Tracing the path of inhaled nitric oxide: Biological consequences of protein nitrosylation

Bhatia, Vikram; Elnagary, Lara; Dakshinamurti, Shyamala

doi:10.1002/ppul.25201

Cited by 11 publications

(10 citation statements)

References 205 publications

(294 reference statements)

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“…S-nitrosylation, as well as S-glutathionylation, serves as a reversible post-translational modification of thiol groups of proteins [15,66,67]. In mammals, nitric oxide (NO) is mainly synthesized by nitric oxide synthase (NOS), for which three isoforms are known: Two constitutive-NOS1 (neuronal, nNOS) and NOS3 (endothelial eNOS)-as well as inducible NOS2 (iNOS), which have approximately 50% homology [68][69][70].…”

Section: Protein S-nitrosylation and Denitrosylationmentioning

confidence: 99%

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Калинина

Novichkova

2021

Molecules

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S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and “switch” functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

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Section: Protein S-nitrosylation and Denitrosylationmentioning

confidence: 99%

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Калинина

Novichkova

2021

Molecules

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“…Pulmonary and cardiac tissues are often hypoxic at the time of therapeutic intervention, which may impair responsiveness to vasodilator therapy. [2][3][4][5] Hypoxia is known to attenuate the sensitivity of pulmonary arterial adenylyl cyclase (AC) to prostacyclin 6 or β-adrenergic stimulation. 7 The AC-Gαs-cAMP pathway is a key pathway for pulmonary vasodilation and cardiac contraction.…”

mentioning

confidence: 99%

Critical cysteines in the functional interaction of adenylyl cyclase isoform 6 with Gαs

et al. 2021

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“…A promising compound currently undergoing clinical trials for COVID-19 is nitric oxide (NO) [70]. Besides its role as an important vasodilator, to prevent blood clot formation, it functions as a vital immune mediator, exerting broad spectrum antiviral effects [71].…”

Section: Resultsmentioning

confidence: 99%

Open modification searching of SARS-CoV-2–human protein interaction data reveals novel viral modification sites

Adams

Boonen

Laukens

et al. 2022

Preprint

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The outbreak of the SARS-CoV-2 coronavirus, the causative agent of the COVID-19 disease, has led to an ongoing global pandemic since 2019. Mass spectrometry can be used to understand the molecular mechanisms of viral infection by SARS-CoV-2, for example, by determining virus-host protein-protein interactions (PPIs) through which SARS-CoV-2 hijacks its human hosts during infection, and to study the role of post-translational modifications (PTMs). We have reanalyzed public affinity purification mass spectrometry data using open modification searching to investigate the presence of PTMs in the context of the SARS-CoV-2 virus-host PPI network. Based on an over two-fold increase in identified spectra, our detected protein interactions show a high overlap with independent mass spectrometry-based SARS-CoV-2 studies and virus-host interactions for alternative viruses, as well as previously unknown protein interactions. Additionally, we identified several novel modification sites on SARS-CoV-2 proteins that we investigated in relation to their interactions with host proteins. A detailed analysis of relevant modifications, including phosphorylation, ubiquitination, and S-nitrosylation, provides important hypotheses about the functional role of these modifications during viral infection by SARS-CoV-2.

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Tracing the path of inhaled nitric oxide: Biological consequences of protein nitrosylation

Cited by 11 publications

References 205 publications

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Critical cysteines in the functional interaction of adenylyl cyclase isoform 6 with Gαs

Open modification searching of SARS-CoV-2–human protein interaction data reveals novel viral modification sites

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