Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
- 30 September 1996
- journal article
- Published by Elsevier in Current Biology
- Vol. 6 (9), 1104-1113
- https://doi.org/10.1016/s0960-9822(02)70677-5
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14‐3‐3 proteinFEBS Letters, 1996
- 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor.The Journal of cell biology, 1996
- Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of PhosphoserineCell, 1996
- Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leavesFEBS Letters, 1995
- Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase CMolecular and Cellular Biochemistry, 1995
- Isoforms of 14‐3‐3 protein can form homo‐ and heterodimers in vivo and in vitro: implications for function as adapter proteinsFEBS Letters, 1995
- Binding of 14-3-3 Proteins to the Protein Kinase Raf and Effects on Its ActivationScience, 1994
- Endogenous fusicoccin‐like ligand revealed in higher plants by radioreceptor and radioimmunoassaysFEBS Letters, 1994
- Partial purification of two proteins (100 kDa and 67 kDa) cooperating in the ATP-dependent inactivation of spinach leaf nitrate reductasePlanta, 1994
- Brain 14‐3‐3 protein is an activator protein that activates tryptophan 5‐monooxygenase and tyrosine 3‐monooxygenase in the presence of Ca2+,calmodulin‐dependent protein kinase IIFEBS Letters, 1987