Results 181 to 190 of about 207,078 (211)
Some of the next articles are maybe not open access.

Nitration of tyrosine in three cobra neurotoxins

Toxicon, 1976
Abstract The curarumimetic snake venom toxins always have a tyrosine residue in the same position in their sequences. This invariant tyrosine in three neurotoxins has been nitrated with tetranitromethane. The toxins were: (1) siamensis 3 of the structural type 71-5 (no. of amino acid residues and disulfides) and with one tyrosine, the main neurotoxin
E, Karlsson, J, Sundelin
openaire   +2 more sources

Protein tyrosine nitration in the cell cycle

Biochemical and Biophysical Research Communications, 2011
Nitration of tyrosine residues in proteins is associated with cell response to oxidative/nitrosative stress. Tyrosine nitration is relatively low abundant post-translational modification that may affect protein functions. Little is known about the extent of protein tyrosine nitration in cells during progression through the cell cycle.
Min, Jia   +2 more
openaire   +2 more sources

Nitration of Tyrosine by Hydrogen Peroxide and Nitrite

Free Radical Research, 1995
Peroxynitrite anion is a powerful oxidant which can initiate nitration and hydroxylation of aromatic rings. Peroxynitrite can be formed in several ways, e.g. from the reaction of nitric oxide with superoxide or from hydrogen peroxide and nitrite at acidic pH.
T D, Oury   +3 more
openaire   +2 more sources

Biochemistry of Peroxynitrite and Protein Tyrosine Nitration

Chemical Reviews, 2018
Peroxynitrite is a short-lived and reactive biological oxidant formed from the diffusion-controlled reaction of the free radicals superoxide (O2•-) and nitric oxide (•NO). In this review, we first analyze the biochemical evidence for the formation of peroxynitrite in vivo and the reactions that lead to it. Then, we describe the principal reactions that
Gerardo Ferrer-Sueta   +7 more
openaire   +2 more sources

Tetranitromethane as a Nitrating Reagent for Tyrosine and Tyrosine-Containing Peptides and Proteins

Canadian Journal of Biochemistry, 1971
After nitration of hemoglobin and ribonuclease with tetranitromethane, the sum of tyrosine and nitrotyrosine accounted for 80% or less of the tyrosyl residues known to be present in these proteins. Reasons for this discrepancy were explored by nitrating tyrosine, glycyltyrosine, and glycyltyrosylglycine.
N D, Boyd, D B, Smith
openaire   +2 more sources

Monitoring peptide tyrosine nitration by spectroscopic methods

Amino Acids, 2020
Oxidative stress can lead to various derivatives of the tyrosine residue in peptides and proteins. A typical product is 3-nitro-L-tyrosine residue (Nit), which can affect protein behavior during neurodegenerative processes, such as those associated with Alzheimer's and Parkinson's diseases. Surface enhanced Raman spectroscopy (SERS) is a technique with
Petr Niederhafner   +5 more
openaire   +2 more sources

Protein Tyrosine Phosphorylation and Protein Tyrosine Nitration in Redox Signaling

Antioxidants & Redox Signaling, 2008
Reversible phosphorylation of protein tyrosine residues by polypeptide growth factor-receptor protein tyrosine kinases is implicated in the control of fundamental cellular processes including the cell cycle, cell adhesion, and cell survival, as well as cell proliferation and differentiation.
Hugo P, Monteiro   +2 more
openaire   +2 more sources

Effects of tyrosine-26 and tyrosine-64 nitration on the photoreactions of bacteriorhodopsin

Biochemistry, 1985
In the dark, all titratable tyrosine residues of bacteriorhodopsin have pK's of greater than 11.0, which may be caused by the hydrophobic environment for buried residues and by high negative charge density for surface residues [Scherrer, P., & Stoeckenius, W. (1984) Biochemistry 23, 6195-6202].
P, Scherrer, W, Stoeckenius
openaire   +2 more sources

Mass Mapping Sites of Nitration in Tyrosine Hydroxylase:  Random vs Selective Nitration of Three Tyrosine Residues

Chemical Research in Toxicology, 2003
Previous work has shown that tyrosine residues Y423, Y428, and Y432 are potential targets for nitration when tyrosine hydroxylase is exposed to peroxynitrite. For any given protein molecule, up to three nitration events involving these residues may occur.
Chad R, Borges   +2 more
openaire   +2 more sources

Modifications of tyrosine and catecholamines by peroxynitrite nitrite and nitrate

Frontiers in Bioscience, 2003
At pH 7.0 in non-"deaired" potassium phosphate buffer, the reactions of L-tyrosine, L-dopa, dopamine, L-norepinephrine, and L-epinephrine with peroxynitrite (PN) or nitrite, generated colored products. These products displayed not only unique colors and patterns of mobility on silica thin layer chromatographic plates, but also varied increase of ...
Wu-Nan, Kuo   +2 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy