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Journal articles on the topic 'Proteins thiol'

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Published: 9 March 2023
Last updated: 10 March 2023

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1

Skaff, Ojia, David I. Pattison, and Michael J. Davies. "Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance." Biochemical Journal 422, no. 1 (July 29, 2009): 111–17. http://dx.doi.org/10.1042/bj20090276.

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MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by H2O2 to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid, also know as cyanosulfenic acid) respectively. Specificity constants indicate that thiocyanate, SCN−, is a major substrate for MPO. HOSCN is also a major oxidant generated by other peroxidases including salivary, gastric and eosinophil peroxidases. Whereas HOCl and HOBr are powerful oxidizing agents, HOSCN appears to be a less reactive, but more thiol-specific oxidant. Although it is established that HOSCN selectively targets thiols, absolute kinetic data for the reactions of thiols with HOSCN are absent from the literature. This study shows for the first time that the reactions of HOSCN with low-molecular-mass thiol residues occur with rate constants in the range from 7.3×103 M−1·s−1 (for N-acetyl-cysteine at pH 7.4) to 7.7×106 M−1·s−1 (for 5-thio-2-nitrobenzoic acid at pH 6.0). An inverse relationship between the rate of reaction and the pKa of the thiol group was observed. The rates of reaction of HOSCN with thiol-containing proteins were also investigated for four proteins (creatine kinase, BSA, β-lactoglobulin and β-L-crystallins). The values obtained for cysteine residues on these proteins are in the range 1×104– 7×104 M−1·s−1. These second-order rate constants indicate that HOSCN is a major mediator of thiol oxidation in biological systems exposed to peroxidase/H2O2 systems at (patho)physiological concentrations of halide and SCN− ions, and that HOSCN may play an important role in inflammation-induced oxidative damage.
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2

Venkatraman, Aparna, Aimee Landar, Ashley J. Davis, Elena Ulasova, Grier Page, Michael P. Murphy, Victor Darley-Usmar, and Shannon M. Bailey. "Oxidative modification of hepatic mitochondria protein thiols: effect of chronic alcohol consumption." American Journal of Physiology-Gastrointestinal and Liver Physiology 286, no. 4 (April 2004): G521—G527. http://dx.doi.org/10.1152/ajpgi.00399.2003.

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Redox modification of mitochondrial proteins is thought to play a key role in regulating cellular function, although direct evidence to support this hypothesis is limited. Using an in vivo model of mitochondrial redox stress, ethanol hepatotoxicity, the modification of mitochondrial protein thiols was examined using a proteomics approach. Specific labeling of reduced thiols in the mitochondrion from the livers of control and ethanol-fed rats was achieved by using the thiol reactive compound (4-iodobutyl)triphenylphosphonium (IBTP). This molecule selectively accumulates in the organelle and can be used to identify thiol-containing proteins. Mitochondrial proteins that have been modified are identified by decreased labeling with IBTP using two-dimensional SDS-PAGE followed by immunoblotting with an antibody directed against the triphenylphosphonium moiety of the IBTP molecule. Analyses of these data showed a significant decrease in IBTP labeling of thiols present in specific mitochondria matrix proteins from ethanol-fed rats compared with their corresponding controls. These proteins were identified as the low- Km aldehyde dehydrogenase and glucose-regulated protein 78. The decrease in IBTP labeling in aldehyde dehydrogenase was accompanied by a decrease in specific activity of the enzyme. These data demonstrate that mitochondrial protein thiol modification is associated with chronic alcohol intake and might contribute to the pathophysiology associated with hepatic injury. Taken together, we have developed a protocol to chemically tag and select thiol-modified proteins that will greatly enhance efforts to establish posttranslational redox modification of mitochondrial protein in in vivo models of oxidative or nitrosative stress.
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3

Ferraro, Anna, Anna Giartosio, Margherita Eufemi, Donatella Barra, Fabio Altieri, and Carlo Turano. "Thiol proteins in chromatin." Bioscience Reports 6, no. 3 (March 1, 1986): 257–63. http://dx.doi.org/10.1007/bf01115154.

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Total half-cystine residues in proteins of pig liver chromatin have been measured. About half of them are present in the reduced state. Thiol groups of non-historic chromatin proteins, which amount to about 40 nmol/mg of protein, are preferentially located in chromatin fragments which are more easily solubilised either by DNAse I or by DNAse II. The data obtained are compatible with an involvement of SH and SS groups in chromatin structure and function.
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4

Turell, Lucia, Ari Zeida, and Madia Trujillo. "Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates." Essays in Biochemistry 64, no. 1 (January 10, 2020): 55–66. http://dx.doi.org/10.1042/ebc20190053.

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Abstract Thiol groups in protein cysteine (Cys) residues can undergo one- and two-electron oxidation reactions leading to the formation of thiyl radicals or sulfenic acids, respectively. In this mini-review we summarize the mechanisms and kinetics of the formation of these species by biologically relevant oxidants. Most of the latter react with the deprotonated form of the thiol. Since the pKa of the thiols in protein cysteines are usually close to physiological pH, the thermodynamics and the kinetics of their oxidation in vivo are affected by the acidity of the thiol. Moreover, the protein microenvironment has pronounced effects on cysteine residue reactivity, which in the case of the oxidation mediated by hydroperoxides, is known to confer specificity to particular protein cysteines. Despite their elusive nature, both thiyl radicals and sulfenic acids are involved in the catalytic mechanism of several enzymes and in the redox regulation of protein function and/or signaling pathways. They are usually short-lived species that undergo further reactions that converge in the formation of different stable products, resulting in several post-translational modifications of the protein. Some of these can be reversed through the action of specific cellular reduction systems. Others damage the proteins irreversibly, and can make them more prone to aggregation or degradation.
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5

Pöther, Dierk-Christoph, Manuel Liebeke, Falko Hochgräfe, Haike Antelmann, Dörte Becher, Michael Lalk, Ulrike Lindequist, et al. "Diamide Triggers Mainly S Thiolations in the Cytoplasmic Proteomes of Bacillus subtilis and Staphylococcus aureus." Journal of Bacteriology 191, no. 24 (October 16, 2009): 7520–30. http://dx.doi.org/10.1128/jb.00937-09.

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ABSTRACT Glutathione constitutes a key player in the thiol redox buffer in many organisms. However, the gram-positive bacteria Bacillus subtilis and Staphylococcus aureus lack this low-molecular-weight thiol. Recently, we identified S-cysteinylated proteins in B. subtilis after treatment of cells with the disulfide-generating electrophile diamide. S cysteinylation is thought to protect protein thiols against irreversible oxidation to sulfinic and sulfonic acids. Here we show that S thiolation occurs also in S. aureus proteins after exposure to diamide. We further analyzed the formation of inter- and intramolecular disulfide bonds in cytoplasmic proteins using diagonal nonreducing/reducing sodium dodecyl sulfate gel electrophoresis. However, only a few proteins were identified that form inter- or intramolecular disulfide bonds under control and diamide stress conditions in B. subtilis and S. aureus. Depletion of the cysteine pool was concomitantly measured in B. subtilis using a metabolomics approach. Thus, the majority of reversible thiol modifications that were previously detected by two-dimensional gel fluorescence-based thiol modification assay are most likely based on S thiolations. Finally, we found that a glutathione-producing B. subtilis strain which expresses the Listeria monocytogenes gshF gene did not show enhanced oxidative stress resistance compared to the wild type.
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6

Tong, Ka-Chung, Chun-Nam Lok, Pui-Ki Wan, Di Hu, Yi Man Eva Fung, Xiao-Yong Chang, Song Huang, Haibo Jiang, and Chi-Ming Che. "An anticancer gold(III)-activated porphyrin scaffold that covalently modifies protein cysteine thiols." Proceedings of the National Academy of Sciences 117, no. 3 (January 2, 2020): 1321–29. http://dx.doi.org/10.1073/pnas.1915202117.

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Cysteine thiols of many cancer-associated proteins are attractive targets of anticancer agents. Herein, we unequivocally demonstrate a distinct thiol-targeting property of gold(III) mesoporphyrin IX dimethyl ester (AuMesoIX) and its anticancer activities. While the binding of cysteine thiols with metal complexes usually occurs via M–S bond formation, AuMesoIX is unique in that the meso-carbon atom of the porphyrin ring is activated by the gold(III) ion to undergo nucleophilic aromatic substitution with thiols. AuMesoIX was shown to modify reactive cysteine residues and inhibit the activities of anticancer protein targets including thioredoxin, peroxiredoxin, and deubiquitinases. Treatment of cancer cells with AuMesoIX resulted in the formation of gold-bound sulfur-rich protein aggregates, oxidative stress-mediated cytotoxicity, and accumulation of ubiquitinated proteins. Importantly, AuMesoIX exhibited effective antitumor activity in mice. Our study has uncovered a gold(III)-induced ligand scaffold reactivity for thiol targeting that can be exploited for anticancer applications.
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7

Mu, Huiying, Koji Miki, Takuya Kubo, Koji Otsuka, and Kouichi Ohe. "Substituted meso-vinyl-BODIPY as thiol-selective fluorogenic probes for sensing unfolded proteins in the endoplasmic reticulum." Chemical Communications 57, no. 14 (2021): 1818–21. http://dx.doi.org/10.1039/d0cc08160d.

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Thiol-selective probes based on BODIPY scaffold were developed for sensing small-molecule thiols and unfolded proteins. The good organelle specificity of probe enables its utility for reporting the protein unfolding under ER stress in living cells.
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8

Deponte, Marcel, and Christopher Horst Lillig. "Enzymatic control of cysteinyl thiol switches in proteins." Biological Chemistry 396, no. 5 (May 1, 2015): 401–13. http://dx.doi.org/10.1515/hsz-2014-0280.

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Abstract The spatiotemporal modification of specific cysteinyl residues in proteins has emerged as a novel concept in signal transduction. Such modifications alter the redox state of the cysteinyl thiol group, with implications for the structure and biological function of the protein. Regulatory cysteines are therefore classified as ‘thiol switches’. In this review we emphasize the relevance of enzymes for specific and efficient redox sensing, evaluate prerequisites and general properties of redox switches, and highlight mechanistic principles for toggling thiol switches. Moreover, we provide an overview of potential mechanisms for the initial formation of regulatory disulfide bonds. In brief, we address the three basic questions (i) what defines a thiol switch, (ii) which parameters confer signal specificity, and (iii) how are thiol switches oxidized?
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9

Cabrillana, María Eugenia, María de los Ángeles Monclus, Tania Estefania Sáez Lancellotti, Paola Vanina Boarelli, Amanda Edith Vincenti, Miguel Matias Fornés, Eduardo Alfredo Sanabria, and Miguel Walter Fornés. "Thiols of flagellar proteins are essential for progressive motility in human spermatozoa." Reproduction, Fertility and Development 29, no. 7 (2017): 1435. http://dx.doi.org/10.1071/rd16225.

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Male infertility is a disorder of the reproductive system defined by the failure to achieve a clinical pregnancy after 12 months or more of regular unprotected sexual intercourse. The presence of low-motile or immotile spermatozoa is one of many causes of infertility; however, this observation provides little or no information regarding the pathogenesis of the malfunction. Good sperm motility depends on correct assembly of the sperm tail in the testis and efficient maturation during epididymal transit. Thiols of flagellar proteins, such as outer dense fibre protein 1 (ODF1), are oxidised to form disulfides during epididymal transit and the spermatozoa become motile. This study was designed to determine how oxidative changes in protein thiol status affect progressive motility in human spermatozoa. Monobromobimane (mBBr) was used as a specific thiol marker and disruptor of sperm progressive motility. When mBBr was blocked by dithiothreitol it did not promote motility changes. The analysis of mBBr-treated spermatozoa revealed a reduction of progressive motility and an increased number of spermatozoa with non-progressive motility without affecting ATP production. Laser confocal microscopy and western blot analysis showed that one of the mBBr-positive proteins reacted with an antibody to ODF1. Monobromobimane fluorescence intensity of the sperm tail was lower in normozoospermic than asthenozoospermic men, suggesting that thiol oxidation in spermatozoa of asthenozoospermic men is incomplete. Our findings indicate that mBBr affects the thiol status of ODF1 in human spermatozoa and interferes with progressive motility.
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10

Peng, An An, Jin Lan Xia, Hong Chang Liu, Wei Zhu, Rui Yong Zhang, Cheng Gui Zhang, and Zhen Yuan Nie. "Thiol-Rich Proteins Play Important Role in Adhesion and Sulfur Oxidation Process of Acidithiobacillus ferroxidans." Advanced Materials Research 825 (October 2013): 137–40. http://dx.doi.org/10.4028/www.scientific.net/amr.825.137.

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The proteomics of the extracellular proteins (EPs), outer membrane proteins (OMPs) and the periplasmic proteins (PPs) ofAcidithiobacillus ferrooxidansATCC 23270 grown on Fe2+and S0substrates, respectively, were comparatively studied. 39 expression up-regulated proteins (including 13 EPs, 9 OMPs and 17 PPs) were identified and 70% of them contain cysteine residues in sequence. Some of the selected proteins especially the EPs contain abundant of the cysteine residues and one or more-CXXC-functional motifs. The thiol groups on theAt. ferrooxidanscell surface were selectively marked by Ca2+and SR-μ-XRF mappingin situobservation revealed that the number of thiols on the surface of the cells grown on S0was about five times as that grown on Fe2+substrate. When 0.01 g/L surfactant Tween-80 was added in the S0culture medium, the adsorption and activation related EPs were down-regulated and the sulfur metabolism related proteins was up-regulated. The same phenomenon was observed when the cells were grown on the more easily adhesion sulfur allotrope μ-S. It indicates that the thiol-rich proteins played important roles in adhesion and sulfur oxidation process ofAt. ferrooxidans.
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11

White, Kylie, Gina Nicoletti, and Hugh Cornell. "Antibacterial Profile of a Microbicidal Agent Targeting Tyrosine Phosphatases and Redox Thiols, Novel Drug Targets." Antibiotics 10, no. 11 (October 27, 2021): 1310. http://dx.doi.org/10.3390/antibiotics10111310.

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The activity profile of a protein tyrosine phosphatase (PTP) inhibitor and redox thiol oxidant, nitropropenyl benzodioxole (NPBD), was investigated across a broad range of bacterial species. In vitro assays assessed inhibitory and lethal activity patterns, the induction of drug variants on long term exposure, the inhibitory interactions of NPBD with antibiotics, and the effect of plasma proteins and redox thiols on activity. A literature review indicates the complexity of PTP and redox signaling and suggests likely metabolic targets. NPBD was broadly bactericidal to pathogens of the skin, respiratory, urogenital and intestinal tracts. It was effective against antibiotic resistant strains and slowly replicating and dormant cells. NPBD did not induce resistant or drug-tolerant phenotypes and showed low cross reactivity with antibiotics in synergy assays. Binding to plasma proteins indicated lowered in-vitro bioavailability and reduction of bactericidal activity in the presence of thiols confirmed the contribution of thiol oxidation and oxidative stress to lethality. This report presents a broad evaluation of the antibacterial effect of PTP inhibition and redox thiol oxidation, illustrates the functional diversity of bacterial PTPs and redox thiols, and supports their consideration as novel targets for antimicrobial drug development. NPBD is a dual mechanism agent with an activity profile which supports consideration of tyrosine phosphatases and bacterial antioxidant systems as promising targets for drug development.
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12

Rogers, K. R., C. J. Morris, and D. R. Blake. "Oxidation of thiol in the vimentin cytoskeleton." Biochemical Journal 275, no. 3 (May 1, 1991): 789–91. http://dx.doi.org/10.1042/bj2750789.

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Sublethal doses of H2O2, which induces oxidative stress, cause substantial alteration to the vimentin cytoskeleton in various cell types. We have used a thiol-blot assay to assess thiol status in individual proteins from cell extracts. Vimentin thiol is oxidized in preference to other cytoskeleton proteins. Immunoblot analysis also demonstrated a loss of reactivity to an anti-vimentin monoclonal antibody under non-reducing conditions, possibly due to thiol-group oxidation. During induced oxidative stress a number of proteins become associated with the cytoskeleton extracts.
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13

Melchers, Johannes, Natalie Dirdjaja, Thomas Ruppert, and R. Luise Krauth-Siegel. "Glutathionylation of Trypanosomal Thiol Redox Proteins." Journal of Biological Chemistry 282, no. 12 (January 22, 2007): 8678–94. http://dx.doi.org/10.1074/jbc.m608140200.

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14

Loreto Palacio, Paola, José R. Godoy, Orhan Aktas, and Eva-Maria Hanschmann. "Changing Perspectives from Oxidative Stress to Redox Signaling—Extracellular Redox Control in Translational Medicine." Antioxidants 11, no. 6 (June 16, 2022): 1181. http://dx.doi.org/10.3390/antiox11061181.

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Extensive research has changed the understanding of oxidative stress that has been linked to every major disease. Today we distinguish oxidative eu- and distress, acknowledging that redox modifications are crucial for signal transduction in the form of specific thiol switches. Long underestimated, reactive species and redox proteins of the Thioredoxin (Trx) family are indeed essential for physiological processes. Moreover, extracellular redox proteins, low molecular weight thiols and thiol switches affect signal transduction and cell–cell communication. Here, we highlight the impact of extracellular redox regulation for health, intermediate pathophenotypes and disease. Of note, recent advances allow the analysis of redox changes in body fluids without using invasive and expensive techniques. With this new knowledge in redox biochemistry, translational strategies can lead to innovative new preventive and diagnostic tools and treatments in life sciences and medicine.
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15

Skalska, Jolanta, Paul S. Brookes, S. M. Nadtochy, Shannon Hilchey, Craig T. Jordan, Monica L. Guzman, Sanjay Maggirwar, Margaret M. Briehl, and Steven H. Bernstein. "Modulation of Cell Surface Protein Free Thiols; A Potential Novel Mechanism of Action of the Sesquiterpene Lactone Parthenolide in Non-Hodgkin's Lymphoma." Blood 114, no. 22 (November 20, 2009): 3774. http://dx.doi.org/10.1182/blood.v114.22.3774.3774.

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Abstract Abstract 3774 Poster Board III-710 Recent data supports the concept that redox regulation of cell surface protein thiols (i.e., exofacial thiols) effects critical cellular functions. We therefore hypothesized that redox-active anti-cancer therapeutics would modulate exofacial thiols, and that such modulation could be related to cell death mechanisms. To test this hypothesis, we used the sesquiterpene lactone parthenolide, a known anti-cancer agent. Parthenolide treatment results in a dose dependent decrease in mantle cell (MCL) and diffuse large cell lymphoma cell viability. Indeed, parthenolide decreases the level of free (ie. reduced) exofacial thiols on Granta MCL cells as assessed by flow cytometry. Parthenolide specifically modifies free thiols of surface proteins having molecular weights of ∼12 kd and ∼22 kd, as determined using a biotinylated thiol reactive reagent N-(biotinoyl)-N-(iodoacetyl) ethylendiamine (BIAM), which binds to free thiol groups and is detected by streptavidin-peroxidase staining of western blots. We further show that the central redox regulator thioredoxin is one of the surface protein thiol targets modified by parthenolide; specifically; (a) thioredoxin is detected on the Granta cell surface; (b) parthenolide directly interacts with free thiol groups on purified human thioredoxin, and; (c) parthenolide directly modifies Granta membrane associated thioredoxin, as determined with BIAM and neutravidin pull-down. To examine the functional consequences of parthenolide induced surface protein thiol modification, Granta cells were pretreated with the cell impermeable thiol antioxidant glutathione (GSH). Pretreatment with GSH inhibits the parthenolide induced; (a) decrease in exofacial free thiols; (b) modification of surface thioredoxin and; (c) Granta cell death. Pretreatment of Granta cells with GSH also inhibits parthenolide-mediated activation of JNK and inhibition of NFkB, two activities previously associated with the drug's anti-cancer activity. Based on these data, we postulate that at least one component of parthenolide's anti-lymphoma activity derives from its ability to modify the redox state of critical exofacial thiols. Indeed, to our knowledge, our data is the first to suggest that cancer cell exofacial thiols may be novel and important targets for cancer therapy. Supported by an NCI SPORE grant in lymphoma 1P50 CA130805. Disclosures: Bernstein: millenium: Consultancy; genentech: Consultancy, Speakers Bureau; enzon: Consultancy.
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16

Ganderton, Tim, Colin N. Chesterman, Michael C. Berndt, and Philip Hogg. "Evidence for Control of von Willebrand Factor Multimer Size by Intramolecular Thiol-Disulfide Exchange." Blood 106, no. 11 (November 16, 2005): 412. http://dx.doi.org/10.1182/blood.v106.11.412.412.

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Abstract Plasma von Willebrand factor (VWF) is a multimeric glycoprotein from endothelial cells and platelets that mediates adhesion of platelets to sites of vascular injury. In the shear force of flowing blood, however, only the very large VWF multimers are effective in capturing platelets. The multimeric size of VWF is controlled by proteolysis at the Tyr842-Met843 peptide bond by ADAMTS13. It is apparent, however, that VWF multimers are processed to a significant degree in the absence of ADAMTS13 in mice and humans. This finding implies that another mechanism of controlling VWF multimer size must exist. We noticed similarities between the structural control of α-keratin and VWF. Both are multimeric elongated proteins whose substrates are linked by disulfide-bonds and both proteins undergo shear-dependent conformational change. Keratin shape is controlled by thiol-mediated events and we have shown that the free thiol of thrombospondin-1 can facilitate cleavage of the disulfide-bonds that hold VWF multimers together. The structure of α-keratin is controlled by shear-dependent intramolecular thiol-disulfide exchange. Free thiols in keratin from unpaired cysteines exchange with nearby disulfides when the α-keratin fibre is exposed to shear. The thiol-disulfide exchange process continues until the shear across the fibre is resolved. We hypothesized that a similar mechanism may be operating in VWF. Intramolecular thiol-disulfide exchange is dependent on the presence of at least one unpaired cysteine thiol in the protein. Using a biotin-linked maleimde that specifically alkylates free thiols, we have shown that plasma VWF does contain unpaired cysteine residues. VWF was coated onto the interior of glass capillary tubes and exposed to shear using a precision syringe pump. VWF eluted from the tube when shear was stepped, but not when the shear was constant, and the eluted VWF was of smaller multimer size than that bound to the tube. These observations imply that VWF multimer size can be controlled by intramolecular thiol-disulfide exchange. We suggest that this mechanism may be responsible for the processing of VWF multimer size observed in the absence of ADAMTS13.
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17

Saluk-Juszczak, Joanna, Beata Olas, Paweł Nowak, Barbara Wachowicz, Edward Bald, Rafał Głowacki, Izabela Pawlaczyk, and Roman Gancarz. "Extract from Conyza canadensis as a modulator of plasma protein oxidation induced by peroxynitrite in vitro." Open Life Sciences 5, no. 6 (December 1, 2010): 800–807. http://dx.doi.org/10.2478/s11535-010-0065-6.

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AbstractThe antioxidative activity of the extract from Conyza canadensis in plasma treated with peroxynitrite (ONOO−) (0.1 mM) was studied. C. canadensis is known to possess a broad set of pharmacological effects because of content of various antioxidants, antiplatelet and anticoagulant compounds. The aim of our study was to assess if this extract protects plasma proteins against oxidative/nitrative damages induced by ONOO−. The plasma components are continuously exposed to reactive oxygen/nitrogen species action. Peroxynitrite evokes oxidative stress and induces undesirable effects in biological systems and causes damage to biomolecules. The extract from Conyza (50–2500 mg/ml) caused a dose-dependent reduction of protein nitration by 90%. The oxidation of plasma proteins was diminished by about 75%. ONOO− oxidized the plasma thiol groups and this process was inhibited by tested extract. The level of reduced protein thiols was increased thrice at the lowest concentration of extract (50 mg/ml). The highest concentration of extract decreased twice the level of protein thiols in reduced forms and increased the homocysteine level about 4.5 times. The obtained results demonstrated that the extract from Conyza possesses antioxidative properties in vitro, protects plasma proteins against toxicity induced by peroxynitrite and has modulating effects on thiol/disulfide redox status.
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18

Chouchani, Edward T., Thomas R. Hurd, Sergiy M. Nadtochiy, Paul S. Brookes, Ian M. Fearnley, Kathryn S. Lilley, Robin A. J. Smith, and Michael P. Murphy. "Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation." Biochemical Journal 430, no. 1 (July 28, 2010): 49–59. http://dx.doi.org/10.1042/bj20100633.

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The S-nitrosation of mitochondrial proteins as a consequence of NO metabolism is of physiological and pathological significance. We previously developed a MitoSNO (mitochondria-targeted S-nitrosothiol) that selectively S-nitrosates mitochondrial proteins. To identify these S-nitrosated proteins, here we have developed a selective proteomic methodology, SNO-DIGE (S-nitrosothiol difference in gel electrophoresis). Protein thiols in control and MitoSNO-treated samples were blocked, then incubated with copper(II) and ascorbate to selectively reduce S-nitrosothiols. The samples were then treated with thiol-reactive Cy3 (indocarbocyanine) or Cy5 (indodicarbocyanine) fluorescent tags, mixed together and individual protein spots were resolved by 2D (two-dimensional) gel electrophoresis. Fluorescent scanning of these gels revealed S-nitrosated proteins by an increase in Cy5 red fluorescence, allowing for their identification by MS. Parallel analysis by Redox-DIGE enabled us to distinguish S-nitrosated thiol proteins from those which became oxidized due to NO metabolism. We identified 13 S-nitrosated mitochondrial proteins, and a further four that were oxidized, probably due to evanescent S-nitrosation relaxing to a reversible thiol modification. We investigated the consequences of S-nitrosation for three of the enzymes identified using SNO-DIGE (aconitase, mitochondrial aldehyde dehydrogenase and α-ketoglutarate dehydrogenase) and found that their activity was selectively and reversibly inhibited by S-nitrosation. We conclude that the reversible regulation of enzyme activity by S-nitrosation modifies enzymes central to mitochondrial metabolism, whereas identification and functional characterization of these novel targets provides mechanistic insight into the potential physiological and pathological roles played by this modification. More generally, the development of SNO-DIGE facilitates robust investigation of protein S-nitrosation across the proteome.
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19

Parasassi, Tiziana, Roberto Brunelli, Graziella Costa, Marco De Spirito, Ewa Krasnowska, Thomas Lundeberg, Eugenia Pittaluga, and Fulvio Ursini. "Thiol Redox Transitions in Cell Signaling: a Lesson from N-Acetylcysteine." Scientific World JOURNAL 10 (2010): 1192–202. http://dx.doi.org/10.1100/tsw.2010.104.

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The functional status of cells is under the control of external stimuli affecting the function of critical proteins and eventually gene expression. Signal sensing and transduction by messengers to specific effectors operate by post-translational modification of proteins, among which thiol redox switches play a fundamental role that is just beginning to be understood. The maintenance of the redox status is, indeed, crucial for cellular homeostasis and its dysregulation towards a more oxidized intracellular environment is associated with aberrant proliferation, ultimately related to diseases such as cancer, cardiovascular disease, and diabetes. Redox transitions occur in sensitive cysteine residues of regulatory proteins relevant to signaling, their evolution to metastable disulfides accounting for the functional redox switch. N-acetylcysteine (NAC) is a thiol-containing compound that is able to interfere with redox transitions of thiols and, thus, in principle, able to modulate redox signaling. We here review the redox chemistry of NAC, then screen possible mechanisms to explain the effects observed in NAC-treated normal and cancer cells; such effects involve a modification of global gene expression, thus of functions and morphology, with a leitmotif of a switch from proliferation to terminal differentiation. The regulation of thiol redox transitions in cell signaling is, therefore, proposed as a new tool, holding promise not only for a deeper explanation of mechanisms, but indeed for innovative pharmacological interventions.
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20

Flaumenhaft, Robert, and Bruce Furie. "Vascular thiol isomerases." Blood 128, no. 7 (August 18, 2016): 893–901. http://dx.doi.org/10.1182/blood-2016-04-636456.

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Abstract Thiol isomerases are multifunctional enzymes that influence protein structure via their oxidoreductase, isomerase, and chaperone activities. These enzymes localize at high concentrations in the endoplasmic reticulum of all eukaryotic cells where they serve an essential function in folding nascent proteins. However, thiol isomerases can escape endoplasmic retention and be secreted and localized on plasma membranes. Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secreted by and localize to the membranes of platelets and endothelial cells. These vascular thiol isomerases are released following vessel injury and participate in thrombus formation. Although most of the activities of vascular thiol isomerases that contribute to thrombus formation are yet to be defined at the molecular level, allosteric disulfide bonds that are modified by thiol isomerases have been described in substrates such as αIIbβ3, αvβ3, GPIbα, tissue factor, and thrombospondin. Vascular thiol isomerases also act as redox sensors. They respond to the local redox environment and influence S-nitrosylation of surface proteins on platelets and endothelial cells. Despite our rudimentary understanding of the mechanisms by which thiol isomerases control vascular function, the clinical utility of targeting them in thrombotic disorders is already being explored in clinical trials.
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Antalík, Marián, Ernest Šturdík, Dušan Podhradský, Ingrid Poleková, and Ľudovít Drobnica. "Kinetics analysis of the decay of phenylhydrazonopropanedinitrile addition products with thiols in aqueous solutions." Collection of Czechoslovak Chemical Communications 54, no. 12 (1989): 3387–96. http://dx.doi.org/10.1135/cccc19893387.

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The reactions of phenylhydrazonopropanedinitriles with thiols are reversible and with increasing pH-values of aqueous solutions the equilibrium is shifted them to the side of the reactants. A mechanism of the decay of corresponding addition products was proposed and the kinetic description based on this mechanism is in good agreement with the obtained experimental data. From the viewpoint of the decay, the pH-dependent dissociation of the proton of the imino group formed by addition of thiol to the nitrile carbon atom plays a decisive role. The obtained knowledge is useful with respect to the use of phenylhydrazonopropanedinitriles as affinants for selective and reversible sorption of low-molecular thiols and thiol-proteins in affinity chromatography as well as for the study of the mechanism of the effect of these substances in oxidative and photosynthetic phosphorylation and biological systems in general.
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22

Urbainsky, Claudia, Rolf Nölker, Marcel Imber, Adrian Lübken, Jörg Mostertz, Falko Hochgräfe, José R. Godoy, Eva-Maria Hanschmann, and Christopher Horst Lillig. "Nucleoredoxin-Dependent Targets and Processes in Neuronal Cells." Oxidative Medicine and Cellular Longevity 2018 (November 21, 2018): 1–11. http://dx.doi.org/10.1155/2018/4829872.

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Nucleoredoxin (Nrx) is an oxidoreductase of the thioredoxin family of proteins. It was shown to act as a signal transducer in some pathways; however, so far, no comprehensive analysis of its regulated substrates and functions was available. Here, we used a combination of two different strategies to fill this gap. First, we analyzed the thiol-redox state of the proteome of SH-SY5Y neuroblastoma cells depleted of Nrx compared to control cells using a differential thiol-labeling technique and quantitative mass spectrometry. 171 proteins were identified with an altered redox state; 161 of these were more reduced in the absence of Nrx. This suggests functions of Nrx in the oxidation of protein thiols. Second, we utilized the active site mutant Cys208Ser of Nrx, which stabilizes a mixed disulfide intermediate with its substrates and therefore trapped interacting proteins from the mouse brain (identifying 1710 proteins) and neuronal cell culture extracts (identifying 609 proteins). Profiling of the affected biological processes and molecular functions in cells of neuronal origin suggests numerous functions of Nrx in the redox regulation of metabolic pathways, cellular morphology, and signal transduction. These results characterize Nrx as a cellular oxidase that itself may be oxidized by the formation of disulfide relays with peroxiredoxins.
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23

Srinivas, Vanishree, and Shubha Gopal. "LmTDRM Database: A Comprehensive Database on Thiol Metabolic Gene/Gene Products in Listeria monocytogenes EGDe." Journal of Integrative Bioinformatics 11, no. 1 (March 1, 2014): 17–29. http://dx.doi.org/10.1515/jib-2014-245.

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Summary There are a number of databases on the Listeria species and about their genome. However, these databases do not specifically address a set of network that is important in defence mechanism of the bacteria. Listeria monocytogenes EGDe is a well-established intracellular model organism to study host pathogenicity because of its versatility in the host environment. Here, we have focused on thiol disulphide redox metabolic network proteins, specifically in L. monocytogenes EGDe. The thiol redox metabolism is involved in oxidative stress mechanism and is found in all living cells. It functions to maintain the thiol disulphide balance required for protein folding by providing reducing power. Nevertheless, they are involved in the reversible oxidation of thiol groups in biomolecules by creating disulphide bonds; therefore, the term thiol disulphide redox metabolism (TDRM). TDRM network genes play an important role in oxidative stress mechanism and during host-pathogen interaction. Therefore, it is essential to have detailed information on these proteins with regard to other bacteria and its genome analysis to understand the presence of tRNA, transposons, and insertion elements for horizontal gene transfer. LmTDRM database is a new comprehensive web-based database on thiol proteins and their functions. It includes: Description, Search, TDRM analysis, and genome viewer. The quality of these data has been evaluated before they were aggregated to produce a final representation. The web interface allows for various queries to understand the protein function and their annotation with respect to their relationship with other bacteria. LmTDRM is a major step towards the development of databases on thiol disulphide redox proteins; it would definitely help researchers to understand the mechanism of these proteins and their interaction. Database URL: www.lmtdrm.com
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24

Marley, Kevin, Duane T. Mooney, Gretchen Clark-Scannell, Tony T. H. Tong, Jeffrey Watson, Tory M. Hagen, Jan F. Stevens, and Claudia S. Maier. "Mass Tagging Approach for Mitochondrial Thiol Proteins." Journal of Proteome Research 4, no. 4 (August 2005): 1403–12. http://dx.doi.org/10.1021/pr050078k.

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25

Brandes, Nicolas, Sebastian Schmitt, and Ursula Jakob. "Thiol-Based Redox Switches in Eukaryotic Proteins." Antioxidants & Redox Signaling 11, no. 5 (May 2009): 997–1014. http://dx.doi.org/10.1089/ars.2008.2285.

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26

Houen, G., and Ib Svendsen. "Affinity chromatography of thiol ester-containing proteins." Journal of Chromatography A 799, no. 1-2 (March 1998): 139–48. http://dx.doi.org/10.1016/s0021-9673(97)01064-9.

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27

Stipanuk, Martha H., Chad R. Simmons, P. Andrew Karplus, and John E. Dominy. "Thiol dioxygenases: unique families of cupin proteins." Amino Acids 41, no. 1 (March 1, 2010): 91–102. http://dx.doi.org/10.1007/s00726-010-0518-2.

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28

Dias, G. M., M. L. López, A. T. S. Ferreira, D. A. Chapeaurouge, A. Rodrigues, J. Perales, and C. A. Retamal. "Thiol-disulfide proteins of stallion epididymal spermatozoa." Animal Reproduction Science 145, no. 1-2 (February 2014): 29–39. http://dx.doi.org/10.1016/j.anireprosci.2013.12.007.

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29

Seligman, J., N. S. Kosower, R. Weissenberg, and R. Shalgi. "Thiol-disulfide status of human sperm proteins." Reproduction 101, no. 2 (July 1, 1994): 435–43. http://dx.doi.org/10.1530/jrf.0.1010435.

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30

Kumar, K. S. Ajish, and Ashraf Brik. "Accessing posttranslationally modified proteins through thiol positioning." Journal of Peptide Science 16, no. 10 (September 16, 2010): 524–29. http://dx.doi.org/10.1002/psc.1229.

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31

Razygraev, A. V., K. I. Taborskaya, M. A. Petrosyan, and Zh N. Tumasova. "Thiol peroxidase activities in rat blood plasma determined with hydrogen peroxide and 5,5`-dithio-bis(2-nitrobenzoic acid)." Biomeditsinskaya Khimiya 62, no. 4 (2016): 431–38. http://dx.doi.org/10.18097/pbmc20166204431.

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Earlier it has been shown that extracellular glutathione peroxidase (GPx3) from human plasma is able to use cysteine (Cys-SH) instead of glutathione (GSH) as a thiol substrate. In the present study, the ability of rat plasma to utilize not only GSH, but also Cys-SH and homocysteine (Hcy-SH), in the thiol peroxidase reaction has been confirmed. The molar ratio between thiol and H2O2 in the catalyzed reaction was 2:1. The specific activity increased with fractionation of proteins. At a fixed thiol concentration of 0.23 mM, the saturation by H2O2 with vmax app of 100, 128, and 132 nmol H2O2 / s per 1 ml of plasma was found for DL-Cys-SH, L-GSH, and DL-Hcy-SH, respectively. Rank distributions of activities towards all three thiol substrates within plasma protein fractions are fully identical (the probability of random full coincidence was less than 0.01). The statistical analysis confirms that Cys-SH peroxidase, Hcy-SH peroxidase, and GSH peroxidase activities are closely associated with each other. The most probable outcome of this result is the ability of rat GPx3 to utilize all three thiols as substrates for oxidation. Probably, thiol peroxidase is a participant of formation of plasma cystine (Cys-SS-Cys) from Cys-SH in plasma. If the forms of Hcy exhibit different toxic effects, it can be suggested that thiol peroxidase regulates Hcy toxicity in hyperhomocysteinemia through Hcy-SH oxidation to homocystine (Hcy-SS-Hcy).
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32

Radzinski, Meytal, Tal Oppenheim, Norman Metanis, and Dana Reichmann. "The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins." Biomolecules 11, no. 3 (March 22, 2021): 469. http://dx.doi.org/10.3390/biom11030469.

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Protein homeostasis is an essential component of proper cellular function; however, sustaining protein health is a challenging task, especially during the aerobic lifestyle. Natural cellular oxidants may be involved in cell signaling and antibacterial defense; however, imbalanced levels can lead to protein misfolding, cell damage, and death. This merges together the processes of protein homeostasis and redox regulation. At the heart of this process are redox-regulated proteins or thiol-based switches, which carefully mediate various steps of protein homeostasis across folding, localization, quality control, and degradation pathways. In this review, we discuss the “redox code” of the proteostasis network, which shapes protein health during cell growth and aging. We describe the sources and types of thiol modifications and elaborate on diverse strategies of evolving antioxidant proteins in proteostasis networks during oxidative stress conditions. We also highlight the involvement of cysteines in protein degradation across varying levels, showcasing the importance of cysteine thiols in proteostasis at large. The individual examples and mechanisms raised open the door for extensive future research exploring the interplay between the redox and protein homeostasis systems. Understanding this interplay will enable us to re-write the redox code of cells and use it for biotechnological and therapeutic purposes.
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33

Armstrong, P. B., and J. P. Quigley. "Limulus α2-macroglobulin. First evidence in an invertebrate for a protein containing an internal thiol ester bond." Biochemical Journal 248, no. 3 (December 15, 1987): 703–7. http://dx.doi.org/10.1042/bj2480703.

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Intra-chain thiol ester bonds are present in a limited number of proteins. The thiol ester class of proteins includes vertebrate alpha 2-macroglobulin and the complement proteins C3 and C4. We report here the first instance of a thiol ester protein from an invertebrate, the alpha 2-macroglobulin proteinase-inhibitor homologue present in the plasma of the American horseshoe crab Limulus polyphemus. Our evidence is of three kinds: (1) the proteinase-binding activity of Limulus alpha 2-macroglobulin is inactivated by the low-molecular-mass primary amine methylamine; (2) the native protein is subject to autolytic fragmentation during mild thermal denaturation, yielding fragments of approx. 125 kDa and 55 kDa, whereas the methylamine-treated protein is stable under these conditions of thermal treatment; (3) new thiol groups are generated rapidly during reaction of the protein with trypsin. The demonstration of the thiol ester bond in a protein from an ancient invertebrate provides evolutionary evidence for the importance of this bond in the function of plasma forms of the alpha 2-macroglobulin-like proteinase inhibitors.
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34

WAN, Feng-Yi, Yi-Nan WANG, and Guo-Jiang ZHANG. "The influence of oxidation of membrane thiol groups on lysosomal proton permeability." Biochemical Journal 360, no. 2 (November 26, 2001): 355–62. http://dx.doi.org/10.1042/bj3600355.

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The influence of oxidation of membrane thiol groups on lysosomal proton permeability was studied by measuring lysosomal pH with FITC-conjugated dextran, determining the membrane potential with 3,3′-dipropylthiadicarbocyanine iodide and monitoring their proton leakage with p-nitrophenol. Residual membrane thiol groups were measured with 5,5′-dithiobis-(2-nitrobenzoic acid). The lysosomal membrane thiol groups were modified by treatment with diamide and dithiothreitol. SDS/PAGE revealed aggregations of the membrane proteins induced by the treatment of lysosomes with diamide. The cross-linkage of proteins could be abolished by subsequent treatment with dithiothreitol, indicating that the proteins were linked via disulphide bonds. Treating the lysosomes with diamide decreased their membrane thiol groups and caused increases in lysosomal pH, membrane potential and proton leakage, which could be reversed by treatment of the lysosomes with dithiothreitol. This indicates that the lysosomal proton permeability can be increased by oxidation of the membrane thiol groups and restored to the normal level by reduction of the groups. Treatment of the lysosomes with N-ethylmaleimide reduced their membrane thiol groups but did not change the lysosomal pH or their degree of proton leakage. It suggests that protein aggregation may be an important mechanism for the increase in lysosomal proton permeability. The results raise the possibility that the proton permeability of lysosomes in vivo may be affected by the redox states of their membrane thiol groups.
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35

Dietz, Karl-Josef, and Rüdiger Hell. "Thiol switches in redox regulation of chloroplasts: balancing redox state, metabolism and oxidative stress." Biological Chemistry 396, no. 5 (May 1, 2015): 483–94. http://dx.doi.org/10.1515/hsz-2014-0281.

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Abstract In photosynthesizing chloroplasts, rapidly changing energy input, intermediate generation of strong reductants as well as oxidants and multiple participating physicochemical processes and pathways, call for efficient regulation. Coupling redox information to protein function via thiol modifications offers a powerful mechanism to activate, down-regulate and coordinate interdependent processes. Efficient thiol switching of target proteins involves the thiol-disulfide redox regulatory network, which is highly elaborated in chloroplasts. This review addresses the features of this network. Its conditional function depends on specificity of reduction and oxidation reactions and pathways, thiol redox buffering, but also formation of heterogeneous milieus by microdomains, metabolite gradients and macromolecular assemblies. One major player is glutathione. Its synthesis and function is under feedback redox control. The number of thiol-controlled processes and involved thiol switched proteins is steadily increasing, e.g., in tetrapyrrole biosynthesis, plastid transcription and plastid translation. Thus chloroplasts utilize an intricate and versatile redox regulatory network for intraorganellar and retrograde communication.
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36

Strandin, Tomas, Jussi Hepojoki, Hao Wang, Antti Vaheri, and Hilkka Lankinen. "Inactivation of hantaviruses by N-ethylmaleimide preserves virion integrity." Journal of General Virology 92, no. 5 (May 1, 2011): 1189–98. http://dx.doi.org/10.1099/vir.0.027896-0.

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Thiol groups of cysteine residues are crucial for the infectivity of various enveloped viruses, but their role in the infectivity of viruses of the family Bunyaviridae has thus far not been studied. This report shows that thiol groups are essential to the infectivity of hantaviruses. Alkylation of the thiol functional groups using the membrane-permeable compound N-ethylmaleimide (NEM) and membrane-impermeable compound 5,5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) showed NEM to be a highly effective inactivator of Puumala and Tula hantaviruses. The NEM-inactivated hantavirus maintained the buoyant density of the wild-type virus. Furthermore, the antigenicity of glycoproteins and the cell attachment capacity of virions were retained at NEM concentrations that totally abolished virus infectivity. These results signified preservation of virion integrity following inactivation with NEM, making chemically inactivated virions valuable research antigens. It was demonstrated with biotin-conjugated maleimide, a mechanistic analogue of NEM, that all the structural proteins of hantavirus were sensitive towards thiol alkylation. In contrast to hantaviruses, NEM did not abolish Uukuniemi phlebovirus infectivity to the same extent. This indicates differences in the use of free thiols in virus entry among members of the family Bunyaviridae.
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37

Qiang, Wenan, Jodi M. Cahill, Jinrong Liu, Xianghong Kuang, Na Liu, Virginia L. Scofield, Jennifer R. Voorhees, et al. "Activation of Transcription Factor Nrf-2 and Its Downstream Targets in Response to Moloney Murine Leukemia Virus ts1-Induced Thiol Depletion and Oxidative Stress in Astrocytes." Journal of Virology 78, no. 21 (November 1, 2004): 11926–38. http://dx.doi.org/10.1128/jvi.78.21.11926-11938.2004.

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ABSTRACT The neuroimmunodegenerative syndrome that develops in mice infected with ts1, a mutant of Moloney murine leukemia virus, resembles human AIDS. Both ts1 and human immunodeficiency virus type 1 infect astrocytes, microglia, and oligodendrocytes but do not infect neurons. Oxidative stress has been implicated in the neuropathology of AIDS dementia and other neurodegenerative diseases. We report here that ts1 infection of astrocytes (both transformed C1 cells and primary cultures) also induces thiol (i.e., glutathione and cysteine) depletion and reactive oxygen species (ROS) accumulation, events occurring in parallel with viral envelope precursor gPr80 env accumulation and upregulated expression of endoplasmic reticulum chaperones GRP78 and GRP94. Furthermore, ts1-infected astrocytes mobilize their thiol redox defenses by upregulating levels of the Nrf-2 transcription factor, as well its targets, the xCT cystine/glutamate antiporter, γ-glutamylcysteine ligase, and glutathione peroxidase. Depleting intracellular thiols by treating uninfected astrocytes with buthionine sulfoximine (BSO), a glutathione synthesis inhibitor, or by culturing in cystine-deficient medium, also induces ROS accumulation, activates Nrf-2, and upregulates Nrf-2 target gene expression in these astrocytes. Overexpression of Nrf-2 in astrocytes specifically increases expression of the above thiol synthesis-related proteins. Further treatment with BSO or N-acetylcysteine in transfected cells modulates this expression. Thiol depletion also accelerates cell death, while thiol supplementation promotes survival of ts1-infected cells. Together, our results indicate that ts1 infection of astrocytes, along with ts1-induced gPr80 env accumulation, endoplasmic reticulum stress, thiol depletion, and oxidative stress, accelerates cell death; in response to the thiol depletion and oxidative stress, astrocytes activate their Nrf-2-mediated thiol antioxidant defenses, promoting cell survival.
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38

Lee, Duk-Shin, and Ji-Eun Kim. "PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A–PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation." International Journal of Molecular Sciences 21, no. 6 (March 18, 2020): 2094. http://dx.doi.org/10.3390/ijms21062094.

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Postsynaptic density-95 (PSD95), a major scaffolding protein, is critical in coupling N-methyl-D-aspartate receptor (NMDAR) to cellular signaling networks in the central nervous system. A couple of cysteine residues in the N-terminus of PSD95 are potential sites for disulfide bonding, S-nitrosylation and/or palmitoylation. Protein disulfide isomerase (PDI) reduces disulfide bonds (S-S) to free thiol (-SH) on various proteins. However, the involvement of PDI in disulfide bond formation/S-nitrosylation of PSD95 and its role in epilepsy are still unknown. In the present study, acute seizure activity significantly increased the bindings of PDI to NR2A, but not to PSD95, while it decreased the NR2A–PSD95 binding. In addition, pilocarpine-induced seizures increased the amount of nitrosylated (SNO-) thiols, not total (free and SNO-) thiols, on PSD95. Unlike acute seizure, spontaneous seizing rats showed the increases in PDI–PSD95 binding, total- and SNO-thiol levels on PSD95, and NR2A–PSD95 interaction. PDI siRNA effectively reduced spontaneous seizure activity with decreases in total thiol level on PSD95 and NR2A–PSD95 association. These findings indicate that PDI-mediated reduction of disulfide-bond formations may facilitate the NR2A–PSD95 binding and contribute to spontaneous seizure generation in epileptic animals.
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39

Klotz. "FOXO Transcription Factors: Regulators of Metabolism and Stress Resistance." Proceedings 11, no. 1 (April 16, 2019): 11. http://dx.doi.org/10.3390/proceedings2019011011.

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FOXO (Forkhead box, class O) proteins are transcriptional regulators ubiquitously expressed in mammalian cells with roles in modulating fuel metabolism, stress resistance and cell death. FOXO transcription factors are regulated by redox processes at several levels, including enzymatic and nonenzymatic posttranslational modification. Target genes controlled by FOXO proteins include genes encoding antioxidant proteins, thus likely contributing to the key role FOXOs play in the cellular response to oxidative stress. Here, an overview is provided on (i) the modulation of FOXO proteins by thiol depleting agents, (ii) consequences of thiol depletion for stress resistance and life span of a model organism, Caenorhabditis elegans and (iii) the role of FOXO proteins therein.
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40

Arumugam, Selvanathan, Sara V. Orski, Ngalle Eric Mbua, Christopher McNitt, Geert-Jan Boons, Jason Locklin, and Vladimir V. Popik. "Photo-click chemistry strategies for spatiotemporal control of metal-free ligation, labeling, and surface derivatization." Pure and Applied Chemistry 85, no. 7 (May 23, 2013): 1499–513. http://dx.doi.org/10.1351/pac-con-13-01-08.

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Three photo-click ligation strategies described in this account provide scientists with efficient and selective tools for derivatization of various molecules, polymers, and surfaces. Fast photochemical reactions that are utilized in these techniques permit spatiotemporal control of the process. The absence of activating reagents and catalysts, as well as compatibility with aqueous media, makes photo-click ligations suitable for biomedical applications. The first of these approaches relies on the photochemical decarbonylation of cyclopropenones to produce cyclooctynes. The latter undergo rapid catalyst-free strain-promoted azide–alkyne cycloaddition (SPAAC) to azide-tagged substrates. The second method is based on a very fast (>104 M–1 s–1) light-triggered hetero-Diels–Alder reaction and permits efficient derivatization of substrates bearing vinyl ether moiety. An even faster reaction between photochemically generated naphthoquinone methides (oNQMs) and thiols (~2 × 105 M–1 s–1) serves as a basis for a third method. This thiol photo-click chemistry allows for the selective derivatization of thiol-functionalized substrates or labeling of free cysteine residues in proteins. The thioether linkage produced by the reaction of oNQMs and a thiol is stable under ambient conditions, but can be cleaved by UV irradiation, regenerating free thiol. This feature permits the removal or replacement of immobilized compounds, as well as traceless substrate release.
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41

Oliveira, Percíllia V. S., and Francisco R. M. Laurindo. "Implications of plasma thiol redox in disease." Clinical Science 132, no. 12 (June 29, 2018): 1257–80. http://dx.doi.org/10.1042/cs20180157.

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Thiol groups are crucially involved in signaling/homeostasis through oxidation, reduction, and disulphide exchange. The overall thiol pool is the resultant of several individual pools of small compounds (e.g. cysteine), peptides (e.g. glutathione), and thiol proteins (e.g. thioredoxin (Trx)), which are not in equilibrium and present specific oxidized/reduced ratios. This review addresses mechanisms and implications of circulating plasma thiol/disulphide redox pools, which are involved in several physiologic processes and explored as disease biomarkers. Thiol pools are regulated by mechanisms linked to their intrinsic reactivity against oxidants, concentration of antioxidants, thiol-disulphide exchange rates, and their dynamic release/removal from plasma. Major thiol couples determining plasma redox potential (Eh) are reduced cysteine (CyS)/cystine (the disulphide form of cysteine) (CySS), followed by GSH/disulphide-oxidized glutathione (GSSG). Hydrogen peroxide and hypohalous acids are the main plasma oxidants, while water-soluble and lipid-soluble small molecules are the main antioxidants. The thiol proteome and thiol-oxidoreductases are emerging investigative areas given their specific disease-related responses (e.g. protein disulphide isomerases (PDIs) in thrombosis). Plasma cysteine and glutathione redox couples exhibit pro-oxidant changes directly correlated with ageing/age-related diseases. We further discuss changes in thiol-disulphide redox state in specific groups of diseases: cardiovascular, cancer, and neurodegenerative. These results indicate association with the disease states, although not yet clear-cut to yield specific biomarkers. We also highlight mechanisms whereby thiol pools affect atherosclerosis pathophysiology. Overall, it is unlikely that a single measurement provides global assessment of plasma oxidative stress. Rather, assessment of individual thiol pools and thiol-proteins specific to any given condition has more solid and logical perspective to yield novel relevant information on disease risk and prognosis.
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42

Hu, Wentao, Sara Tedesco, Brian McDonagh, José Antonio Bárcena, Catherine Keane, and David Sheehan. "Selection of thiol- and disulfide-containing proteins of Escherichia coli on activated thiol-Sepharose." Analytical Biochemistry 398, no. 2 (March 2010): 245–53. http://dx.doi.org/10.1016/j.ab.2009.11.002.

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43

Vašková, Janka, Ladislav Kočan, Ladislav Vaško, and Pál Perjési. "Glutathione-Related Enzymes and Proteins: A Review." Molecules 28, no. 3 (February 2, 2023): 1447. http://dx.doi.org/10.3390/molecules28031447.

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The tripeptide glutathione is found in all eukaryotic cells, and due to the compartmentalization of biochemical processes, its synthesis takes place exclusively in the cytosol. At the same time, its functions depend on its transport to/from organelles and interorgan transport, in which the liver plays a central role. Glutathione is determined as a marker of the redox state in many diseases, aging processes, and cell death resulting from its properties and reactivity. It also uses other enzymes and proteins, which enables it to engage and regulate various cell functions. This paper approximates the role of these systems in redox and detoxification reactions such as conjugation reactions of glutathione-S-transferases, glyoxylases, reduction of peroxides through thiol peroxidases (glutathione peroxidases, peroxiredoxins) and thiol–disulfide exchange reactions catalyzed by glutaredoxins.
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Kinnula, V. L., K. Vuorinen, H. Ilumets, P. Rytila, and M. Myllarniemi. "Thiol Proteins, Redox Modulation and Parenchymal Lung Disease." Current Medicinal Chemistry 14, no. 2 (January 1, 2007): 213–22. http://dx.doi.org/10.2174/092986707779313345.

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45

Park, Jeong-Won, Jae-Young Song, Hyang-Ran Hwang, Hee-Jin Park, Hee-Shang Youn, Ji-Hyun Seo, Hyung-Lyun Kang, et al. "Proteomic Analysis of Thiol-active Proteins ofHelicobacter pylori26695." Journal of Bacteriology and Virology 42, no. 3 (2012): 211. http://dx.doi.org/10.4167/jbv.2012.42.3.211.

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46

Ma, Kaiqing, He Yang, Tianruo Shen, Yongkang Yue, Lingling Zhao, Xiaogang Liu, Fangjun Huo, and Caixia Yin. "Unique assembly of carbonylpyridinium and chromene reveals mitochondrial thiol starvation under ferroptosis and novel ferroptosis inducer." Chemical Science 13, no. 13 (2022): 3706–12. http://dx.doi.org/10.1039/d2sc00328g.

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Carbonylpyridinium and chromene were elaborately assembled to highly target mitochondrial thiol assay by releasing o-quinone methide from CM-Mit to label proteins, thus avoiding diffusion out of the mitochondria, which enabled accurately spatiotemporal detection of thiol.
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Yoshida, Keisuke, Ayaka Hara, Kazunori Sugiura, Yuki Fukaya, and Toru Hisabori. "Thioredoxin-like2/2-Cys peroxiredoxin redox cascade supports oxidative thiol modulation in chloroplasts." Proceedings of the National Academy of Sciences 115, no. 35 (August 13, 2018): E8296—E8304. http://dx.doi.org/10.1073/pnas.1808284115.

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Thiol-based redox regulation is central to adjusting chloroplast functions under varying light conditions. A redox cascade via the ferredoxin-thioredoxin reductase (FTR)/thioredoxin (Trx) pathway has been well recognized to mediate the light-responsive reductive control of target proteins; however, the molecular basis for reoxidizing its targets in the dark remains unidentified. Here, we report a mechanism of oxidative thiol modulation in chloroplasts. We biochemically characterized a chloroplast stroma-localized atypical Trx from Arabidopsis, designated as Trx-like2 (TrxL2). TrxL2 had redox-active properties with an unusually less negative redox potential. By an affinity chromatography-based method, TrxL2 was shown to interact with a range of chloroplast redox-regulated proteins. The direct discrimination of thiol status indicated that TrxL2 can efficiently oxidize, but not reduce, these proteins. A notable exception was found in 2-Cys peroxiredoxin (2CP); TrxL2 was able to reduce 2CP with high efficiency. We achieved a complete in vitro reconstitution of the TrxL2/2CP redox cascade for oxidizing redox-regulated proteins and draining reducing power to hydrogen peroxide (H2O2). We further addressed the physiological relevance of this system by analyzing protein-oxidation dynamics. In Arabidopsis plants, a decreased level of 2CP led to the impairment of the reoxidation of redox-regulated proteins during light–dark transitions. A delayed response of protein reoxidation was concomitant with the prolonged accumulation of reducing power in TrxL2. These results suggest an in vivo function of the TrxL2/2CP redox cascade for driving oxidative thiol modulation in chloroplasts.
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48

Allen, J. W. A., and S. J. Ferguson. "The Escherichia coli cytochrome c maturation (Ccm) apparatus can mature cytochromes with an extra cysteine within or adjacent to the CXXCH motif." Biochemical Society Transactions 34, no. 1 (January 20, 2006): 91–93. http://dx.doi.org/10.1042/bst0340091.

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c-Type cytochromes are characterized by covalent attachment of haem to protein through thioether bonds between the vinyl groups of the haem and the thiols of a Cys-Xaa-Xaa-Cys-His motif. Proteins of this type play crucial roles in the biochemistry of the nitrogen cycle. Many Gram-negative bacteria use the Ccm (cytochrome c maturation) proteins for the post-translational haem attachment to their c-type cytochromes. The Ccm system can correctly mature c-type cytochromes with CCXXCH, CCXCH, CXCCH and CXXCHC motifs, even though these are not found naturally and the extra cysteine might, in principle, disrupt the biogenesis proteins. The non-occurrence of these motifs probably relates to the destructive chemistry that can occur if a free thiol reacts with haem iron to generate a radical.
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49

Hamitouche, Fella, Jean Armengaud, Luc Dedieu, and Catherine Duport. "Cysteine Proteome Reveals Response to Endogenous Oxidative Stress in Bacillus cereus." International Journal of Molecular Sciences 22, no. 14 (July 14, 2021): 7550. http://dx.doi.org/10.3390/ijms22147550.

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At the end of exponential growth, aerobic bacteria have to cope with the accumulation of endogenous reactive oxygen species (ROS). One of the main targets of these ROS is cysteine residues in proteins. This study uses liquid chromatography coupled to high-resolution tandem mass spectrometry to detect significant changes in protein abundance and thiol status for cysteine-containing proteins from Bacillus cereus during aerobic exponential growth. The proteomic profiles of cultures at early-, middle-, and late-exponential growth phases reveals that (i) enrichment in proteins dedicated to fighting ROS as growth progressed, (ii) a decrease in both overall proteome cysteine content and thiol proteome redox status, and (iii) changes to the reduced thiol status of some key proteins, such as the transition state transcriptional regulator AbrB. Taken together, our data indicate that growth under oxic conditions requires increased allocation of protein resources to attenuate the negative effects of ROS. Our data also provide a strong basis to understand the response mechanisms used by B. cereus to deal with endogenous oxidative stress.
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50

Lou, Marjorie F. "Glutathione and Glutaredoxin in Redox Regulation and Cell Signaling of the Lens." Antioxidants 11, no. 10 (October 1, 2022): 1973. http://dx.doi.org/10.3390/antiox11101973.

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The ocular lens has a very high content of the antioxidant glutathione (GSH) and the enzymes that can recycle its oxidized form, glutathione disulfide (GSSG), for further use. It can be synthesized in the lens and, in part, transported from the neighboring anterior aqueous humor and posterior vitreous body. GSH is known to protect the thiols of the structural lens crystallin proteins from oxidation by reactive oxygen species (ROS) so the lens can maintain its transparency for proper visual function. Age-related lens opacity or senile cataract is the major visual impairment in the general population, and its cause is closely associated with aging and a constant exposure to environmental oxidative stress, such as ultraviolet light and the metabolic end product, H2O2. The mechanism for senile cataractogenesis has been hypothesized as the results of oxidation-induced protein-thiol mixed disulfide formation, such as protein-S-S-glutathione and protein-S-S-cysteine mixed disulfides, which if not reduced in time, can change the protein conformation to allow cascading modifications of various kinds leading to protein–protein aggregation and insolubilization. The consequence of such changes in lens structural proteins is lens opacity. Besides GSH, the lens has several antioxidation defense enzymes that can repair oxidation damage. One of the specific redox regulating enzymes that has been recently identified is thioltransferase (glutaredoxin 1), which works in concert with GSH, to reduce the oxidative stress as well as to regulate thiol/disulfide redox balance by preventing protein-thiol mixed disulfide accumulation in the lens. This oxidation-resistant and inducible enzyme has multiple physiological functions. In addition to protecting structural proteins and metabolic enzymes, it is able to regulate the redox signaling of the cells during growth factor-stimulated cell proliferation and other cellular functions. This review article focuses on describing the redox regulating functions of GSH and the thioltransferase enzyme in the ocular lens.
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