{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["25(15)"],"submitter":["Villa-Diaz F"],"pubmed_abstract":["(1) Background: voltage-gated sodium channels (Na<sub>v</sub>s) are integral membrane proteins that allow the sodium ion flux into the excitable cells and initiate the action potential. They comprise an α (Na<sub>v</sub>α) subunit that forms the channel pore and are coupled to one or more auxiliary β (Na<sub>v</sub>β) subunits that modulate the gating to a variable extent. (2) Methods: after performing homology in silico modeling for all nine isoforms (Na<sub>v</sub>1.1α to Na<sub>v</sub>1.9α), the Na<sub>v</sub>α and Na<sub>v</sub>β protein-protein interaction (PPI) was analyzed chemometrically based on the primary and secondary structures as well as topological or spatial mapping. (3) Results: our findings reveal a unique isoform-specific correspondence between certain segments of the ex"],"journal":["Molecules (Basel, Switzerland)"],"pagination":["E3551"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7435598"],"repository":["biostudies-literature"],"pubmed_title":["Chemometric Models of Differential Amino Acids at the Na<sub>v</sub>α and Na<sub>v</sub>β Interface of Mammalian Sodium Channel Isoforms."],"pmcid":["PMC7435598"],"pubmed_authors":["Scior T","Lopez-Nunez S","Salinas-Stefanon EM","Villa-Diaz F","Ruiz-Castelan JE"],"additional_accession":[]},"is_claimable":false,"name":"Chemometric Models of Differential Amino Acids at the Na<sub>v</sub>α and Na<sub>v</sub>β Interface of Mammalian Sodium Channel Isoforms.","description":"(1) Background: voltage-gated sodium channels (Na<sub>v</sub>s) are integral membrane proteins that allow the sodium ion flux into the excitable cells and initiate the action potential. They comprise an α (Na<sub>v</sub>α) subunit that forms the channel pore and are coupled to one or more auxiliary β (Na<sub>v</sub>β) subunits that modulate the gating to a variable extent. (2) Methods: after performing homology in silico modeling for all nine isoforms (Na<sub>v</sub>1.1α to Na<sub>v</sub>1.9α), the Na<sub>v</sub>α and Na<sub>v</sub>β protein-protein interaction (PPI) was analyzed chemometrically based on the primary and secondary structures as well as topological or spatial mapping. (3) Results: our findings reveal a unique isoform-specific correspondence between certain segments of the ex","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-05-03T00:11:53.266Z","creation":"2020-08-31T07:30:01Z"},"accession":"S-EPMC7435598","cross_references":{"pubmed":["32756517"],"doi":["10.3390/molecules25153551"]}}