Polycations Globally Enhance Binding of 14-3-3ω to Target Proteins in Spinach Leaves
Author:
Publisher
Oxford University Press (OUP)
Subject
Cell Biology,Plant Science,Physiology,General Medicine
Link
http://academic.oup.com/pcp/article-pdf/47/6/764/19671385/pcj050.pdf
Reference28 articles.
1. Athwal, G.S. and Huber, S.C. (2002) Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase. Plant J.29: 119–129.
2. Athwal, G.S., Huber, J.L. and Huber, S.C. (1998) 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. Plant Physiol.118: 1041–1048.
3. Athwal, G.S., Lombardo, C., Huber, J.L., Masters, S.C., Fu, H. and Huber, S.C. (2000) Modulation of 14-3-3 interactions with target proteins by physical and metabolic effectors. Plant Cell Physiol.41: 523–533.
4. Bridges, D. and Moorhead, G.B.G. (2005) 14-3-3 proteins: a number of functions for a numbered protein. Sci. STKE re10/DC2.
5. Camoni, L., Visconti, S., Marra, M. and Aducci, P. (2001) Adenosine 5′-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H+-ATPase. J. Biol. Chem.276: 31709–31712.
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