{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pinheiro-Junior EL"],"funding":["São Paulo Research Foundation","F.W.O.-Vlaanderen","Johann Wolfgang Goethe-Universität, Frankfurt am Main","LOEWE TBG","EU COST Action","KU Leuven funding"],"pagination":["164"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11288129"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(1)"],"pubmed_abstract":["<h4>Background</h4>The identification of novel toxins from overlooked and taxonomically exceptional species bears potential for various pharmacological applications. The remipede Xibalbanus tulumensis, an underwater cave-dwelling crustacean, is the only crustacean for which a venom system has been described. Its venom contains several xibalbin peptides that have an inhibitor cysteine knot (ICK) scaffold.<h4>Results</h4>Our screenings revealed that all tested xibalbin variants particularly inhibit potassium channels. Xib<sub>1</sub> and xib<sub>13</sub> with their eight-cysteine domain similar to spider knottins also inhibit voltage-gated sodium channels. No activity was noted on calcium channels. Expanding the functional testing, we demonstrate that xib<sub>1</sub> and xib<sub>13</sub> inc"],"journal":["BMC biology"],"pubmed_title":["Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling."],"pmcid":["PMC11288129"],"funding_grant_id":["G0E7120N","GOC2319 N","CA19144 EUVEN","GOA4919 N","2016/04761-4","PDM/19/164"],"pubmed_authors":["Furst R","Hempel BF","Koludarov I","Erkoc P","Peigneur S","Isensee J","Tytgat J","von Reumont BM","Schiffmann S","Sennoner T","Hucho T","Alirahimi E","Pinheiro-Junior EL","Vilcinskas A"],"additional_accession":[]},"is_claimable":false,"name":"Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling.","description":"<h4>Background</h4>The identification of novel toxins from overlooked and taxonomically exceptional species bears potential for various pharmacological applications. The remipede Xibalbanus tulumensis, an underwater cave-dwelling crustacean, is the only crustacean for which a venom system has been described. Its venom contains several xibalbin peptides that have an inhibitor cysteine knot (ICK) scaffold.<h4>Results</h4>Our screenings revealed that all tested xibalbin variants particularly inhibit potassium channels. Xib<sub>1</sub> and xib<sub>13</sub> with their eight-cysteine domain similar to spider knottins also inhibit voltage-gated sodium channels. No activity was noted on calcium channels. Expanding the functional testing, we demonstrate that xib<sub>1</sub> and xib<sub>13</sub> inc","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-03T00:18:27.999Z","creation":"2026-04-22T03:11:59.952Z"},"accession":"S-EPMC11288129","cross_references":{"pubmed":["39075558"],"doi":["10.1186/s12915-024-01955-5"]}}