<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Andrade-Silva D</submitter><funding>Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)</funding><funding>MCTI | Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)</funding><pagination>1261-1284</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6030720</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>17(7)</volume><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 &lt;i>Bothrops&lt;/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 &lt;i>Bothrops&lt;/i> species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separat</pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pubmed_title>Structures of N-Glycans of &lt;i>Bothrops&lt;/i> Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes.</pubmed_title><pmcid>PMC6030720</pmcid><funding_grant_id>2014/12245–0</funding_grant_id><funding_grant_id>2013/13548–4</funding_grant_id><funding_grant_id>2013/07467–1</funding_grant_id><funding_grant_id>308133/2015–3</funding_grant_id><funding_grant_id>2013/14651–3</funding_grant_id><pubmed_authors>Travaglia Cardoso SR</pubmed_authors><pubmed_authors>Tran T</pubmed_authors><pubmed_authors>Zelanis A</pubmed_authors><pubmed_authors>Serrano SMT</pubmed_authors><pubmed_authors>Lopes AS</pubmed_authors><pubmed_authors>Reinhold V</pubmed_authors><pubmed_authors>Andrade-Silva D</pubmed_authors><pubmed_authors>Ashline D</pubmed_authors><pubmed_authors>Reis MDS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structures of N-Glycans of &lt;i>Bothrops&lt;/i> Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes.</name><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 &lt;i>Bothrops&lt;/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 &lt;i>Bothrops&lt;/i> species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separat</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Jul</publication><modification>2025-05-29T19:21:25.225Z</modification><creation>2025-05-29T19:21:25.225Z</creation></dates><accession>S-EPMC6030720</accession><cross_references><pubmed>29716988</pubmed><doi>10.1074/mcp.RA118.000748</doi><doi>10.1074/mcp.ra118.000748</doi></cross_references></HashMap>