod platform to obtain detailed profiles and characterize N‐glycans (N‐glycome), O‐glycans (O‐glycome), and glycolipids (Glycolipidome) from neonatal and adult mouse organs and tissues.