scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0014-5793(99)00868-6 |
P8608 | Fatcat ID | release_icdn2xbrxbaojdtcln525xb5ee |
P698 | PubMed publication ID | 10428475 |
P2093 | author name string | H Weiner | |
W M Kaiser | |||
P2860 | cites work | The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein | Q71171758 |
Plant metabolism: enzyme regulation by 14-3-3 proteins | Q71824288 | ||
Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion | Q72310731 | ||
Antibodies That Distinguish between the Serine-158 Phospho- and Dephospho-Form of Spinach Leaf Sucrose-Phosphate Synthase | Q74781499 | ||
Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins | Q77790311 | ||
Short-term effects of nitrate on sucrose synthesis in wheat leaves | Q86638539 | ||
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 | ||
A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity | Q28276506 | ||
Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins | Q28293607 | ||
The structural basis for 14-3-3:phosphopeptide binding specificity | Q29547190 | ||
Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation | Q29614709 | ||
14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins | Q35624026 | ||
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors | Q36237082 | ||
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 | ||
14-3-3 proteins: structure resolved, functions less clear | Q40427588 | ||
Nitrate: nutrient and signal for plant growth | Q40462834 | ||
Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins | Q44870214 | ||
Regulation of sucrose-phosphate-synthase activity in spinach leaves by protein level and covalent modification | Q44870508 | ||
Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways. | Q48667801 | ||
Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation | Q68156237 | ||
P433 | issue | 1-2 | |
P921 | main subject | proteolysis | Q33123 |
P304 | page(s) | 75-78 | |
P577 | publication date | 1999-07-01 | |
P1433 | published in | FEBS Letters | Q1388051 |
P1476 | title | 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves | |
P478 | volume | 455 |
Q34405540 | 14-3-3 proteins; bringing new definitions to scaffolding |
Q86434617 | 14-3-3 regulates 1-aminocyclopropane-1-carboxylate synthase protein turnover in Arabidopsis |
Q30880095 | 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells |
Q45153587 | A Robot-based platform to measure multiple enzyme activities in Arabidopsis using a set of cycling assays: comparison of changes of enzyme activities and transcript levels during diurnal cycles and in prolonged darkness |
Q42114522 | A model for the circadian oscillations in expression and activity of nitrate reductase in higher plants. |
Q35176852 | Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1. |
Q51949807 | Beta-subunits of the SnRK1 complexes share a common ancestral function together with expression and function specificities; physical interaction with nitrate reductase specifically occurs via AKINbeta1-subunit. |
Q73084597 | Binding to 14-3-3 proteins is not sufficient to inhibit nitrate reductase in spinach leaves |
Q34667579 | Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity. |
Q44764590 | Control of nitrate reductase by circadian and diurnal rhythms in tomato |
Q73907275 | Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties |
Q64240990 | Extensive Variations in Diurnal Growth Patterns and Metabolism Among spp. Strains |
Q73591709 | Increased glutamine synthetase activity and changes in amino acid pools in leaves treated with 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR) |
Q30475806 | Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions. |
Q35040499 | Metabolic enzymes as targets for 14-3-3 proteins |
Q52584644 | Nitrate Reductases Are Relocalized to the Nucleus by AtSIZ1 and Their Levels Are Negatively Regulated by COP1 and Ammonium. |
Q38078367 | Nitric oxide in plants: an assessment of the current state of knowledge. |
Q46681874 | Phosphorylation and subsequent interaction with 14-3-3 proteins regulate plastid glutamine synthetase in Medicago truncatula |
Q34053551 | Regulatory 14-3-3 protein-protein interactions in plant cells |
Q37425274 | Ribosome and transcript copy numbers, polysome occupancy and enzyme dynamics in Arabidopsis. |
Q36241760 | Role of 14-3-3 proteins in eukaryotic signaling and development |
Q34667530 | Sugar sensing and signaling in plants |
Q35166332 | The 14-3-3 proteins: gene, gene expression, and function |
Q39250062 | p70S6K1 (S6K1)-mediated Phosphorylation Regulates Phosphatidylinositol 4-Phosphate 5-Kinase Type I γ Degradation and Cell Invasion. |
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