Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. (Q38353528)

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19 October 2019

title

Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin (English)

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19 October 2019

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19 October 2019

G Moorhead

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19 October 2019

P Douglas

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19 October 2019

N Morrice

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19 October 2019

M Scarabel

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19 October 2019

A Aitken

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19 October 2019

language of work or name

English

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publication date

1 September 1996

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19 October 2019

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19 October 2019

volume

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19 October 2019

issue

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19 October 2019

page(s)

1104-1113

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Nitrate: nutrient and signal for plant growth

19 October 2019

cites work

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7 January 2021

Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation

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7 January 2021

Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves

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7 January 2021

Identification of a Protein That Inhibits the Phosphorylated Form of Nitrate Reductase from Spinach (Spinacia oleracea) Leaves

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7 January 2021

Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase

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7 January 2021

Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion

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7 January 2021

Interaction of the protein kinase Raf-1 with 14-3-3 proteins

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7 January 2021

Activation of Raf-1 by 14-3-3 proteins

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7 January 2021

Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation

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Association of polyomavirus middle tumor antigen with 14-3-3 proteins

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Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family

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7 January 2021

Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells

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14-3-3 proteins associate with cdc25 phosphatases

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14-3-3 and its possible role in co-ordinating multiple signalling pathways

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14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins

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14-3-3 proteins: structure resolved, functions less clear

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7 January 2021

Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C

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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 II

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Exo1 and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells

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14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor

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7 January 2021

A fusicoccin binding protein belongs to the family of 14-3-3 brain protein homologs

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7 January 2021

Evolutionary implications of the family of 14-3-3 brain protein homologs in Arabidopsis thaliana

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14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae

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The genetics of cell cycle checkpoints

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The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family

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7 January 2021

Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase

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7 January 2021

14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner

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7 January 2021

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

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7 January 2021

Crystal structure of the zeta isoform of the 14-3-3 protein

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Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins

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7 January 2021

Bcr and Raf form a complex in vivo via 14-3-3 proteins

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7 January 2021

The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein

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7 January 2021

Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)

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7 January 2021

Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation).

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Endogenous fusicoccin-like ligand revealed in higher plants by radioreceptor and radioimmunoassays

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