| P2093 | author name string | H Weiner | |
| | W M Kaiser | |
| P2860 | cites work | Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine | Q24322674 |
| | Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways | Q27729753 |
| | 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins | Q35624026 |
| | A conserved acidic motif in the N-terminal domain of nitrate reductase is necessary for the inactivation of the enzyme in the dark by phosphorylation and 14-3-3 binding | Q38329724 |
| | Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. | Q38353528 |
| | Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase | Q44866783 |
| | Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins | Q44870214 |
| | Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors | Q44873348 |
| | Partial Purification and Characterization of a Calcium-Dependent Protein Kinase and an Inhibitor Protein Required for Inactivation of Spinach Leaf Nitrate Reductase | Q44878394 |
| | Ser-534 in the hinge 1 region of Arabidopsis nitrate reductase is conditionally required for binding of 14-3-3 proteins and in vitro inhibition | Q46345290 |
| | The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein | Q71171758 |
| | Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion | Q72310731 |
| | Nitrate reductases from leaves of Ricinus (Ricinus communis L.) and spinach (Spinacia oleracea L.) have different regulatory properties | Q74188472 |
| | Characterization of Nitrate Reductase from Light- and Dark-Exposed Leaves (Comparison of Different Species and Effects of 14-3-3 Inhibitor Proteins) | Q74770697 |
| | Identification of a Protein That Inhibits the Phosphorylated Form of Nitrate Reductase from Spinach (Spinacia oleracea) Leaves | Q74781240 |
| | Antibodies That Distinguish between the Serine-158 Phospho- and Dephospho-Form of Spinach Leaf Sucrose-Phosphate Synthase | Q74781499 |
| | 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 | Q77532353 |
| | Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins | Q77790311 |
| | 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves | Q78068276 |
| | The 14-3-3 proteins: cellular regulators of plant metabolism | Q78172717 |
| P433 | issue | 2-3 | |
| P304 | page(s) | 217-220 | |
| P577 | publication date | 2000-09-01 | |
| P1433 | published in | FEBS Letters | Q1388051 |
| P1476 | title | Binding to 14-3-3 proteins is not sufficient to inhibit nitrate reductase in spinach leaves | |
| P478 | volume | 480 | |