Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

This publication has 26 references indexed in Scilit:

• 14‐3‐3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform‐specific manner and reduce dephosphorylation of Ser‐543 by endogenous protein phosphatases
  FEBS Letters, 1996
• Plant metabolism: Enzyme regulation by 14-3-3 proteins
  Current Biology, 1996
• Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
  Current Biology, 1996
• The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14‐3‐3 protein
  FEBS Letters, 1996
• The H+-ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation
  FEBS Letters, 1996
• Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
  Cell, 1996
• The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins
  FEBS Letters, 1994
• Purification and photoaffinity labeling of fusicoccin receptors from maize
  European Journal of Biochemistry, 1993
• Fusicoccin Activates the Plasma Membrane H+-ATPase by a Mechanism Involving the C-Terminal Inhibitory Domain.
  Plant Cell, 1993
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976