Results 121 to 130 of about 4,880 (161)
The red blood cell proteome and interactome identify a Band 3-BLVRB axis regulating hypoxic metabolic adaptation. [PDF]
BloodIssaian AV +28 more
europepmc +1 more source
Proteomic methods for analysis of S-nitrosation [PDF]
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, 2007 This review discusses proteomic methods to detect and identify S-nitrosated proteins. Protein S-nitrosation, the post-translational modification of thiol residues to form S-nitrosothiols, has been suggested to be a mechanism of cellular redox signaling by which nitric oxide can alter cellular function through modification of protein thiol residues.
Neil Hogg +2 more
exaly +3 more sources
SNObase, a database for S-nitrosation modification [PDF]
Protein and Cell, 2012 S-Nitros(yl)ation is a ubiquitous redox-based post-translational modification of protein cysteine thiols by nitric oxide or its derivatives, which transduces the bioactivity of nitric oxide (NO) by regulation of protein conformation, activity, stability, localization and protein-protein interactions.
Bo Huang, Yuying Zhang, Xu Zhang
exaly +3 more sources
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Methods in enzymology, 1999
A series of peptidyl N-nitrosoanilines were designed, synthesized, and evaluated as inactivators of cysteine protease papain. These new compounds exhibited different inhibitory activities toward cysteine protease papain in a time- and concentration-dependent manner with second-order rate constants (ki/KI) ranging over two orders of magnitude from 0.604
Z, Guo, N, Miranda, P G, Wang
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A series of peptidyl N-nitrosoanilines were designed, synthesized, and evaluated as inactivators of cysteine protease papain. These new compounds exhibited different inhibitory activities toward cysteine protease papain in a time- and concentration-dependent manner with second-order rate constants (ki/KI) ranging over two orders of magnitude from 0.604
Z, Guo, N, Miranda, P G, Wang
openaire +3 more sources
Nature Chemical Biology, 2005
Protein nitrosation is an important signaling mechanism in vivo; however, mechanisms for selective nitric oxide modification of cysteines have not been described. Thioredoxin is now shown to rapidly and site-specifically catalyze S-nitrosation of an active site cysteine of caspase-3.
Steven R Tannenbaum, Ji-Eun Kim
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Protein nitrosation is an important signaling mechanism in vivo; however, mechanisms for selective nitric oxide modification of cysteines have not been described. Thioredoxin is now shown to rapidly and site-specifically catalyze S-nitrosation of an active site cysteine of caspase-3.
Steven R Tannenbaum, Ji-Eun Kim
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Further study on S-nitrosation by nitrite
Frontiers in Bioscience, 2003At neutral pH, S-nitrosoglutathione was formed by the reaction of reduced glutathione and sodium nitrite. The degradation of S-nitrosoglutathione, presumably by transnitrosation/denitrosation, was catalyzed by L-cysteine, or CoA-SH. Additionally, from the crude extract of rat brain, one protein with a large molecular mass was nitrosolated with nitrite,
Wu-Nan, Kuo +4 more
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Kinetics and equilibria of the S-nitrosation of alkylthioureas
Journal of the Chemical Society, Perkin Transactions 2, 1975The equilibrium constants for the addition of the nitrosonium ion to the sulphur atom of a range of alkylthioureas have been measured, and shown to correlate well with the ionisation constants of the corresponding conjugate acids. Stopped-flow studies of the rate of reaction show it to occur by an encounter-controlled process.
Peter Collings +2 more
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Inactivation of Soluble Guanylate Cyclase by Stoichiometric S-Nitrosation
Molecular Pharmacology, 2009Dysfunction of vascular nitric oxide (NO)/cGMP signaling is believed to contribute essentially to various cardiovascular disorders. Besides synthesis and/or bioavailability of endothelial NO, impaired function of soluble guanylate cyclase (sGC) may play a key role in vascular dysfunction.
Bernd, Mayer +6 more
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S-Nitrosation and Regulation of Inducible Nitric Oxide Synthase
Biochemistry, 2005The inducible isoform of nitric oxide synthase (iNOS) and three zinc tetrathiolate mutants (C104A, C109A, and C104A/C109A) were expressed in Escherichia coli and purified. The mutants were found by ICP-AES and the zinc-specific PAR colorimetric assay to be zinc free, whereas the wild-type iNOS zinc content was 0.38 +/- 0.01 mol of Zn/mol of iNOS dimer.
Douglas A, Mitchell +3 more
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Warhead Strategy for Targeted Protein S-Nitrosation
Journal of the American Chemical SocietyProtein post-translational modifications (PTMs) are critical factors in disease progression. While progress has been made in regulating disease-associated PTMs such as phosphorylation and acetylation, the approach to achieving targeted S-nitrosation for disease treatment, particularly in vivo, remains largely uncharted.
Chen Zhang +11 more
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