Distinguishing the interactions in the fructose-1,6-bisphosphate binding site of human liver pyruvate kinase that contribute to allostery

Lignende værker

• The phosphate moiety of phosphoenolpyruvate does NOT contribute to allosteric regulation of liver pyruvate kinase by fructose-1,6-bisphosphate
  af: Chappell, Benjamin M., et al.
  Udgivet: (2020)
• Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase
  af: Urness, James M., et al.
  Udgivet: (2012)
• The pH dependence of the allosteric response of human liver pyruvate kinase to fructose-1,6-bisphosphate, ATP, and alanine
  af: Fenton, Aron W., et al.
  Udgivet: (2009)
• The cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase.
  af: Murcott, T H, et al.
  Udgivet: (1992)
• Benchmarking predictions of allostery in liver pyruvate kinase in CAGI4
  af: Xu, Qifang, et al.
  Udgivet: (2017)