Gurdeep S. Athwal

Works (8)

Updated: February 10th, 2025 16:10

2009 article

Overexpression of a directed mutant of 14-3-3ω in Arabidopsis leaves affects phosphorylation and protein content of nitrate reductaseThis paper is one of a selection published in a Special Issue comprising papers presented at the 50th Annual Meeting of the Canadian Society of Plant Physiologists (CSPP) held at the University of Ottawa, Ontario, in June 2008.

Oh, M.-H., Huber, J. L., Shen, W., Athwal, G. S., Wu, X., & Huber, S. C. (2009, July 1). Botany.

By: M. Oh *, J. Huber*, W. Shen*, G. Athwal*, X. Wu * & S. Huber *

author keywords: Arabidopsis thaliana; 14-3-3 protein; beta-glucosidase; glutathione S-transferase; two-dimensional difference gel electrophoresis; site-directed mutagenesis
topics (OpenAlex): 14-3-3 protein interactions; Photosynthetic Processes and Mechanisms; Ubiquitin and proteasome pathways
TL;DR: This work generated transgenic Arabidopsis plants constitutively overexpressing a directed mutant of 14-3-3 isoform ω that inhibits phosphorylated nitrate reductase (pNR) in a largely divalent-cation-independent manner in vitro. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2002 article

Divalent cations and polyamines bind to loop 8 of 14‐3‐3 proteins, modulating their interaction with phosphorylated nitrate reductase

Athwal, G. S., & Huber, S. C. (2002, January 1). The Plant Journal.

By: G. Athwal* & S. Huber n

author keywords: 14-3-3 proteins; nitrate reductase; polyamines; cation-binding site; site-directed mutagenesis; truncated proteins
MeSH headings : 14-3-3 Proteins; Arabidopsis Proteins; Binding Sites / genetics; Calcium-Binding Proteins / metabolism; Cations, Divalent / metabolism; Cations, Divalent / pharmacology; Magnesium / metabolism; Magnesium / pharmacology; Mutagenesis, Site-Directed; Mutation; Nitrate Reductase; Nitrate Reductases / antagonists & inhibitors; Nitrate Reductases / metabolism; Phosphorylation / drug effects; Plant Proteins / metabolism; Polyamines / metabolism; Polyamines / pharmacology; Protein Binding; Protein Conformation; Spermidine / pharmacology; Spermine / pharmacology; Tyrosine 3-Monooxygenase / chemistry; Tyrosine 3-Monooxygenase / genetics; Tyrosine 3-Monooxygenase / metabolism
topics (OpenAlex): 14-3-3 protein interactions; Fungal and yeast genetics research; Microbial metabolism and enzyme function
TL;DR: It is reported that micromolar concentrations of the polyamines, spermidine(4+) and spermine(3+), can substitute for divalent cations in modulating 14-3-3 action and proposed that binding of polyamines to 14- 3-3s could be involved in their regulation of plant growth and development. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2000 article

Modulation of 14-3-3 Protein Interactions with Target Polypeptides by Physical and Metabolic Effectors

Athwal, G. S., Lombardo, C. R., Huber, J. L., Masters, S. C., Fu, H., & Huber, S. C. (2000, April 1). Plant and Cell Physiology.

By: G. Athwal n, C. Lombardo*, J. Huber*, S. Masters*, H. Fu * & S. Huber*

MeSH headings : 14-3-3 Proteins; Adenosine Monophosphate / pharmacology; Arabidopsis; Biosensing Techniques; Cations, Divalent / pharmacology; Fungal Proteins; Gene Expression Regulation, Enzymologic; Ligands; Nitrate Reductase; Nitrate Reductases / metabolism; Peptide Fragments / metabolism; Phosphopeptides / metabolism; Plant Proteins; Protein Binding / drug effects; Proteins / genetics; Proteins / metabolism; Protons; Recombinant Proteins / metabolism; Saccharomyces cerevisiae; Spinacia oleracea; Tyrosine 3-Monooxygenase
topics (OpenAlex): 14-3-3 protein interactions; Ubiquitin and proteasome pathways; Fungal and yeast genetics research
TL;DR: The proteins commonly referred to as 14-3-3s have recently come to prominence in the study of protein:protein interactions, having been shown to act as allosteric or steric regulators and possibly scaffolds, and to interact directly with cations, which bind and affect surface hydrophobicity. (via Semantic Scholar)
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Source: NC State University Libraries
Added: August 6, 2018

1998 article

Biological Significance of Divalent Metal Ion Binding to 14-3-3 Proteins In Relationship to Nitrate Reductase Inactivation

Athwal, G. S., Huber, J. L., & Huber, S. C. (1998, October 1). Plant and Cell Physiology.

By: G. Athwal n, J. Huber n & S. Huber n

author keywords: 14-3-3 protein; conformational change; fluorescence; metal binding site; nitrate reductase; protonation
MeSH headings : 14-3-3 Proteins; Binding Sites; Cations, Divalent; Metals / metabolism; Nitrate Reductase (NADH); Nitrate Reductases / antagonists & inhibitors; Nitrate Reductases / metabolism; Phosphopeptides / chemical synthesis; Phosphopeptides / metabolism; Protein Conformation; Proteins / chemistry; Proteins / metabolism; Protons; Tyrosine 3-Monooxygenase
topics (OpenAlex): 14-3-3 protein interactions; Microbial metabolism and enzyme function; Fungal and yeast genetics research
TL;DR: It is proposed that protonation of amino acid residues brings about a similar effect to metal ion binding, and a possible regulatory mechanism, where the 14-3-3 protein has to be "primed" prior to binding a target protein, is discussed. (via Semantic Scholar)
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6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Nitrate effect on carbon and nitrogen assimilating enzymes of maize hybrids representing seven eras of breeding

Maydica, 43(2), 83–94.

By: A. Purcino, C. Arellano, G. Athwal & S. Huber

Source: NC State University Libraries
Added: August 6, 2018

1998 article

Phosphorylated Nitrate Reductase and 14-3-3 Proteins

Athwal, G. S., Huber, J. L., & Huber, S. C. (1998, November 1). PLANT PHYSIOLOGY.

By: G. Athwal*, J. Huber* & S. Huber n

MeSH headings : 14-3-3 Proteins; Adenosine Monophosphate / metabolism; Amino Acid Sequence; Binding Sites; Molecular Sequence Data; Nitrate Reductase; Nitrate Reductases / metabolism; Peptides / chemistry; Phosphorylation; Protein Binding; Proteins / metabolism; Sequence Homology, Amino Acid; Serine / metabolism; Spinacia oleracea / enzymology; Spinacia oleracea / metabolism; Tyrosine 3-Monooxygenase
topics (OpenAlex): 14-3-3 protein interactions; Ubiquitin and proteasome pathways; Lipid metabolism and biosynthesis
TL;DR: It is shown that serine and threonine residues at the +6 to +8 positions, relative to the known regulatory binding site involving serine-543, are important in the interaction with GF14omega, a recombinant plant 14-3-3. (via Semantic Scholar)
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2. Zero Hunger (Web of Science)
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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

Regulation of glutamate dehydrogenase activity by manipulation of nucleotide supply in Daucus carota suspension cultures

Athwal, G. S., Pearson, J., & Laurie, S. (1997, November 1). Physiologia Plantarum.

By: G. Athwal*, J. Pearson & S. Laurie

author keywords: apiaceae; Daucus carota; carrot suspension culture; glutamate dehydrogenase; nucleotides; respiration
topics (OpenAlex): GABA and Rice Research
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
2. Zero Hunger (Web of Science)
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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