{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Andrade-Silva D"],"funding":["Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)","MCTI | Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)"],"pagination":["1261-1284"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6030720"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(7)"],"pubmed_abstract":["The complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation. Glycosylation is the main post-translational modification (PTM) of viperid venoms but currently there is little understanding of how protein glycosylation impacts the variation of venom proteomes. We have previously reported that <i>Bothrops</i> venom glycoproteomes contain a core of components that markedly define their composition and parallel their phylogenetic classification. Here we extend those observations to eight <i>Bothrops</i> species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separat"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Structures of N-Glycans of <i>Bothrops</i> Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes."],"pmcid":["PMC6030720"],"funding_grant_id":["2014/12245–0","2013/13548–4","2013/07467–1","308133/2015–3","2013/14651–3"],"pubmed_authors":["Travaglia Cardoso SR","Tran T","Zelanis A","Serrano SMT","Lopes AS","Reinhold V","Andrade-Silva D","Ashline D","Reis MDS"],"additional_accession":[]},"is_claimable":false,"name":"Structures of N-Glycans of <i>Bothrops</i> Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes.","description":"The complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation. Glycosylation is the main post-translational modification (PTM) of viperid venoms but currently there is little understanding of how protein glycosylation impacts the variation of venom proteomes. We have previously reported that <i>Bothrops</i> venom glycoproteomes contain a core of components that markedly define their composition and parallel their phylogenetic classification. Here we extend those observations to eight <i>Bothrops</i> species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separat","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jul","modification":"2025-05-29T19:21:25.225Z","creation":"2025-05-29T19:21:25.225Z"},"accession":"S-EPMC6030720","cross_references":{"pubmed":["29716988"],"doi":["10.1074/mcp.RA118.000748","10.1074/mcp.ra118.000748"]}}