Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase
Author:
Publisher
Wiley
Subject
Cell Biology,Plant Science,Genetics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.0960-7412.2001.01200.x/fullpdf
Reference50 articles.
1. Biological significance of divalent cation binding to 14-3-3 proteins in relationship to nitrate reductase inactivation;Athwal;Plant Cell Physiol.,1998a
2. Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins;Athwal;Plant Physiol.,1998b
3. Modulation of 14-3-3 interactions with target proteins by physical and metabolic effectors;Athwal;Plant Cell Physiol.,2000
4. Partial purification and characterization of a calcium-dependent protein kinase and an inhibitor protein required for inactivation of spinach leaf nitrate reductase;Bachmann;Plant Physiol.,1995
5. Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase;Bachmann;Plant Cell,1996a
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