Gurdeep S. Athwal

Works (8)

Updated: August 16th, 2024 13:38

2009 article

Overexpression of a directed mutant of 14-3-3 omega in Arabidopsis leaves affects phosphorylation and protein content of nitrate reductase

Oh, M.-H., Huber, J. L., Shen, W., Athwal, G. S., Wu, X., & Huber, S. C. (2009, July). BOTANY, Vol. 87, pp. 691–701.

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
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)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2002 journal article

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

PLANT JOURNAL, 29(2), 119–129.

By: G. Athwal n & 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
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)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2000 journal article

Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors

Plant and Cell Physiology, 41(4), 523–533.

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
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)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: NC State University Libraries
Added: August 6, 2018

1998 journal article

Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation

PLANT AND CELL PHYSIOLOGY, 39(10), 1065–1072.

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
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)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
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 journal article

Phosphorylated nitrate reductase and 14-3-3 proteins - Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins

PLANT PHYSIOLOGY, 118(3), 1041–1048.

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
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)
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

1998 journal article

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

FEBS LETTERS, 435(1), 110–114.

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
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)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1997 journal article

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

PHYSIOLOGIA PLANTARUM, 101(3), 503–509.

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

author keywords: apiaceae; Daucus carota; carrot suspension culture; glutamate dehydrogenase; nucleotides; respiration
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

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2025) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.