Reversible modification of cysteines such as disulfide bond formation, glutathionylation, and nitrosylation may also be a means of protection from further, generally irreversible, modifications to sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acids [ 9 ]. (hindawi.com)
Proteomic1
In this study, we present a highly efficient method for proteomic profiling of cysteine residues in complex proteomes and in living cells. (unige.ch)
Thus, reversible cysteine modifications can influence protein activity and the relative quantification of the status of the thiol can potentially provide valuable insights into protein activity where the protein exists in a range of redox states. (hindawi.com)
Xiao and intestinal alterations indicative of mucosal dysbiosis (Grasberger IFN\ and IFN\ (Fink (Fink model of lung epithelial injury in mice (Gorissen redox\dependent regulation of cell signalling pathways, by reversible oxidation of functional cysteine residues. (ees2010prague.org)
Proteomics2
We anticipate that this new method for cysteine profiling will find broad application in chemical proteomics and drug discovery. (unige.ch)
We have developed a proteomics approach to quantitatively profile the changes of sulfhydrated cysteines in biological systems. (pharmaceuticalintelligence.com)
Redox5
We propose application of iTRAQ reagents in combination with a previous thiol selection method to relatively quantify the redox state of cysteines both within and between samples in a single analysis. (hindawi.com)
Our method allows for the identification of the proteins, identification of redox-sensitive cysteines within proteins, and quantification of the redox status of individual cysteine-containing peptides. (hindawi.com)
Cysteine is the most important redox-responsive amino acid within proteins largely due to the wide range of oxidation states that sulfur can occupy-so called, "sulfur switches" [ 4 ]. (hindawi.com)
Cysteines often form part of active sites, allowing for the protein to be switched on or off depending on redox state. (hindawi.com)
The biological significance of the Cys150 modification by H2S is not well-studied, but H2S could serve as a biological switch for protein function acting via oxidative modification of specific cysteine residues in response to redox homeostasis (Paul and Snyder, 2012). (pharmaceuticalintelligence.com)
Proteins7
Cysteines are one of the most rarely used amino acids, but when conserved in proteins they often play critical roles in structure, function, or regulation. (hindawi.com)
Indeed, it has been demonstrated that cysteines are characterized by the most extreme conservation pattern, being highly conserved in functional positions of proteins but poorly conserved otherwise [ 5 ]. (hindawi.com)
In proteins where cysteine is not within the active site, activity can be modulated by changing conformation or by influencing its regulatory role, for example, ironsulfur complexes (ISCs) in aconitase possess cysteines required for its activity [ 7 ]. (hindawi.com)
Interactions with other proteins or molecules are another feature of cysteines that can affect protein activity. (hindawi.com)
Allosterically regulated proteins that require an activator are sometimes based on a thiol exchange interaction involving cysteines, for example, pyruvate kinase uses fructose bisphosphate (FBPs) as a heterotrophic activator and it contains a cysteine in its FBP binding site [ 8 ]. (hindawi.com)
Reactive cysteine residues in proteins have high nucleophilicity and low pKa values and serve as a major target for oxidative modifications, which can vary depending on the subcellular environment, including the type and intensity of intracellular or environmental cues. (pharmaceuticalintelligence.com)
Amino acid1
The covalent modification of specific amino acid residues influences diverse biological processes and cell physiology across species. (pharmaceuticalintelligence.com)
Glutathionylation1
2009). Sulfhydrated GAPDH at Cys150 exhibits an increase in its catalytic activity, in contrast to the inhibitory effects of nitrosylation or glutathionylation of the same cysteine residue (Mustafa et al. (pharmaceuticalintelligence.com)
Enzymes2
In pancreatic β cells exposed to endoplasmic reticulum (ER) stress, elevated H2S promotes the sulfhydration of enzymes in energy metabolism and stimulates glycolytic flux. (pharmaceuticalintelligence.com)
We propose that transcriptional and translational reprogramming by the Integrated Stress Response (ISR) in pancreatic β cells is coupled to metabolic alternations triggered by sulfhydration of key enzymes in intermediary metabolism. (pharmaceuticalintelligence.com)
Cellular1
Our results demonstrate that curcumin covalently modifies several key players of cellular signaling and metabolism, most notably the enzyme casein kinase I gamma. (unige.ch)
Important1
2016). The identity of the DUOX1 cysteines targeted by these electrophiles is yet to be established, but these studies offer the exciting prospect that selective targeting of specific functionally important cysteines within DUOX1 may lead to inhibition of DUOX1, and could be exploited for the development of DUOX\selective inhibitors to treat allergic disorders such as asthma, allergic rhinitis, atopic dermatitis and conjunctivitis. (ees2010prague.org)
Identification1
2012). Despite great progress in bioinformatics and advanced mass spectroscopic techniques (MS), identification of different cysteine-based protein modifications has been slow compared to other post-translational modifications. (pharmaceuticalintelligence.com)
Analysis1
Bioinformatics analysis revealed that sulfhydrated cysteines are part of a wide range of biological functions. (pharmaceuticalintelligence.com)
Oxidation4
Accurate quantification of cysteine oxidation is therefore crucial for decoding protein redox regulation. (bvsalud.org)
Here, we present CysQuant, a novel approach for simultaneous quantification of cysteine oxidation degrees and protein abundancies. (bvsalud.org)
CysQuant involves light/heavy iodoacetamide isotopologues for differential labeling of reduced and reversibly oxidized cysteines analyzed by data-dependent acquisition (DDA) or data-independent acquisition mass spectrometry (DIA-MS). Using plexDIA with in silico predicted spectral libraries, we quantified an average of 18% cysteine oxidation in Arabidopsis thaliana by DIA-MS, including a subset of highly oxidized cysteines forming disulfide bridges in AlphaFold2 predicted structures. (bvsalud.org)
2 h) in the extracellular environment by oxidation of critical cysteine residues 31 . (nature.com)
Crucial1
Numerous familial hypercholestorolemia mutations of the LDL receptor alter the calcium coordinating residue of LDL-A domains or other crucial scaffolding residues. (embl.de)
Amino3
The results of the present research state that the effects of Ag were increased total free amino acids, glutathione, organic acids, proline, reducing sugars, thiol compounds, and cysteine, so the accumulation of these compounds was higher in metallicolous populations than non-metallicolous. (bvsalud.org)
containing a basic amino group, an acidic carboxyl group, and a side chain attached to an alpha carbon atom, and that link together by peptide bonds to form proteins, or that function as chemical messengers and as intermediates in metabolism. (nih.gov)
Cysteine -- A sulfur-containing nonessential amino acid produced by the enzymatic or acid hydrolysis of proteins. (nih.gov)
Role1
Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. (embl.de)
Highly1
Overall, CysQuant is a highly versatile tool for assessing the cysteine modification status that can be widely applied across various mass spectrometry platforms and organisms. (bvsalud.org)