{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xie Y"],"funding":["NIA NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["9501-9512"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8162070"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(35)"],"pubmed_abstract":["The cell membrane is composed of a network of glycoconjugates including glycoproteins and glycolipids that presents a dense matrix of carbohydrates playing critical roles in many biological processes. Lectin-based technology has been widely used to characterize glycoconjugates in tissues and cell lines. However, their specificity toward their putative glycan ligand and sensitivity <i>in situ</i> have been technologically difficult to study. Additionally, because they recognize primarily glycans, the underlying glycoprotein targets are generally not known. In this study, we employed lectin proximity oxidative labeling (Lectin PROXL) to identify cell surface glycoproteins that contain glycans that are recognized by lectins. Commonly used lectins were modified with a probe to produce hydroxid"],"journal":["Chemical science"],"pubmed_title":["Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics."],"pmcid":["PMC8162070"],"funding_grant_id":["R01 AG062240","RO1GM049077","RO1 AG062240","R01 GM049077"],"pubmed_authors":["Lebrilla CB","Sheng Y","Xie Y","Li Q","Ju S","Reyes J"],"additional_accession":[]},"is_claimable":false,"name":"Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics.","description":"The cell membrane is composed of a network of glycoconjugates including glycoproteins and glycolipids that presents a dense matrix of carbohydrates playing critical roles in many biological processes. Lectin-based technology has been widely used to characterize glycoconjugates in tissues and cell lines. However, their specificity toward their putative glycan ligand and sensitivity <i>in situ</i> have been technologically difficult to study. Additionally, because they recognize primarily glycans, the underlying glycoprotein targets are generally not known. In this study, we employed lectin proximity oxidative labeling (Lectin PROXL) to identify cell surface glycoproteins that contain glycans that are recognized by lectins. Commonly used lectins were modified with a probe to produce hydroxid","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-05-07T22:53:16.376Z","creation":"2022-02-10T14:09:19.858Z"},"accession":"S-EPMC8162070","cross_references":{"pubmed":["34094216"],"doi":["10.1039/d0sc04199h"]}}