@article{RDM,
      author = {Zhu, Wendy and Silva, Jonathan R.},
      url = {http://data.library.wustl.edu/record/3},
      title = {Dataset for Figure 1: Mechanisms of non-Covalent  Subunit  Regulation of Nav Channel Gating and Pharmacology},
      abstract = {Voltage-gated Na+ (NaV) channels comprise a macromolecular  complex, whose members tailor their function according to  cell type. Key members are the non-covalently bound NaV 1  and 3 subunits that regulate channel gating, expression,  and pharmacology. To probe the molecular basis of this  regulation, we applied voltage-clamp fluorometry to measure  how the subunits affect conformations within the cardiac  NaV channel (NaV1.5) voltage-sensing domains (VSDs). The  pore-forming NaV1.5-subunit contains four domains (DI-DIV),  each with a VSD. Our results show that 1 and 3 regulate  NaV1.5 by altering DIII- and DIV-VSD activation, an  interaction that is significantly altered by atrial  fibrillation-variants in both subunits. 1 and 3 strongly  affected the interaction of Class Ib anti-arrhythmic drugs,  lidocaine and ranolazine, with the DIII-VSD. Our results  demonstrate that 1 and 3 regulation of the NaV1.5 VSDs can  significantly determine NaV1.5 pathology and its  therapeutic response.},
      number = {RDM},
      doi = {https://doi.org/10.7936/K7J102MF},
      recid = {3},
      pages = {268.5 MB},
      address = {2018-05-07},
}