Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin.
about
Phosphorylation of Thr-948 at the C terminus of the plasma membrane H(+)-ATPase creates a binding site for the regulatory 14-3-3 protein14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphataseInvolvement of 14-3-3 proteins in nuclear localization of telomerase14-3-3 proteins interact with specific MEK kinasesData mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSGAS160 phosphotyrosine-binding domain constructs inhibit insulin-stimulated GLUT4 vesicle fusion with the plasma membraneNitrite-dependent nitric oxide production pathway: implications for involvement of active nitrogen species in photoinhibition in vivoEichhornia azurea decomposition and the bacterial dynamic: an experimental researchNitrate uptake and reduction in higher and lower plantsEvolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells.Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signallingDifferences in spatial expression between 14-3-3 isoforms in germinating barley embryos.14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesisThe mononuclear molybdenum enzymes.Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases.14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.Biochemical and molecular characterization of RcSUS1, a cytosolic sucrose synthase phosphorylated in vivo at serine 11 in developing castor oil seeds.Loss of ypk1 function causes rapamycin sensitivity, inhibition of translation initiation and synthetic lethality in 14-3-3-deficient yeast.Regulation of starch accumulation by granule-associated plant 14-3-3 proteinsMolybdenum enzymes in higher organisms.Coupling oxidative signals to protein phosphorylation via methionine oxidation in ArabidopsisMetabolic signalling and carbon partitioning: role of Snf1-related (SnRK1) protein kinase.Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism.Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processesDynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.14-3-3 proteins: a number of functions for a numbered protein.The 14-3-3 proteins of Arabidopsis regulate root growth and chloroplast development as components of the photosensory system.14-3-3 inhibits the Dictyostelium myosin II heavy-chain-specific protein kinase C activity by a direct interaction: identification of the 14-3-3 binding domainAn Integrated Biochemical, Proteomics, and Metabolomics Approach for Supporting Medicinal Value of Panax ginseng Fruits.A complex containing SNF1-related kinase (SnRK1) and adenosine kinase in ArabidopsisNitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Fusicoccin, 14-3-3 proteins, and defense responses in tomato plants.The 14-3-3 proteins associate with the plant plasma membrane H(+)-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system.Plant SnRK1 Kinases: Structure, Regulation, and Function.Regulation of autophagic activity by 14-3-3ζ proteins associated with class III phosphatidylinositol-3-kinase.In low transpiring conditions, nitrate and water fluxes for growth of B. napus plantlets correlate with changes in BnNrt2.1 and BnNrt1.1 transporter expressionLight modulated activity of root alkaline/neutral invertase involves the interaction with 14-3-3 proteins.Three spinach leaf nitrate reductase-3-hydroxy-3-methylglutaryl-CoA reductase kinases that are regulated by reversible phosphorylation and/or Ca2+ ions.
P2860
Q24543953-67F24B54-9B6B-47D6-9B73-0A9238FF00FCQ24681544-475F3281-50B4-4797-A66F-3969CA62D579Q24685623-2C174B19-2127-4611-823F-36F021B37672Q28260788-F9678B47-882D-4384-8455-A16C00539776Q28351256-68DFB09D-8717-4ACC-AB3E-1243AECEB276Q28363624-8BE1324B-C2EA-4809-9AD7-D4FAB69B8FB2Q28580015-9D53AB44-18DB-46CE-8216-DA866D79449AQ28765080-2AEB3657-3087-4471-91F6-DD03404E46D6Q28833717-133B4420-6A78-44F4-942B-DE7547832E8EQ29399561-10D6EF2F-E442-404E-BC0C-84B828875725Q30369786-0C03EB9C-0836-4FC5-B09B-33E02E814693Q30880095-FB90F81D-476E-4F94-BE69-0564BF4E59E4Q33291681-392635BD-1CA4-4860-BE4B-DF8D3705A14CQ33333980-023E276E-3728-4441-BCC7-90DCDC2A5BE4Q33584128-8435B03F-12C4-488C-8425-355607B95901Q33840734-687A7614-6208-449D-9FDE-8952D1085CDCQ34022222-AF9BFDF8-4096-40A6-91AF-7CC32F53C353Q34445338-14818C09-22D1-4EF4-B19C-9B53D6A82CD5Q34580327-D96CFB43-36F5-4014-ABDE-35CD37819E26Q34615601-2861EC82-750C-4E4B-8B1A-C96A00E0853DQ34627569-E188A62A-ADC0-4392-9845-6DA5FCF4174DQ34812986-BA3DBEA7-ED33-48AE-BCEC-057F0109BFC5Q34986830-48700748-E87C-4E14-8D48-8A7461B936F6Q35036751-FCF8CA71-447B-4682-A825-424CDBBB8946Q35036804-6FD9D8A3-079E-4351-987B-5D9EA9052F13Q35748563-82B4849B-CC92-416B-9DA9-E8CFE53CB053Q35787179-27EA956B-FB25-4779-8B44-60109C2EF3EDQ35841994-F658A53E-8231-4B4A-87FD-FF3F9F369F9BQ35955026-7B663E57-7FD5-48F3-BA9E-9C3EDCD516E0Q36927763-753D5134-BD43-4CAA-A6DB-312073A6D9D6Q37060360-9C5504B5-9136-4AF5-9A97-5A5F6F37A313Q37534636-3E77583D-5A61-45ED-83F2-8D9EEB8BC63EQ38318607-E00E5692-ECF3-4CE3-8CDF-01DEA2146E37Q38326154-6CA7B3C2-AE0C-4433-A6D5-D39FE4829F4AQ38335181-7EC8F3D1-72D7-4941-B4C5-C8D1DBCCDC1AQ38998431-9C653222-0047-4861-AD19-B72303C37E03Q39649364-07E699B7-6CC0-42EE-BAFB-AF2CEC4813EAQ40797350-0D028FCA-EAD6-43C5-9505-2EADFED78C5CQ42466195-3BECD502-6A4B-45DA-B16F-FD7685B4625CQ42716276-559B709A-8B79-41EB-A078-50D87458E42D
P2860
Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Phosphorylated nitrate reducta ...... s and activated by fusicoccin.
@en
type
label
Phosphorylated nitrate reducta ...... s and activated by fusicoccin.
@en
prefLabel
Phosphorylated nitrate reducta ...... s and activated by fusicoccin.
@en
P2093
P1433
P1476
Phosphorylated nitrate reducta ...... ns and activated by fusicoccin
@en
P2093
P304
P356
10.1016/S0960-9822(02)70677-5
P407
P577
1996-09-01T00:00:00Z