Skip to Main Content



  • Cover Image

    Cover Image

    issue cover

    Cover picture: Structural model of Xenopus α1/β3 Na+/K+ pump, based on dogfish Na+/K+-ATPase (Protein Data Bank accession no. 2ZXE; Shinoda et al. 2009. Nature. 459:446–450), with α (grey, with colored transmembrane helices), β (green surface), and γ (red helix) subunits. The Na+/K+ pump is found to be a hybrid transporter that mediates proton import during Na+/K+ exchange, and the proton route is identified. See Vedovato and Gadsby (449–464) and Hilgemann (437–441).

  • PDF Icon PDF LinkTable of Contents
  • PDF Icon PDF LinkEditorial Board
ISSN 0022-1295
EISSN 1540-7748

Generally Physiological



Research Articles

The Na+/K+ pump is a hybrid transporter that can also import protons at physiological K+ and Na+ concentrations.

The analgesic α-conotoxin Vc1.1 inhibits Cav2.3 channels through a GABAB receptor–dependent pathway involving c-Src.

Ex vivo analyses indicate that spontaneous activity in vestibular neurons depends on resting hair cell mechanotransduction and HCN channels in calyx terminals.

Agonists bind to sites on all four subunits to activate human ether-a-go-go–related gene 1 (hERG1) K+ channels.

Methods and Approaches

Nanoscale imaging of cultured cardiomyocytes allows the quantitative assessment of changes in the length of single sarcomeres during contractile events.

Close Modal
This Feature Is Available To Subscribers Only

Sign In or Create an Account

Close Modal
Close Modal