• AQP9
• Human placenta
• Nitrative stress
• Trophoblast

• Nitric oxide synthase
• Nitrosylation
• Post-translational modifications
• Reactive oxygen species
• Signalling

• Nitric Oxide/metabolism
• Plants/metabolism
• Stress, Physiological/physiology
• Signal Transduction
• Plant Physiological Phenomena

• Attention mechanisms
• Deep learning
• Dense convolutional networks
• S-nitrosoylation

• COVID-19
• NO-sartans
• Nitric oxide
• RNA.
• SARS-CoV-2
• cardiovascular system

• Antiviral Agents/pharmacology
• Antiviral Agents/chemistry
• Antiviral Agents/therapeutic use
• SARS-CoV-2/drug effects
• Humans
• Molecular Docking Simulation
• Computer Simulation
• Angiotensin-Converting Enzyme 2/metabolism
• COVID-19 Drug Treatment
• Endoribonucleases/metabolism
• Endoribonucleases/antagonists & inhibitors
• Nitric Oxide/metabolism
• Viral Nonstructural Proteins/antagonists & inhibitors
• Viral Nonstructural Proteins/metabolism
• Molecular Dynamics Simulation

• 3-nitrotyrosine
• cancer biology
• cell signaling
• posttranslational modifications
• tyrosine nitration

• Animals
• Humans
• Neoplasms
• Phosphorylation
• Proteins/metabolism
• Signal Transduction
• Tyrosine/metabolism

• Brain
• COVID-19
• lungs
• nitric oxide
• peroxynitrite
• vascular endothelium

• Diabetes
• Diabetic cardiomyopathy
• Diabetic heart
• Mitochondria
• Oxidative stress
• Reactive oxygen species

• Antioxidants
• Diabetes Mellitus
• Diabetic Cardiomyopathies/drug therapy
• Diabetic Cardiomyopathies/genetics
• Humans
• NADPH Oxidases/metabolism
• Oxidative Stress
• Reactive Oxygen Species

• R01 HL118067 NHLBI NIH HHS
• R61 HL141783 NHLBI NIH HHS
• U54 HL112311 NHLBI NIH HHS
• R24 DK092784 NIDDK NIH HHS
• R01 HL073167 NHLBI NIH HHS
• R03 AG042860 NIA NIH HHS
• U01 HL087947 NHLBI NIH HHS
• U01 HL070525 NHLBI NIH HHS

An early event in atherogenesis is the recruitment and infiltration of circulating monocytes and macrophage activation in the subendothelial space. Atherosclerosis subsequently progresses as a unresolved inflammatory disease, particularly in hypercholesterolemic conditions. Although physical exercise training has been a widely accepted strategy to inhibit atherosclerosis, its impact on arterial wall inflammation and macrophage phenotype and function has not yet been directly evaluated. Thus, the aim of this study was to investigate the effects of aerobic exercise training on the inflammatory state of atherosclerotic lesions with a focus on macrophages. Hypercholesterolemic LDL-receptor-deficient male mice were subjected to treadmill training for 8 weeks and fed a high-fat diet. Analyses included plasma lipoprotein and cytokine levels; aortic root staining for lipids (oil red O); macrophages (CD68, MCP1 and IL1β); oxidative (nitrotyrosine and, DHE) and endoplasmic reticulum (GADD) stress markers. Primary bone marrow-derived macrophages (BMDM) were assayed for migration activity, motility phenotype (Rac1 and F-actin) and inflammation-related gene expression. Plasma levels of HDL cholesterol were increased, while levels of proinflammatory cytokines (TNFa, IL1b, and IL6) were markedly reduced in the exercised mice. The exercised mice developed lower levels of lipid content and inflammation in atherosclerotic plaques. Additionally, lesions in the exercised mice had lower levels of oxidative and ER stress markers. BMDM isolated from the exercised mice showed a marked reduction in proinflammatory cytokine gene expression and migratory activity and a disrupted motility phenotype. More importantly, bone marrow from exercised mice transplanted into sedentary mice led to reduced atherosclerosis in the recipient sedentary mice, thus suggesting that epigenetic mechanisms are associated with exercise. Collectively, the presented data indicate that exercise training prevents atherosclerosis by inhibiting bone marrow-derived macrophage recruitment and activation.

• atherosclerosis
• bone-marrow transplantation
• exercise
• inflammation
• macrophages

Environmental pollutants like fine particulate matter can cause adverse health effects through oxidative stress and inflammation. Reactive oxygen and nitrogen species (ROS/RNS) such as peroxynitrite can chemically modify proteins, but the effects of such modifications on the immune system and human health are not well understood. In the course of inflammatory processes, the Toll-like receptor 4 (TLR4) can sense damage-associated molecular patterns (DAMPs). Here, we investigate how the TLR4 response and pro-inflammatory potential of the proteinous DAMPs α-Synuclein (α-Syn), heat shock protein 60 (HSP60), and high-mobility-group box 1 protein (HMGB1), which are relevant in neurodegenerative and cardiovascular diseases, changes upon chemical modification with peroxynitrite.

For the peroxynitrite-modified proteins, we found a strongly enhanced activation of TLR4 and the pro-inflammatory transcription factor NF-κB in stable reporter cell lines as well as increased mRNA expression and secretion of the pro-inflammatory cytokines TNF-α, IL-1β, and IL-8 in human monocytes (THP-1). This enhanced activation of innate immunity via TLR4 is mediated by covalent chemical modifications of the studied DAMPs.

Our results show that proteinous DAMPs modified by peroxynitrite more potently amplify inflammation via TLR4 activation than the native DAMPs, and provide first evidence that such modifications can directly enhance innate immune responses via a defined receptor. These findings suggest that environmental pollutants and related ROS/RNS may play a role in promoting acute and chronic inflammatory disorders by structurally modifying the body's own DAMPs. This may have important consequences for chronic neurodegenerative, cardiovascular or gastrointestinal diseases that are prevalent in modern societies, and calls for action, to improve air quality and climate in the Anthropocene.

•

Pollutants and oxidative stress can cause protein nitration and oligomerization.

• HMGB1
• HSP60
• Peroxynitrite
• Protein modification
• TLR4
• α-Synuclein

This study investigated whether levosimendan, an inotropic calcium sensitizer, when combined with moderate therapeutic hypothermia, may exert synergistic benefits on post–cardiac arrest myocardial dysfunction and improve outcomes.

After 9.5‐minute asphyxia‐induced cardiac arrest and resuscitation, 48 rats were randomized equally into 4 groups following return of spontaneous circulation (ROSC), including normothermia, hypothermia, normothermia–levosimendan, and hypothermia–levosimendan groups. For the normothermia group, the target temperature was 37°C while for the hypothermia group, the target temperature was 32°C, both of which were to be maintained for 4 hours after ROSC. Levosimendan was administered after ROSC with a loading dose of 10 μg/kg and then infused at 0.1 μg/kg per min for 4 hours. In the hypothermia–levosimendan group, left ventricular systolic function and cardiac output increased significantly, whereas the heart rate and systemic vascular resistance decreased significantly compared with the normothermia group. Also, the concentrations of interleukin 1β at 4 hours post‐ROSC and the production of NO between 1 hour and 4 hours post‐ROSC were reduced significantly in the hypothermia–levosimendan group compared with the normothermia group. The 72‐hour post‐ROSC survival and neurological recovery were also significantly better in the hypothermia–levosimendan group compared with the normothermia group (survival, 100% versus 50%, χ² test, P=0.006).

Compared with normothermia, only combined moderate therapeutic hypothermia and levosimendan treatment could consistently improve post–cardiac arrest myocardial dysfunction and decrease the release of pro‐inflammatory molecules, thereby improving survival and neurological outcomes. These findings suggest synergistic benefits between moderate therapeutic hypothermia and levosimendan.

• brain injury
• cardiac arrest
• cardiac dysfunction
• hypothermia
• inflammation
• levosimendan
• survival

• HPLC with electrochemical detection
• mitochondrial superoxide
• oxidative stress
• peroxynitrite
• protein-bound 3-nitrotyrosine

• Novel and neglected cardiovascular risk factors: molecular mechanisms and therapeutics Boehringer Ingelheim Stiftung
• Partner Site Rhine-Main, Mainz Deutsches Zentrum für Herz-Kreislaufforschung

• Amino Acid Sequence
• Animals
• Carbohydrate Sequence
• Humans
• Lipids/analysis
• Lipids/radiation effects
• Mass Spectrometry/methods
• Nucleic Acids/analysis
• Nucleic Acids/radiation effects
• Oligosaccharides/analysis
• Oligosaccharides/radiation effects
• Peptides/analysis
• Peptides/metabolism
• Peptides/radiation effects
• Protein Processing, Post-Translational
• Proteins/analysis
• Proteins/metabolism
• Proteins/radiation effects
• Proteomics
• Ultraviolet Rays

• R01 GM103655 NIGMS NIH HHS
• R01 GM121714 NIGMS NIH HHS

• Rheumatoid arthritis
• alpha 2 macroglobulin
• autoimmunity
• nitration
• peroxynitrite

• Animals
• Arthritis, Rheumatoid
• Autoantibodies/immunology
• Epitopes/immunology
• Humans
• Peroxynitrous Acid
• Rabbits
• alpha-Macroglobulins/immunology

Low temperature (LT) negatively affects plant growth and development via the alteration of the metabolism of reactive oxygen and nitrogen species (ROS and RNS). Among RNS, tyrosine nitration, the addition of an NO₂ group to a tyrosine residue, can modulate reduced nicotinamide-dinucleotide phosphate (NADPH)-generating systems and, therefore, can alter the levels of NADPH, a key cofactor in cellular redox homeostasis. NADPH also acts as an indispensable electron donor within a wide range of enzymatic reactions, biosynthetic pathways, and detoxification processes, which could affect plant viability. To extend our knowledge about the regulation of this key cofactor by this nitric oxide (NO)-related post-translational modification, we analyzed the effect of tyrosine nitration on another NADPH-generating enzyme, the NADP-malic enzyme (NADP-ME), under LT stress. In Arabidopsis thaliana seedlings exposed to short-term LT (4 °C for 48 h), a 50% growth reduction accompanied by an increase in the content of superoxide, nitric oxide, and peroxynitrite, in addition to diminished cytosolic NADP-ME activity, were found. In vitro assays confirmed that peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration. The mass spectrometric analysis of nitrated NADP-ME2 enabled us to determine that Tyr-73 was exclusively nitrated to 3-nitrotyrosine by peroxynitrite. The in silico analysis of the Arabidopsis NADP-ME2 protein sequence suggests that Tyr73 nitration could disrupt the interactions between the specific amino acids responsible for protein structure stability. In conclusion, the present data show that short-term LT stress affects the metabolism of ROS and RNS, which appears to negatively modulate the activity of cytosolic NADP-ME through the tyrosine nitration process.

• NADP malic enzyme
• low temperature
• nitric oxide
• nitro-oxidative stress
• peroxynitrite
• reactive nitrogen species
• reactive oxygen species
• tyrosine nitration

• Antioxidation
• Catalytic activity
• Peroxynitrite decomposition
• Protein nitration
• Water-soluble iron porphyrins

Arterial stiffness, which increases with aging and hypertension, is an independent cardiovascular risk factor. While stiffer substrates are known to affect single endothelial cell morphology and migration, the effect of substrate stiffness on endothelial monolayer function is less understood. The objective of this study was to determine if substrate stiffness increased endothelial monolayer reactive oxygen species (ROS) in response to protein kinase C (PKC) activation and if this oxidative stress then impacted adherens junction integrity. Porcine aortic endothelial cells were cultured on varied stiffness polyacrylamide gels and treated with phorbol 12-myristate 13-acetate (PMA), which stimulates PKC and ROS without increasing actinomyosin contractility. PMA-treated endothelial cells on stiffer substrates increased ROS and adherens junction loss without increased contractility. ROS scavengers abrogated PMA effects on cell-cell junctions, with a more profound effect in cells on stiffer substrates. Finally, endothelial cells in aortae from elastin haploinsufficient mice (Eln+/-), which were stiffer than aortae from wild-type mice, showed decreased VE-cadherin colocalization with peripheral actin following PMA treatment. These data suggest that oxidative stress may be enhanced in endothelial cells in stiffer vessels, which could contribute to the association between arterial stiffness and cardiovascular disease.

• Acute myocardial infarction
• Adenosine triphosphate (ATP)
• Atherosclerosis
• DNA repair
• Heart failure
• Nicotinamide adenine dinucleotide (NAD+)
• PARP inhibition
• Poly(ADP-ribose)polymerase-1 (PARP1)

• Peroxynitrite
• autoimmunity
• biomolecules
• free radicals
• nitrotyrosine

A high glucose state readily causes peripheral axon atrophy, demyelination, loss of nerve fiber function, and delayed regeneration. However, few studies have examined whether nitration is also critical for diabetic peripheral neuropathy. Therefore, this study investigated the effects of high glucose on proliferation, apoptosis, and 3-nitrotyrosine levels of Schwann cells treated with butylphthalide. In addition, we explored potential protective mechanisms of butylphthalide on peripheral nerves. Schwann cells were cultured in vitro with high glucose then stimulated with the peroxynitrite anion inhibitors uric acid and 3-n-butylphthalide for 48 hours. Cell Counting Kit-8 and flow cytometry were used to investigate the effects of uric acid and 3-n-butylphthalide on proliferation and apoptosis of Schwann cells exposed to a high glucose environment. Effects of uric acid and 3-n-butylphthalide on levels of 3-nitrotyrosine in Schwann cells were detected by enzyme-linked immunosorbent assay. The results indicated that Schwann cells cultured in high glucose showed decreased proliferation, but increased apoptosis and intracellular 3-nitrotyrosine levels. However, intervention with uric acid or 3-n-butylphthalide could increase proliferation of Schwann cells cultured in high glucose, and inhibited apoptosis and intracellular 3-nitrotyrosine levels. According to our data, 3-n-butylphthalide may inhibit cell nitrification and apoptosis, and promote cell proliferation, thereby reducing damage to Schwann cells caused by high glucose.

• 3-n-butylphthalide
• 3-nitrotyrosine
• Schwann cells
• apoptosis
• diabetic peripheral neuropathy
• nerve regeneration
• neural regeneration
• nitration stress
• peroxynitrite anions
• proliferation
• uric acid

• AMP-Activated Protein Kinases/metabolism
• Alkynes
• Animals
• Anti-Retroviral Agents/pharmacology
• Anti-Retroviral Agents/therapeutic use
• Benzoxazines/pharmacology
• Benzoxazines/therapeutic use
• Cyclopropanes
• Diet, High-Fat
• Drug Therapy, Combination
• Emtricitabine/pharmacology
• Emtricitabine/therapeutic use
• Heart/drug effects
• Male
• Myocardium/metabolism
• Nitric Oxide Synthase Type III/metabolism
• Obesity/pathology
• Oxidative Stress/drug effects
• Proto-Oncogene Proteins c-akt/metabolism
• Rats
• Rats, Wistar
• Reperfusion Injury/metabolism
• Reperfusion Injury/prevention & control
• Reperfusion Injury/veterinary
• Tenofovir/pharmacology
• Tenofovir/therapeutic use

• South African National Research Foundation
• South African Research Foundation
• Harry Crossley Foundation
• South African Department of Science and Technology

Protein nitration and nitrosylation are essential post-translational modifications (PTMs) involved in many fundamental cellular processes. Recent studies have revealed that excessive levels of nitration and nitrosylation in some critical proteins are linked to numerous chronic diseases. Therefore, the identification of substrates that undergo such modifications in a site-specific manner is an important research topic in the community and will provide candidates for targeted therapy. In this study, we aimed to develop a computational tool for predicting nitration and nitrosylation sites in proteins. We first constructed four types of encoding features, including positional amino acid distributions, sequence contextual dependencies, physicochemical properties, and position-specific scoring features, to represent the modified residues. Based on these encoding features, we established a predictor called DeepNitro using deep learning methods for predicting protein nitration and nitrosylation. Using n-fold cross-validation, our evaluation shows great AUC values for DeepNitro, 0.65 for tyrosine nitration, 0.80 for tryptophan nitration, and 0.70 for cysteine nitrosylation, respectively, demonstrating the robustness and reliability of our tool. Also, when tested in the independent dataset, DeepNitro is substantially superior to other similar tools with a 7%−42% improvement in the prediction performance. Taken together, the application of deep learning method and novel encoding schemes, especially the position-specific scoring feature, greatly improves the accuracy of nitration and nitrosylation site prediction and may facilitate the prediction of other PTM sites. DeepNitro is implemented in JAVA and PHP and is freely available for academic research at http://deepnitro.renlab.org.

• Deep learning
• Feature extraction
• Functional site prediction
• Protein nitration and nitrosylation
• Web service

Preeclampsia is a persistent hypertensive gestational disease characterized by high blood pressure and proteinuria, which presents from the second trimester of pregnancy. At the cellular level, preeclampsia has largely been associated with the release of free radicals by the placenta. Placenta-borne oxidative and nitrosative stresses are even sometimes considered as the major molecular determinants of the maternal disease. In this review, we present the recent literature evaluating free radical production in both normal and pathological placentas (including preeclampsia and other major pregnancy diseases), in humans and animal models. We then assess the putative effects of these free radicals on the placenta and maternal endothelium. This analysis was conducted with regard to recent papers and possible therapeutic avenues.

• oxidative stress
• placenta
• preeclampsia
• pregnancy
• vascular endothelium

• Abdominal aortic aneurysm
• Autoimmunity
• Fibrinogen
• Nitric oxide
• Smoking

The primary function of chemokines is to direct the migration of leukocytes to the site of injury during inflammation. The effects of chemokines are modulated by several means, including binding to G-protein coupled receptors (GPCRs), binding to glycosaminoglycans (GAGs), and through post-translational modifications (PTMs). GAGs, present on cell surfaces, bind chemokines released in response to injury. Chemokines bind leukocytes via their GPCRs, which directs migration and contributes to local inflammation. Studies have shown that GAGs or GAG-binding peptides can be used to interfere with chemokine binding and reduce leukocyte recruitment. Post-translational modifications of chemokines, such as nitration, which occurs due to the production of reactive species during oxidative stress, can also alter their biological activity. This review describes the regulation of chemokine function by GAG-binding ability and by post-translational nitration. These are both aspects of chemokine biology that could be targeted if the therapeutic potential of chemokines, like CXCL8, to modulate inflammation is to be realised.

• PTM
• chemokine nitration
• chemokine-GAG interaction
• synthetic peptide chemistry

• Animals
• Chemokines/metabolism
• Glycosaminoglycans/metabolism
• Humans
• Inflammation/metabolism
• Inflammation/pathology
• Oxidative Stress
• Protein Processing, Post-Translational
• Receptors, Chemokine/metabolism

• FS/15/19/31327 British Heart Foundation

• Air Pollutants
• Air Pollution
• Allergens/immunology
• Climate Change
• Humans
• Hypersensitivity

Glutamate dehydrogenase (GDH) of animal cells is usually considered to be a mitochondrial enzyme. However, this enzyme has recently been reported to be also present in nucleus, endoplasmic reticulum and lysosomes. These extramitochondrial localizations are associated with moonlighting functions of GDH, which include acting as a serine protease or an ATP-dependent tubulin-binding protein. Here, we review the published data on kinetics and localization of multiple forms of animal GDH taking into account the splice variants, post-translational modifications and GDH isoenzymes, found in humans and apes. The kinetic properties of human GLUD1 and GLUD2 isoenzymes are shown to be similar to those published for GDH1 and GDH2 from bovine brain. Increased functional diversity and specific regulation of GDH isoforms due to alternative splicing and post-translational modifications are also considered. In particular, these structural differences may affect the well-known regulation of GDH by nucleotides which is related to recent identification of thiamine derivatives as novel GDH modulators. The thiamine-dependent regulation of GDH is in good agreement with the fact that the non-coenzyme forms of thiamine, i.e., thiamine triphosphate and its adenylated form are generated in response to amino acid and carbon starvation.

• acetylation
• adenylated thiamine triphosphate
• glutamate dehydrogenase alternative splicing
• glutamate dehydrogenase isoenzymes
• glutamate dehydrogenase isoforms
• nucleotide-dependent regulation

• Adventitial fibroblast
• Interleukin-1β
• Macrophage
• TAC model
• Vascular fibrosis
• iNOS

• beetroot
• blood pressure
• ischaemia
• nitric oxide
• vasodilatation

Nitration of tyrosine and other aromatic amino acid residues in proteins occurs in the setting of inflammatory, neurodegenerative, and cardiovascular diseases—importantly, this modification has been implicated in the pathogenesis of diverse diseases and the physiological process of aging. To understand the biological consequences of aromatic nitration in both health and disease, it is critical to molecularly identify the proteins that undergo nitration, specify their cognate modification sites and quantify their extent of nitration. To date, unbiased identification of nitrated proteins has often involved painstaking 2D-gel electrophoresis followed by Western Blotting with an anti-nitrotyrosine antibody for detection. Apart from being relatively slow and laborious, this method suffers from limited coverage, the potential for false-positive identifications, and failure to reveal specific amino acid modification sites. To overcome these shortcomings, we have developed a solid-phase, chemical-capture approach for unbiased and high-throughput discovery of nitrotyrosine and nitrotryptophan sites in proteins. Utilizing this method, we have successfully identified several endogenously nitrated proteins in rat brain and a total of 244 nitrated peptides from 145 proteins following in vitro exposure of rat brain homogenates to the nitrating agent peroxynitrite (1 mM). As expected, Tyr residues constituted the great majority of peroxynitrite-mediated protein nitration sites; however, we were surprised to discover several brain proteins that contain nitrated Trp residues. By incorporating a stable-isotope labeling step, this new Aromatic Nitration Site IDentification (ANSID) method was also adapted for relative quantification of nitration site abundances in proteins. Application of the ANSID method offers great potential to advance our understanding of the role of protein nitration in disease pathogenesis and normal physiology.

• nitric oxide
• nitrosative stress
• nitrotryptophan
• nitrotyrosine
• peroxynitrite
• post-translational modifications
• proteomics

• S-nitrosylation
• ascorbate-glutathione cycle
• catalase
• nitric oxide
• peroxiredoxin
• superoxide dismutase
• tyrosine nitration

There has been some dispute regarding reaction products formed at physiological peroxynitrite fluxes in the nanomolar range with phenolic molecules, when used to predict the behavior of protein-bound aromatic amino acids like tyrosine. Previous data showed that at nanomolar fluxes of peroxynitrite, nitration of these phenolic compounds was outcompeted by dimerization (e.g. biphenols or dityrosine). Using 3-morpholino sydnonimine (Sin-1), we created low fluxes of peroxynitrite in our reaction set-up to demonstrate that salicylaldehyde displays unique features in the detection of physiological fluxes of peroxynitrite, yielding detectable nitration but only minor dimerization products.

By means of HPLC analysis and detection at 380 nm we could identify the expected nitration products 3- and 5-nitrosalicylaldehyde, but also novel nitrated products. Using mass spectrometry, we also identified 2-nitrophenol and a not fully characterized nitrated dimerization product. The formation of 2-nitrophenol could proceed either by primary generation of a phenoxy radical, followed by addition of the NO₂-radical to the various resonance structures, or by addition of the peroxynitrite anion to the polarized carbonyl group with subsequent fragmentation of the adduct (as seen with carbon dioxide). Interestingly, we observed almost no 3- and 5-nitrosalicylic acid products and only minor dimerization reaction.

Our results disagree with the previous general assumption that nitration of low molecular weight phenolic compounds is always outcompeted by dimerization at nanomolar peroxynitrite fluxes and highlight unique features of salicylaldehyde as a probe for physiological concentrations of peroxynitrite.

•

There are no specific probes for peroxynitrite formation in vivo.

• aging
• exercise
• oxidative stress
• retina
• treadmill

• 8-Hydroxy-2'-Deoxyguanosine
• Aging/metabolism
• Aging/physiology
• Animals
• Deoxyguanosine/analogs & derivatives
• Deoxyguanosine/metabolism
• Lysine/analogs & derivatives
• Lysine/metabolism
• Male
• Mice
• Oxidative Stress
• Physical Conditioning, Animal/methods
• Physical Conditioning, Animal/physiology
• Retina/cytology
• Retina/metabolism
• Tyrosine/analogs & derivatives
• Tyrosine/metabolism

• Capsicum annuum
• MALDI-TOF/TOF
• NO gas
• RNS
• Solanaceae
• confocal laser scanning microscopy
• nitric oxide
• nitro-tyrosine
• nitrosothiols
• pepper fruit
• protein nitration
• proteomics
• reactive nitrogen species
• ripening

• Capsicum/growth & development
• Capsicum/metabolism
• Fruit/growth & development
• Fruit/metabolism
• Nitro Compounds/metabolism
• Plant Proteins/metabolism
• Proteomics
• Tyrosine/metabolism

• Inducible NO synthase
• Oxidative stress
• Pigs
• S-Nitrosylated proteins
• Tachyarrhythmic experimental model of heart failure

• Animals
• Coronary Artery Disease/metabolism
• Coronary Artery Disease/pathology
• Ischemic Preconditioning, Myocardial
• Nitric Oxide/metabolism
• Protein Processing, Post-Translational
• Signal Transduction

• Apoplast
• Arabidopsis thaliana
• Nicotina tabacum
• Nitrotyrosines
• Proteomics
• Suspension cultures

• Apoproteins/metabolism
• Apoptosis Regulatory Proteins/metabolism
• Arabidopsis/metabolism
• Cells, Cultured
• Nitric Oxide/metabolism
• Nitrogen/metabolism
• Plant Proteins/metabolism
• Nicotiana/metabolism
• Tyrosine/analogs & derivatives
• Tyrosine/metabolism