The Ca(2+)-ATPase (SERCA1) Is Inhibited by 4-Aminoquinoline Derivatives through Interference with Catalytic Activation by Ca(2+), Whereas the ATPase E(2) State Remains Functional

Lignende værker

• Distinctive Features of Catalytic and Transport Mechanisms in Mammalian Sarco-endoplasmic Reticulum Ca(2+) ATPase (SERCA) and Cu(+) (ATP7A/B) ATPases
  af: Lewis, David, et al.
  Udgivet: (2012)
• Effects of High-Affinity Inhibitors on Partial Reactions, Charge Movements, and Conformational States of the Ca(2+) Transport ATPase (Sarco-Endoplasmic Reticulum Ca(2+) ATPase)
  af: Tadini-Buoninsegni, Francesco, et al.
  Udgivet: (2008)
• Ca(2+)/H(+) exchange, lumenal Ca(2+) release and Ca(2+)/ATP coupling ratios in the sarcoplasmic reticulum ATPase
  af: Inesi, Giuseppe, et al.
  Udgivet: (2013)
• High-yield Heterologous Expression of Wild Type and Mutant Ca(2+) ATPase: Characterization of Ca(2+) Binding Sites by Charge Transfer
  af: Liu, Yueyong, et al.
  Udgivet: (2009)
• Time-Resolved Charge Translocation by Sarcoplasmic Reticulum Ca-ATPase Measured on a Solid Supported Membrane
  af: Buoninsegni, Francesco Tadini, et al.
  Udgivet: (2004)