Results 151 to 160 of about 8,951 (194)
The Bright and Dark Sides of Nitric Oxide in Neurodegenerative Diseases. [PDF]
J Pers MedBuccarello L +9 more
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5-Hydroxymethylfurfural: A Particularly Harmful Molecule Inducing Toxic Lipids and Proteins? [PDF]
MoleculesGreilberger J +4 more
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Light‐Controlled Tyrosine Nitration of Proteins
Angewandte Chemie - International Edition, 2021AbstractTyrosine nitration of proteins is one of the most important oxidative post‐translational modifications in vivo. A major obstacle for its biochemical and physiological studies is the lack of efficient and chemoselective protein tyrosine nitration reagents. Herein, we report a generalizable strategy for light‐controlled protein tyrosine nitration
Julian D Hegemann, Huan Wang
exaly +3 more sources
Protein tyrosine nitration—An update
Archives of Biochemistry and Biophysics, 2009Tyrosine nitration is a covalent post-translational protein modification derived from the reaction of proteins with nitrating agents. Tyrosine nitration has been used as a marker of oxidant burden in human diseases. However, it remains unclear whether protein nitration is responsible for alterations in protein function that imparts an increased risk ...
Harry Ischiropoulos
exaly +3 more sources
Biochemical and Biophysical Research Communications, 2009
Protein tyrosine nitration (PTN) is a selective post-translational modification often associated with pathophysiological conditions. Although yeast cells lack of mammalian nitric oxide synthase (NOS) orthologues, still it has been shown that they are capable of producing nitric oxide (NO).
Uddalak Majumdar +2 more
exaly +3 more sources
Protein tyrosine nitration (PTN) is a selective post-translational modification often associated with pathophysiological conditions. Although yeast cells lack of mammalian nitric oxide synthase (NOS) orthologues, still it has been shown that they are capable of producing nitric oxide (NO).
Uddalak Majumdar +2 more
exaly +3 more sources
Journal of Proteome Research, 2009
Protein tyrosine nitration (PTN) is a post-translational modification occurring under the action of a nitrating agent. Tyrosine is modified in the 3-position of the phenolic ring through the addition of a nitro group (NO2). In the present article, we review the main nitration reactions and elucidate why nitration is not a random chemical process.
Huib Kerstjens +2 more
exaly +4 more sources
Protein tyrosine nitration (PTN) is a post-translational modification occurring under the action of a nitrating agent. Tyrosine is modified in the 3-position of the phenolic ring through the addition of a nitro group (NO2). In the present article, we review the main nitration reactions and elucidate why nitration is not a random chemical process.
Huib Kerstjens +2 more
exaly +4 more sources
Protein tyrosine nitration in atherosclerotic endothelial dysfunction
Clinica Chimica Acta, 2022Accumulation of reactive oxygen species (ROS) can induce both protein tyrosine nitration and endothelial dysfunction in atherosclerosis. Endothelial dysfunction refers to impaired endothelium-dependent vasorelaxation that can be triggered by an imbalance in nitric oxide (NO) production and consumption.
Miao Jiang, Da-Wei Zhang, Guixue Wang
exaly +3 more sources
Mitochondrial protein tyrosine nitration
Free Radical Research, 2010Mitochondria are primary loci for the intracellular formation and reactions of reactive oxygen and nitrogen species including superoxide (O₂•⁻), hydrogen peroxide (H₂O₂) and peroxynitrite (ONOO⁻). Depending on formation rates and steady-state levels, the mitochondrial-derived short-lived reactive species contribute to signalling events and/or ...
Laura, Castro +3 more
openaire +2 more sources
Mitochondria and regulated tyrosine nitration
Biochemical Society Transactions, 2005The conditions of the cellular microenvironment in complex multicellular organisms fluctuate, enforcing permanent adaptation of cells at multiple regulatory levels. Covalent post-translational modifications of proteins provide the short-term response tools for cellular adjustment and growing evidence supports the possibility that protein tyrosine ...
T, Koeck, D J, Stuehr, K S, Aulak
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