• Cholesterol depletion inhibits Na+,K+-ATPase activity in a near-native membrane environment 

      Garcia, Alvaro; Lev, Bogdan; Hossain, Khondker R.; Gorman, Amy; Diaz, Dil; Pham, T. H. Nguyen; Cornelius, Flemming; Allen, Toby W.; Clarke, Ronald J.
      Published 2019-02-15
      Cholesterol’s effects on Na+,K+-ATPase reconstituted in phospholipid vesicles have been extensively studied. However, previous studies have reported both cholesterol-mediated stimulation and inhibition of Na+,K+-ATPase ...
      Open Access
      Article
    • Electrostatic stabilization plays a central role in autoinhibitory regulation of the Na+,K+-ATPase 

      Jiang, Qiucen; Garcia, Alvaro; Han, Minwoo; Cornelius, Flemming; Apell, Hans-Jurgen; Khandelia, Himanshu; Clarke, Ronald J.
      Published 2017-01-24
      The Na+,K+-ATPase is present in the plasma membrane of all animal cells. It plays a crucial role in maintaining the Na+ and K+ electrochemical potential gradients across the membrane, which are essential in numerous ...
      Open Access
      Article
    • Glutathionylation-dependence of N+-K+-pump currents can mimic reduced subsarcolemmal Na+ diffusion 

      Garcia, Alvaro; Liu, Chia-Chi; Cornelius, Flemming; Clarke, Ronald J.; Rasmussen, Helge H.
      Published 2016-03-01
      The existence of a subsarcolemmal space with restricted diffusion for Na+ in cardiac myocytes has been inferred from a transient peak electrogenic Na+-K+ pump current beyond steady state on re-exposure of myocytes to K+ ...
      Open Access
      Article
    • Identification of electric-field-dependent steps in the Na+,K+-pump cycle 

      Mares, Laura J.; Garcia, Alvaro; Rasmussen, Helge H.; Cornelius, Flemming; Mahmmoud, Yasser A.; Berlin, Joshua R.; Lev, Bogdan; Allen, Toby W.; Clarke, Ronald J.
      Published 2014-09-01
      The charge transporting activity of the Na+,K+-ATPase depends on its surrounding electric field. To isolate which steps of the enzyme’s reaction cycle involve charge movement we have investigated the response of the ...
      Open Access
      Article
    • Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes 

      Nguyen, Khoa; Garcia, Alvaro; Sani, Marc-Antoine; Diaz, Dil; Dubey, Vikas; Clayton, Daniel; Dal Poggetto, Giovanni; Cornelius, Flemming; Payne, Richard J.; Separovic, Frances; Khandelia, Himanshu; Clarke, Ronald J.
      Published 2018-03-06
      The Na+,K+-ATPase, which is present in the plasma membrane of all animal cells, plays a crucial role in maintaining the Na+ and K+ electrochemical potential gradients across the membrane. Recent studies have suggested that ...
      Open Access
      Article
    • Membrane accessibility of glutathione 

      Garcia, Alvaro; Eljack, Nasma D.; Sani, Marc-Antoine; Separovic, Frances; Rasmussen, Helge H.; Kopec, Wojciech; Khandelia, Himanshu; Cornelius, Flemming; Clarke, Ronald J.
      Published 2015-07-30
      Regulation of the ion pumping activity of the Na+,K+-ATPase is crucial to the survival of animal cells. Recent evidence has suggested that the activity of the enzyme could be controlled by glutathionylation of cysteine ...
      Open Access
      Article
    • Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases 

      Hossain, Khondker Rufaka; Clayton, Daniel; Goodchild, Sophia C; Rodger, Alison; Payne, Richard James; Cornelius, Flemming; Ronald, James Clarke
      Published 2020-01-01
      Membrane protein structure and function are modulated via interactions with their lipid environment. This is particularly true for the integral membrane pumps, the P-type ATPases. These ATPases play vital roles in cell ...
      Article
    • The voltage-sensitive dye RH421 detects a Na+,K+-ATPase conformational change at the membrane interface 

      Garcia, Alvaro; Promod, Pratap R.; Lupfert, Christian; Cornelius, Flemming; Jacquemin, Denis; Lev, Bogdan; Allen, Toby W.; Clarke, Ronald J.
      Published 2017-01-20
      RH421 is a voltage-sensitive fluorescent styrylpyridinium dye which has often been used to probe the kinetics of Na+,K+-ATPase partial reactions. The origin of the dye’s response has up to now been unclear. Here we show ...
      Open Access
      Article