PROTEOMICS, ISSN 1615-9853, 01/2016, Volume 16, Issue 2, pp. 197 - 213
PTMs are defined as covalent additions to functional groups of amino acid residues in proteins like phosphorylation, glycosylation, S‐nitrosylation,...
Redox proteomics | Animal proteomics | Mass spectrometry | Redox modifications | OXIDATIVE STRESS | NONENZYMATICALLY GLYCATED PEPTIDES | CARBONYLATED PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CYSTEINE SULFENIC ACID | S-NITROSYLATED PROTEINS | LOSS-DRIVEN MS3 | TANDEM MASS-SPECTROMETRY | DIFFERENCE GEL-ELECTROPHORESIS | QUANTITATIVE-ANALYSIS | MITOCHONDRIAL PROTEINS | Protein Carbonylation | Tandem Mass Spectrometry | Animals | Oxidation-Reduction | Oxidative Stress | Glycation End Products, Advanced - isolation & purification | Humans | Proteomics | Chromatography, Liquid | Proteome - isolation & purification | Proteome - metabolism | Proteins | Methods | Enrichment | Oxidative stress | Residues | Phosphorylation | Identification methods | Homeostasis | Amino acids | SUMO protein | Biomolecules | Physiology | Oxidation | Acetylation | Sugars | Advanced glycosylation end products | Neurodegenerative diseases | Diabetes mellitus | Chemical reactions | Glycosylation | Chemical compounds | Diseases | Neurological diseases | Methylation | Functional groups | Cancer
Redox proteomics | Animal proteomics | Mass spectrometry | Redox modifications | OXIDATIVE STRESS | NONENZYMATICALLY GLYCATED PEPTIDES | CARBONYLATED PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CYSTEINE SULFENIC ACID | S-NITROSYLATED PROTEINS | LOSS-DRIVEN MS3 | TANDEM MASS-SPECTROMETRY | DIFFERENCE GEL-ELECTROPHORESIS | QUANTITATIVE-ANALYSIS | MITOCHONDRIAL PROTEINS | Protein Carbonylation | Tandem Mass Spectrometry | Animals | Oxidation-Reduction | Oxidative Stress | Glycation End Products, Advanced - isolation & purification | Humans | Proteomics | Chromatography, Liquid | Proteome - isolation & purification | Proteome - metabolism | Proteins | Methods | Enrichment | Oxidative stress | Residues | Phosphorylation | Identification methods | Homeostasis | Amino acids | SUMO protein | Biomolecules | Physiology | Oxidation | Acetylation | Sugars | Advanced glycosylation end products | Neurodegenerative diseases | Diabetes mellitus | Chemical reactions | Glycosylation | Chemical compounds | Diseases | Neurological diseases | Methylation | Functional groups | Cancer
Journal Article
Plant Physiology, ISSN 0032-0889, 7/2015, Volume 168, Issue 3, pp. 768 - 775
Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their...
Proteins | Nitration | Enzymes | Phosphorylation | Topical Review on Posttranslational Modifications in Chloroplasts | Chloroplasts | Plants | Acetylation | Physiological regulation | Post translational modification | Plant cells | N-TERMINAL ACETYLATION | PHOSPHOPROTEOME PROFILING REVEALS | ARABIDOPSIS-THALIANA | CHLAMYDOMONAS-REINHARDTII | S-NITROSYLATED PROTEINS | LARGE SUBUNIT | LYSINE ACETYLATION | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE | TYROSINE NITRATION | SECRETORY PATHWAY | PLANT SCIENCES | Models, Biological | Chloroplast Proteins - metabolism | Protein Processing, Post-Translational | Post-translational modification | Genetic aspects | Gene expression | Identification and classification
Proteins | Nitration | Enzymes | Phosphorylation | Topical Review on Posttranslational Modifications in Chloroplasts | Chloroplasts | Plants | Acetylation | Physiological regulation | Post translational modification | Plant cells | N-TERMINAL ACETYLATION | PHOSPHOPROTEOME PROFILING REVEALS | ARABIDOPSIS-THALIANA | CHLAMYDOMONAS-REINHARDTII | S-NITROSYLATED PROTEINS | LARGE SUBUNIT | LYSINE ACETYLATION | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE | TYROSINE NITRATION | SECRETORY PATHWAY | PLANT SCIENCES | Models, Biological | Chloroplast Proteins - metabolism | Protein Processing, Post-Translational | Post-translational modification | Genetic aspects | Gene expression | Identification and classification
Journal Article
Plant Biology, ISSN 1435-8603, 07/2013, Volume 15, Issue 4, pp. 694 - 706
Photorespiration allows the recycling of carbon atoms of 2-phosphoglycolate produced by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) oxygenase...
Phosphoproteome | Protein phosphorylation | Arabidopsis | Photorespiration | KINASE | protein phosphorylation | S-NITROSYLATED PROTEINS | MEDIATED SIGNAL-TRANSDUCTION | IDENTIFICATION | phosphoproteome | PLANT SCIENCES | photorespiration | PHOSPHOPROTEOME PROFILING REVEALS | GLYCOLATE OXIDASE | LIPOAMIDE DEHYDROGENASE | GLYCINE DECARBOXYLASE | GLUTAMINE-SYNTHETASE | Carbon - metabolism | Phosphorylation | Arabidopsis - enzymology | Models, Molecular | Proteome | Phosphoproteins - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Arabidopsis - radiation effects | Cell Respiration | Light | Proteomics | Protein Processing, Post-Translational | Photosynthesis | Proteins | Arabidopsis thaliana | Physiological aspects | Index Medicus
Phosphoproteome | Protein phosphorylation | Arabidopsis | Photorespiration | KINASE | protein phosphorylation | S-NITROSYLATED PROTEINS | MEDIATED SIGNAL-TRANSDUCTION | IDENTIFICATION | phosphoproteome | PLANT SCIENCES | photorespiration | PHOSPHOPROTEOME PROFILING REVEALS | GLYCOLATE OXIDASE | LIPOAMIDE DEHYDROGENASE | GLYCINE DECARBOXYLASE | GLUTAMINE-SYNTHETASE | Carbon - metabolism | Phosphorylation | Arabidopsis - enzymology | Models, Molecular | Proteome | Phosphoproteins - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Arabidopsis - radiation effects | Cell Respiration | Light | Proteomics | Protein Processing, Post-Translational | Photosynthesis | Proteins | Arabidopsis thaliana | Physiological aspects | Index Medicus
Journal Article
Antioxidants & Redox Signaling, ISSN 1523-0864, 03/2017, Volume 26, Issue 7, pp. 329 - 344
Significance: Reactive oxygen species are produced during normal metabolism in cells, and their excesses have been implicated in protein damage and toxicity,...
Forum Review Articles | Redox proteomics | Thiol switch | Cys oxidation | H2O2 | ICAT | DISULFIDE BOND FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | S-NITROSYLATED PROTEINS | redox proteomics | MASS-SPECTROMETRY | REACTIVE OXYGEN | TRANSCRIPTION FACTOR PAP1 | thiol switch | IN-VIVO | ENDOCRINOLOGY & METABOLISM | HYDROGEN-PEROXIDE | SULFENIC ACID FORMATION | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Signal Transduction | Humans | Pancreatitis-Associated Proteins | Hydrogen Peroxide - metabolism | Sulfhydryl Compounds - metabolism | Animals | Mass Spectrometry | Cysteine - metabolism | Protein Processing, Post-Translational | Oxidative Stress - drug effects | Proteomics - methods | Proteome - metabolism | Usage | Reactive oxygen species | Proteomics | Electrophoresis | Peroxides | Research | Health aspects | Hydrogen peroxide | Yeast | Thiols | Toxicity | Mass spectroscopy | Metabolism | Proteins | Antioxidants | Signaling | Cascades | Oxidation | Sensors | Mass spectrometry | Hydrogen ion concentration | Index Medicus | Tiols | Oxidació | Proteòmica | Proteïnes
Forum Review Articles | Redox proteomics | Thiol switch | Cys oxidation | H2O2 | ICAT | DISULFIDE BOND FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | S-NITROSYLATED PROTEINS | redox proteomics | MASS-SPECTROMETRY | REACTIVE OXYGEN | TRANSCRIPTION FACTOR PAP1 | thiol switch | IN-VIVO | ENDOCRINOLOGY & METABOLISM | HYDROGEN-PEROXIDE | SULFENIC ACID FORMATION | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Signal Transduction | Humans | Pancreatitis-Associated Proteins | Hydrogen Peroxide - metabolism | Sulfhydryl Compounds - metabolism | Animals | Mass Spectrometry | Cysteine - metabolism | Protein Processing, Post-Translational | Oxidative Stress - drug effects | Proteomics - methods | Proteome - metabolism | Usage | Reactive oxygen species | Proteomics | Electrophoresis | Peroxides | Research | Health aspects | Hydrogen peroxide | Yeast | Thiols | Toxicity | Mass spectroscopy | Metabolism | Proteins | Antioxidants | Signaling | Cascades | Oxidation | Sensors | Mass spectrometry | Hydrogen ion concentration | Index Medicus | Tiols | Oxidació | Proteòmica | Proteïnes
Journal Article
Journal of Experimental Botany, ISSN 0022-0957, 1/2011, Volume 62, Issue 10, pp. 3501 - 3517
Nitration of tyrosine (Y) residues of proteins is a low abundant post-translational modification that modulates protein function or fate in animal systems....
Nitration | Dehydrogenases | Chloroplasts | Gels | Proteomics | Antibodies | Oxides | Plants | Shotguns | RESEARCH PAPER | Post translational modification | nitroY | nitric oxide | Arabidopsis | AminoY | nitrotyrosine | protein nitration | post-translational modification | PLANT-PATHOGEN INTERACTIONS | PEROXYNITRITE | METHIONINE SYNTHASE | S-NITROSYLATED PROTEINS | IDENTIFICATION | MASS-SPECTROMETRY | PLANT SCIENCES | REDOX REGULATION | NITRIC-OXIDE | PROTEOMIC ANALYSIS | Arabidopsis Proteins - genetics | Immunoprecipitation | Electrophoresis, Gel, Two-Dimensional | Blotting, Western | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Nitrates - metabolism | Tandem Mass Spectrometry | Tyrosine - metabolism | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - metabolism | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - genetics | Chromatography, Liquid | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Research Papers
Nitration | Dehydrogenases | Chloroplasts | Gels | Proteomics | Antibodies | Oxides | Plants | Shotguns | RESEARCH PAPER | Post translational modification | nitroY | nitric oxide | Arabidopsis | AminoY | nitrotyrosine | protein nitration | post-translational modification | PLANT-PATHOGEN INTERACTIONS | PEROXYNITRITE | METHIONINE SYNTHASE | S-NITROSYLATED PROTEINS | IDENTIFICATION | MASS-SPECTROMETRY | PLANT SCIENCES | REDOX REGULATION | NITRIC-OXIDE | PROTEOMIC ANALYSIS | Arabidopsis Proteins - genetics | Immunoprecipitation | Electrophoresis, Gel, Two-Dimensional | Blotting, Western | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Nitrates - metabolism | Tandem Mass Spectrometry | Tyrosine - metabolism | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - metabolism | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - genetics | Chromatography, Liquid | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Research Papers
Journal Article
Redox Biology, ISSN 2213-2317, 2014, Volume 3, Issue C, pp. 109 - 123
Mitochondria are critically important in providing cellular energy ATP as well as their involvement in anti-oxidant defense, fat oxidation, intermediary...
Redox | Nitroxidative stress | Post-translational modifications | Mitochondrial dysfunction | Mitochondrial proteins | Tissue injury | OXIDATIVE STRESS | LIPID-PEROXIDATION | ALDEHYDE DEHYDROGENASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NADP(+)-DEPENDENT ISOCITRATE DEHYDROGENASE | INDUCED LIVER-INJURY | TERMINAL KINASE | CELL-DEATH | CYTOCHROME-C-OXIDASE | REACTIVE OXYGEN | NITRIC-OXIDE | Ethanol - metabolism | Humans | Translational Medical Research | Liver Diseases - pathology | Diet, High-Fat - adverse effects | Mitochondria - metabolism | Antioxidants - pharmacology | Mitochondria - drug effects | Antioxidants - therapeutic use | Animals | Protein Processing, Post-Translational - drug effects | Ethanol - adverse effects | Liver Diseases - etiology | Oxidation-Reduction - drug effects | Liver Diseases - drug therapy | Oxidative Stress - drug effects | Liver Diseases - metabolism
Redox | Nitroxidative stress | Post-translational modifications | Mitochondrial dysfunction | Mitochondrial proteins | Tissue injury | OXIDATIVE STRESS | LIPID-PEROXIDATION | ALDEHYDE DEHYDROGENASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NADP(+)-DEPENDENT ISOCITRATE DEHYDROGENASE | INDUCED LIVER-INJURY | TERMINAL KINASE | CELL-DEATH | CYTOCHROME-C-OXIDASE | REACTIVE OXYGEN | NITRIC-OXIDE | Ethanol - metabolism | Humans | Translational Medical Research | Liver Diseases - pathology | Diet, High-Fat - adverse effects | Mitochondria - metabolism | Antioxidants - pharmacology | Mitochondria - drug effects | Antioxidants - therapeutic use | Animals | Protein Processing, Post-Translational - drug effects | Ethanol - adverse effects | Liver Diseases - etiology | Oxidation-Reduction - drug effects | Liver Diseases - drug therapy | Oxidative Stress - drug effects | Liver Diseases - metabolism
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 01/2012, Volume 11, Issue 1, pp. 412 - 424
Regulation of protein function through oxidative modification has emerged as an important molecular mechanism modulating various biological processes. Here, we...
AtCIAPIN1 | Redox proteomics | Arabidopsis | hydrogen peroxide | salicylic acid | flg22 | oxidative stress | BIOCHEMICAL RESEARCH METHODS | PLANT-DISEASE RESISTANCE | S-NITROSYLATED PROTEINS | redox proteomics | CELL-DEATH | YEAST SACCHAROMYCES-CEREVISIAE | TYROSINE-PHOSPHATASE 1B | FUNDAMENTAL PROCESSES | NITRIC-OXIDE | HYDROGEN-PEROXIDE | CYSTEINE RESIDUES | Arabidopsis - physiology | Oxidants - pharmacology | Oxidative Stress | Proteome - chemistry | Arabidopsis Proteins - metabolism | Biotin - chemistry | Salicylic Acid - pharmacology | Sulfhydryl Compounds - metabolism | Peptide Mapping | Sulfhydryl Compounds - chemistry | Plant Leaves - drug effects | Fluoresceins - chemistry | Arabidopsis - drug effects | Oxidation-Reduction | Ethylenediamines - chemistry | Hydrogen Peroxide - pharmacology | Apoptosis Regulatory Proteins - metabolism | Arabidopsis - metabolism | Peptide Fragments - chemistry | Arabidopsis Proteins - chemistry | Plant Leaves - metabolism | Staining and Labeling | Proteomics | Proteome - metabolism | Plant Leaves - physiology | Biotin - analogs & derivatives
AtCIAPIN1 | Redox proteomics | Arabidopsis | hydrogen peroxide | salicylic acid | flg22 | oxidative stress | BIOCHEMICAL RESEARCH METHODS | PLANT-DISEASE RESISTANCE | S-NITROSYLATED PROTEINS | redox proteomics | CELL-DEATH | YEAST SACCHAROMYCES-CEREVISIAE | TYROSINE-PHOSPHATASE 1B | FUNDAMENTAL PROCESSES | NITRIC-OXIDE | HYDROGEN-PEROXIDE | CYSTEINE RESIDUES | Arabidopsis - physiology | Oxidants - pharmacology | Oxidative Stress | Proteome - chemistry | Arabidopsis Proteins - metabolism | Biotin - chemistry | Salicylic Acid - pharmacology | Sulfhydryl Compounds - metabolism | Peptide Mapping | Sulfhydryl Compounds - chemistry | Plant Leaves - drug effects | Fluoresceins - chemistry | Arabidopsis - drug effects | Oxidation-Reduction | Ethylenediamines - chemistry | Hydrogen Peroxide - pharmacology | Apoptosis Regulatory Proteins - metabolism | Arabidopsis - metabolism | Peptide Fragments - chemistry | Arabidopsis Proteins - chemistry | Plant Leaves - metabolism | Staining and Labeling | Proteomics | Proteome - metabolism | Plant Leaves - physiology | Biotin - analogs & derivatives
Journal Article
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Full Text
A Novel Approach to Identify Proteins Modified by Nitric Oxide: the HIS-TAG Switch Method
Journal of Proteome Research, ISSN 1535-3893, 08/2007, Volume 6, Issue 8, pp. 3224 - 3231
S-nitrosylation is emerging as an important signaling mechanism that regulates a broad range of cellular functions. The recognition of Cysteine residues that...
Post-translational modifications | Mass spectrometry | Nitric oxide | Proteomics | S-nitrosylation | nitric oxide | proteomics | BIOCHEMICAL RESEARCH METHODS | GUANINE-NUCLEOTIDE EXCHANGE | S-NITROSYLATED PROTEINS | IDENTIFICATION | MASS-SPECTROMETRY | STATISTICAL-MODEL | SIGNAL-TRANSDUCTION | SMOOTH-MUSCLE | NITROSOTHIOLS | GLUTATHIONE | ENDOTHELIAL-CELLS | mass spectrometry | post-translational modifications | Amino Acid Sequence | Nitric Oxide - chemistry | Ovalbumin - analysis | Cerebellum - metabolism | Nerve Tissue Proteins - analysis | Molecular Sequence Data | Rats | Male | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Rats, Sprague-Dawley | Nerve Tissue Proteins - chemistry | Nitroso Compounds - chemistry | Animals | S-Nitrosoglutathione - chemistry | Female | Nitric Oxide - metabolism | Ovalbumin - chemistry
Post-translational modifications | Mass spectrometry | Nitric oxide | Proteomics | S-nitrosylation | nitric oxide | proteomics | BIOCHEMICAL RESEARCH METHODS | GUANINE-NUCLEOTIDE EXCHANGE | S-NITROSYLATED PROTEINS | IDENTIFICATION | MASS-SPECTROMETRY | STATISTICAL-MODEL | SIGNAL-TRANSDUCTION | SMOOTH-MUSCLE | NITROSOTHIOLS | GLUTATHIONE | ENDOTHELIAL-CELLS | mass spectrometry | post-translational modifications | Amino Acid Sequence | Nitric Oxide - chemistry | Ovalbumin - analysis | Cerebellum - metabolism | Nerve Tissue Proteins - analysis | Molecular Sequence Data | Rats | Male | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Rats, Sprague-Dawley | Nerve Tissue Proteins - chemistry | Nitroso Compounds - chemistry | Animals | S-Nitrosoglutathione - chemistry | Female | Nitric Oxide - metabolism | Ovalbumin - chemistry
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1747, pp. 103 - 111
Protein S-nitrosylation, the NO-dependent regulatory mechanism, is a posttranslational modification of reactive cysteine thiols to form S-nitrosothiols. The...
Surface plasmon resonance spectroscopy | S-Nitrosylated protein | Nitric oxide | Tandem Mass Spectrometry | Reactive Oxygen Species - metabolism | Peptides - chemistry | Humans | Chromatography, Liquid | Search Engine | Protein Processing, Post-Translational | Surface Plasmon Resonance - methods | Nitric Oxide - metabolism | Peptides - analysis
Surface plasmon resonance spectroscopy | S-Nitrosylated protein | Nitric oxide | Tandem Mass Spectrometry | Reactive Oxygen Species - metabolism | Peptides - chemistry | Humans | Chromatography, Liquid | Search Engine | Protein Processing, Post-Translational | Surface Plasmon Resonance - methods | Nitric Oxide - metabolism | Peptides - analysis
Journal Article
Journal of Molecular Recognition, ISSN 0952-3499, 01/2019, Volume 32, Issue 1, pp. e2754 - n/a
Plants, as sessile organisms, have acquired through evolution sophisticated regulatory signal pathways to overcome external variable factors during each stage...
proteomics | molecular dynamics simulation | reactive oxygen species | post‐translational modifications | S‐nitrosylation | reactive nitrogen species | cell wall | S-nitrosylation | post-translational modifications | ARABIDOPSIS-THALIANA | ABIOTIC STRESS | NITROSATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | S-NITROSYLATED PROTEINS | HYDROGEN-SULFIDE | BIOPHYSICS | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | NITRIC-OXIDE | PECTIN METHYLESTERASE | CELL-DIFFERENTIATION | TYROSINE NITRATION | Proteins | Tyrosine | Post-translational modification | Nitration | Cysteine | Plant physiology | Hydrogen | Analysis | Molecular dynamics | Plants | Cell differentiation | Hydrogen bonding | Regulators | Reactive oxygen species | Cell walls | Differentiation (biology) | Reactive nitrogen species | Mass spectroscopy | Pectin | Plant cells | Xyloglucan | Pathways | Hemostasis | Life cycle engineering | Extracellular matrix | Metabolic pathways | Hemostatics | Intracellular | Mass spectrometry | Pectinesterase | Life cycles
proteomics | molecular dynamics simulation | reactive oxygen species | post‐translational modifications | S‐nitrosylation | reactive nitrogen species | cell wall | S-nitrosylation | post-translational modifications | ARABIDOPSIS-THALIANA | ABIOTIC STRESS | NITROSATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | S-NITROSYLATED PROTEINS | HYDROGEN-SULFIDE | BIOPHYSICS | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | NITRIC-OXIDE | PECTIN METHYLESTERASE | CELL-DIFFERENTIATION | TYROSINE NITRATION | Proteins | Tyrosine | Post-translational modification | Nitration | Cysteine | Plant physiology | Hydrogen | Analysis | Molecular dynamics | Plants | Cell differentiation | Hydrogen bonding | Regulators | Reactive oxygen species | Cell walls | Differentiation (biology) | Reactive nitrogen species | Mass spectroscopy | Pectin | Plant cells | Xyloglucan | Pathways | Hemostasis | Life cycle engineering | Extracellular matrix | Metabolic pathways | Hemostatics | Intracellular | Mass spectrometry | Pectinesterase | Life cycles
Journal Article
Physiologia Plantarum, ISSN 0031-9317, 04/2010, Volume 138, Issue 4, pp. 372 - 383
Over the past 20 years, nitric oxide (NO) research has generated a lot of interest in various aspects of plant biology. It is now clear that NO plays a role in...
IN-VITRO | DEFENSE RESPONSES | NICOTIANA-BENTHAMIANA | VERTICILLIUM-DAHLIAE TOXINS | INDUCED STOMATAL CLOSURE | NITRIC-OXIDE SYNTHASE | ARABIDOPSIS-THALIANA PLANTS | S-NITROSYLATED PROTEINS | NITRATE REDUCTASE | CELL-DEATH | PLANT SCIENCES<
IN-VITRO | DEFENSE RESPONSES | NICOTIANA-BENTHAMIANA | VERTICILLIUM-DAHLIAE TOXINS | INDUCED STOMATAL CLOSURE | NITRIC-OXIDE SYNTHASE | ARABIDOPSIS-THALIANA PLANTS | S-NITROSYLATED PROTEINS | NITRATE REDUCTASE | CELL-DEATH | PLANT SCIENCES<