• 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
    • Evidence for ATP interaction with phosphatidylcholine bilayers 

      Garcia, Alvaro; Pochinda, Simon; Elgaard-Jorgensen, Paninnguaq N.; Khandelia, Himanshu; Clarke, Ronald J.
      Published 2019-07-10
      ATP is a fundamental intracellular molecule and is thought to diffuse freely throughout the cytosol. Evidence obtained from nucleoside-sensing sarcolemmal ion channels and red blood cells, however, suggest that ATP is ...
      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