Dikran Toroser

Works (6)

Updated: July 5th, 2023 16:04

2000 article

Carbon and nitrogen metabolism and reversible protein phosphorylation

Toroser, D., & Huber, S. C. (2000, January 1). Advances in Botanical Research.

By: D. Toroser n & S. Huber n

topics (OpenAlex): Metabolism, Diabetes, and Cancer; Plant nutrient uptake and metabolism; Protein Kinase Regulation and GTPase Signaling
TL;DR: This chapter focuses on the regulation of activity of several enzymes involved in carbon- and nitrogen-metabolisms that are phosphorylated by either calmodulin-like domain protein kinases (CDPKs) or sucrose nonfermenting-1 (SNF1)-related protein. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2000 article

Regulation of a Plant SNF1-Related Protein Kinase by Glucose-6-Phosphate

Toroser, D., Plaut, Z., & Huber, S. C. (2000, May 1). PLANT PHYSIOLOGY.

By: D. Toroser n, Z. Plaut n & S. Huber n

MeSH headings : Barium / metabolism; Glucose-6-Phosphate / pharmacology; Hydrogen-Ion Concentration; Magnesium / metabolism; Plants / enzymology; Protein Serine-Threonine Kinases / antagonists & inhibitors; Protein Serine-Threonine Kinases / isolation & purification; Protein Serine-Threonine Kinases / metabolism; Substrate Specificity
topics (OpenAlex): Plant Gene Expression Analysis; Plant tissue culture and regeneration
TL;DR: Glc-6-P inhibition of PK(III) activity potentially provides a mechanism for metabolic regulation of the reactions catalyzed by these important protein kinases. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1999 article

Site‐directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose‐phosphate synthase modulation

Toroser, D., McMichael, R., Krause, K. P., Kurreck, J., Sonnewald, U., Stitt, M., & Huber, S. C. (1999, February 1). The Plant Journal.

By: D. Toroser n, R. McMichael n, K. Krause, J. Kurreck *, U. Sonnewald *, M. Stitt *, S. Huber n

MeSH headings : Base Sequence; Circadian Rhythm; DNA Primers; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Glucosyltransferases / genetics; Glucosyltransferases / metabolism; Mutagenesis, Site-Directed; Plant Leaves / enzymology; Plants, Genetically Modified / genetics; Plants, Genetically Modified / physiology; Plants, Toxic; Serine / genetics; Serine / metabolism; Spinacia oleracea / enzymology; Spinacia oleracea / genetics; Tobacco / genetics; Tobacco / physiology
topics (OpenAlex): Plant tissue culture and regeneration; Legume Nitrogen Fixing Symbiosis; Plant-Microbe Interactions and Immunity
TL;DR: The results demonstrate the regulatory significance of Ser158 as the major site responsible for dark inactivation of spinach SPS in vivo, and indicate that the significance of phosphorylation is the introduction of a negative charge at the Ser158 position. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1998 article

3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Kinase and Sucrose–Phosphate Synthase Kinase Activities in Cauliflower Florets: Ca2+Dependence and Substrate Specificities

Toroser, D., & Huber, S. C. (1998, July 1). Archives of Biochemistry and Biophysics.

By: D. Toroser n & S. Huber n

author keywords: protein kinase; 3-hydroxy-3-methylglutaryl-CoA reductase; Brassica oleracea; sucrose-phosphate synthase; phosphorylation motif
MeSH headings : AMP-Activated Protein Kinases; Amino Acid Sequence; Binding Sites; Brassica; Calcium / physiology; Chromatography, Gel; Enzyme Activation; Glucosyltransferases / isolation & purification; Glucosyltransferases / metabolism; Hydroxymethylglutaryl CoA Reductases / metabolism; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes / isolation & purification; Multienzyme Complexes / metabolism; Nitrate Reductase; Nitrate Reductase (NADH); Nitrate Reductases / metabolism; Peptides / chemical synthesis; Peptides / metabolism; Phosphorylation; Plant Structures / enzymology; Protein Kinases / isolation & purification; Protein Kinases / metabolism; Protein Serine-Threonine Kinases; Spinacia oleracea; Substrate Specificity
topics (OpenAlex): Plant biochemistry and biosynthesis; Plant Gene Expression Analysis; Biochemical and biochemical processes
TL;DR: The novel aspects are that PKIII has not been detected in previous cauliflower studies, that SAMS* is a more specific peptide substrate to identify potential HMGR kinases, and that the major HM GR kinase in cauliflower is Ca2+ dependent. (via Semantic Scholar)
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Source: Web Of Science
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1998 article

Site‐specific regulatory interaction between spinach leaf sucrose‐phosphate synthase and 14‐3‐3 proteins

Toroser, D., Athwal, G. S., & Huber, S. C. (1998, September 11). FEBS Letters.

By: D. Toroser n, G. Athwal n & S. Huber n

author keywords: sucrose-phosphate synthase; 14-3-3 protein; Spinach; protein : protein interaction; surface plasmon resonance
MeSH headings : 14-3-3 Proteins; Amino Acid Sequence; Aminoimidazole Carboxamide / analogs & derivatives; Aminoimidazole Carboxamide / pharmacology; Binding Sites; Enzyme Activation / drug effects; Enzyme Inhibitors / metabolism; Enzyme Inhibitors / pharmacology; Glucosyltransferases / drug effects; Glucosyltransferases / metabolism; Magnesium / metabolism; Molecular Sequence Data; Peptide Fragments / metabolism; Phosphorylation; Plant Leaves / drug effects; Plant Leaves / enzymology; Proteins / metabolism; Proteins / pharmacology; Ribonucleotides / pharmacology; Serine / metabolism; Spinacia oleracea / drug effects; Spinacia oleracea / enzymology; Tyrosine 3-Monooxygenase
topics (OpenAlex): 14-3-3 protein interactions; Ubiquitin and proteasome pathways; Peptidase Inhibition and Analysis
TL;DR: An Mg2+‐dependent interaction between spinach leaf sucrose‐phosphate synthase (SPS) and endogenous 14‐3‐3 proteins is reported, as evidenced by co‐elution during gel filtration and co‐immunoprecipitation. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1997 article

Protein Phosphorylation as a Mechanism for Osmotic-Stress Activation of Sucrose-Phosphate Synthase in Spinach Leaves

Toroser, D., & Huber, S. C. (1997, July 1). PLANT PHYSIOLOGY.

By: D. Toroser n & S. Huber n

MeSH headings : Amino Acid Sequence; Calcium / pharmacology; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Conserved Sequence; Darkness; Enzyme Activation; Glucosyltransferases / biosynthesis; Glucosyltransferases / isolation & purification; Glucosyltransferases / metabolism; Light; Molecular Sequence Data; Osmolar Concentration; Peptide Fragments / chemistry; Peptide Fragments / metabolism; Phosphopeptides / chemistry; Phosphorylation; Phosphoserine; Plant Leaves; Protein Kinases / isolation & purification; Protein Kinases / metabolism; Sequence Alignment; Spinacia oleracea / enzymology; Spinacia oleracea / physiology
topics (OpenAlex): Plant nutrient uptake and metabolism; Plant Stress Responses and Tolerance; Photosynthetic Processes and Mechanisms
TL;DR: At least part of the osmotic stress activation of SPS in dark leaves results from phosphorylation of serine-424 catalyzed by a Ca2+-dependent, 150-kD protein kinase. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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