A comprehensive landscape of human organ N-glycoproteome

A comprehensive landscape of human organ N-glycoproteome | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article A comprehensive landscape of human organ N-glycoproteome Zhixin Tian, ming bi, Tao Wang, Chao Qin, Yanggang Yuan, Suideng Qin, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-5869453/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted You are reading this latest preprint version Abstract N-glycosylation, as a common post-translational modification with enormous structures, plays key roles in protein folding, cellular recognition and signaling pathways. State-of-the-art mass spectrometry-based N-glycoproteomics has enabled deep N-glycoproteome characterization of various human organs. However, a comprehensive N-glycoproteome landscape of human organs remains lacking. Here we present a systematic human N-glycoproteome atlas spanning 18 organs/tissues with identification of 31,003 N-glycan structure-level and 14,043 monosaccharide composition-level intact N-glycopeptides on 5,539 N-glycosites of 3,681 N-glycoproteins. Tissue-specific N-glycosylation patterns, novel glycoforms and crosstalk between sialylation and fucosylation are observed. This atlas, complemented by a unified multi-software analysis framework, provides insights into organ-specific glycobiology and establishes a fundamental reference for understanding physiological N-glycosylation characteristics of human tissues. Biological sciences/Biotechnology/Proteomics Biological sciences/Biotechnology/Expression systems N-glycoproteome human N-glycoproteomics draft structure-specific Full Text Additional Declarations There is NO Competing Interest. Supplementary Files SupplementaryTables.xlsx Supplementary Tables Cite Share Download PDF Status: Under Review Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-5869453","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":406341601,"identity":"335e30db-1ff7-4cf6-9737-379ac750ef48","order_by":0,"name":"Zhixin 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