Relevant bibliographies by topics / Cysteine redox

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Cysteine redox'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Cysteine redox"

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Kisty, Eleni A., Emma C. Saart, and Eranthie Weerapana. "Identifying Redox-Sensitive Cysteine Residues in Mitochondria." Antioxidants 12, no. 5 (2023): 992. http://dx.doi.org/10.3390/antiox12050992.

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The mitochondrion is the primary energy generator of a cell and is a central player in cellular redox regulation. Mitochondrial reactive oxygen species (mtROS) are the natural byproducts of cellular respiration that are critical for the redox signaling events that regulate a cell’s metabolism. These redox signaling pathways primarily rely on the reversible oxidation of the cysteine residues on mitochondrial proteins. Several key sites of this cysteine oxidation on mitochondrial proteins have been identified and shown to modulate downstream signaling pathways. To further our understanding of mi
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Behring, Jessica B., Sjoerd van der Post, Arshag D. Mooradian, et al. "Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation." Science Signaling 13, no. 615 (2020): eaay7315. http://dx.doi.org/10.1126/scisignal.aay7315.

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Stimulation of plasma membrane receptor tyrosine kinases (RTKs), such as the epidermal growth factor receptor (EGFR), locally increases the abundance of reactive oxygen species (ROS). These ROS then oxidize cysteine residues in proteins to potentiate downstream signaling. Spatial confinement of ROS is an important regulatory mechanism of redox signaling that enables the stimulation of different RTKs to oxidize distinct sets of downstream proteins. To uncover additional mechanisms that specify cysteines that are redox regulated by EGF stimulation, we performed time-resolved quantification of th
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Martinez-Banaclocha, Marcos A. "Targeting the Cysteine Redox Proteome in Parkinson’s Disease: The Role of Glutathione Precursors and Beyond." Antioxidants 12, no. 7 (2023): 1373. http://dx.doi.org/10.3390/antiox12071373.

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Encouraging recent data on the molecular pathways underlying aging have identified variants and expansions of genes associated with DNA replication and repair, telomere and stem cell maintenance, regulation of the redox microenvironment, and intercellular communication. In addition, cell rejuvenation requires silencing some transcription factors and the activation of pluripotency, indicating that hidden molecular networks must integrate and synchronize all these cellular mechanisms. Therefore, in addition to gene sequence expansions and variations associated with senescence, the optimization o
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Nagahara, Noriyuki. "Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases." Journal of Amino Acids 2011 (December 28, 2011): 1–7. http://dx.doi.org/10.4061/2011/709404.

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Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate. The redox changes of these enzymes are involved in their catalytic processes. On the other hand, transferases, and also some phosphatases and hydrolases, have a single-catalytic site cysteine residue. The cysteines are redox active, but their sulfenyl forms, which are inactive, are not well explained biologically. In particula
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Suzuki, Yuichiro J., Lucia Marcocci, Takashi Shimomura, Yuki Tatenaka, Yuya Ohuchi, and Tinatin I. Brelidze. "Protein Redox State Monitoring Studies of Thiol Reactivity." Antioxidants 8, no. 5 (2019): 143. http://dx.doi.org/10.3390/antiox8050143.

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Protein cysteine thiol status is a major determinant of oxidative stress and oxidant signaling. The -SulfoBiotics- Protein Redox State Monitoring Kit provides a unique opportunity to investigate protein thiol states. This system adds a 15-kDa Protein-SHifter to reduced cysteine residues, and this molecular mass shift can be detected by gel electrophoresis. Even in biological samples, Protein-SHifter Plus allows the thiol states of specific proteins to be studied using Western blotting. Peroxiredoxin 6 (Prx6) is a unique one-cysteine peroxiredoxin that scavenges peroxides by utilizing conserved
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Percio, Anna, Michela Cicchinelli, Domiziana Masci, Mariagrazia Summo, Andrea Urbani, and Viviana Greco. "Oxidative Cysteine Post Translational Modifications Drive the Redox Code Underlying Neurodegeneration and Amyotrophic Lateral Sclerosis." Antioxidants 13, no. 8 (2024): 883. http://dx.doi.org/10.3390/antiox13080883.

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Redox dysregulation, an imbalance between oxidants and antioxidants, is crucial in the pathogenesis of various neurodegenerative diseases. Within this context, the “redoxome” encompasses the network of redox molecules collaborating to maintain cellular redox balance and signaling. Among these, cysteine-sensitive proteins are fundamental for this homeostasis. Due to their reactive thiol groups, cysteine (Cys) residues are particularly susceptible to oxidative post-translational modifications (PTMs) induced by free radicals (reactive oxygen, nitrogen, and sulfur species) which profoundly affect
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McDonagh, Brian, Pablo Martínez-Acedo, Jesús Vázquez, C. Alicia Padilla, David Sheehan, and José Antonio Bárcena. "Application of iTRAQ Reagents to Relatively Quantify the Reversible Redox State of Cysteine Residues." International Journal of Proteomics 2012 (July 15, 2012): 1–9. http://dx.doi.org/10.1155/2012/514847.

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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. Reversible cysteine modifications allow for potential redox regulation of proteins. Traditional measurement of the relative absolute quantity of a protein between two samples is not always necessarily proportional to the activity of the protein. 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 analysi
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Dafre, Alcir Luiz, Tiago A. S. Brandão, and Evaldo Reischl. "Involvement of vertebrate hemoglobin in antioxidant protection: chicken blood as a model." Canadian Journal of Zoology 85, no. 3 (2007): 404–12. http://dx.doi.org/10.1139/z07-020.

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Redox balance can be described as the equilibrium between oxidative and reductive forces within the cell. These forces control several cellular events, including the modulation of redox-sensitive receptors and signaling pathways. In cells, glutathione is the major non-protein thiol and is considered the main redox buffer. The ratio between the oxidized (GSSG) and reduced (GSH) forms reflects the cellular redox balance. Reactive protein thiols, including vertebrate hemoglobin (Hb), have been proposed as effective antioxidants that can contribute to the redox balance. To further explore this pos
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Baidanoff, Fernando Martin, Laura Lucía Trebucq, Santiago Andrés Plano, Phillip Eaton, Diego Andrés Golombek, and Juan José Chiesa. "Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2." Biomolecules 12, no. 7 (2022): 892. http://dx.doi.org/10.3390/biom12070892.

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The molecular circadian clock is based on a transcriptional/translational feedback loop in which the stability and half-life of circadian proteins is of importance. Cysteine residues of proteins are subject to several redox reactions leading to S-thiolation and disulfide bond formation, altering protein stability and function. In this work, the ability of the circadian protein period 2 (PER2) to undergo oxidation of cysteine thiols was investigated in HEK-293T cells. PER2 includes accessible cysteines susceptible to oxidation by nitroso cysteine (CysNO), altering its stability by decreasing it
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Poncin, Mégane A., Pierre Van Meerbeeck, Joshua D. Simpson, et al. "Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function." Antioxidants 10, no. 12 (2021): 1902. http://dx.doi.org/10.3390/antiox10121902.

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Human peroxiredoxin-5 (PRDX5) is a unique redox-sensitive protein that plays a dual role in brain ischemia-reperfusion injury. While intracellular PRDX5 has been reported to act as a neuroprotective antioxidative enzyme by scavenging peroxides, once released extracellularly from necrotic brain cells, the protein aggravates neural cell death by inducing expression of proinflammatory cytokines in macrophages through activation of Toll-like receptor (TLR) 2 (TLR2) and 4 (TLR4). Although recent evidence showed that PRDX5 was able to interact directly with TLR4, little is known regarding the role o
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Dissertations / Theses on the topic "Cysteine redox"

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Paulech, Jana. "Development of Redox Proteomic Techniques to Profile Cysteine Post-translational Modifications in the Myocardium." Thesis, The University of Sydney, 2014. http://hdl.handle.net/2123/12006.

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Once thought to be an unfortunate consequence of aerobic life, the generation of reactive oxygen and nitrogen species (ROS / RNS) is now known to be integral to the proper functioning of the cell. Cysteine (Cys) residues in proteins show all the necessary properties to act as a sensor / responder to redox signals. The potential role for Cys residues in both the physiological function and pathological dysfunction of the cell has lead to much interest in the identification of target proteins / cellular processes and sites regulated by Cys post-translational modification (PTM). Progress in this a
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Caubrière, Damien. "Développement de nouveaux biosenseurs redox pour composés soufrés." Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0359.

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Au cours des dix dernières années, le développement de biosenseurs redox fluorescents a permis de générer des outils permettant d'étudier les dynamiques in vivo de molécules comme les formes réduite et oxydée du glutathion ou le peroxyde d'hydrogène. La cystéine étant un métabolite clé du métabolisme du soufre, l'objectif de ce projet de thèse était de développer un biosenseur redox fluorescent spécifique de la cystéine en couplant une oxydoréductase à la roGFP2 (reduction-oxidation green fluorescent protein). Tout d'abord les activités de plusieurs isoformes de cystéine désulfurases (CD) et d
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Di, Giacinto Nastasia <1987&gt. "Cysteine-Based Redox Modifications in the Regulation of Calvin-Benson Cycle Enzymes from Chlamydomonas Reinhartdtii." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2016. http://amsdottorato.unibo.it/7647/1/digiacinto_nastasia_tesi.pdf.

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In photosynthetic organisms the redox-dependent modification of thiols belonging to enzymes of the photosynthetic cycle, plays a prominent role in the regulation of metabolism and signalling. An important regulatory mechanism is represented by light that acts through a ferredoxin-thioredoxin system. The system permits the reduction/oxidation of disulfide bridges of the target enzymes. Moreover, cysteines residues can undergo other modifications such as glutathionylation and nitrosylation. Proteomic studies have allowed the identification of new putative targets of redox modifications, includin
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Di, Giacinto Nastasia <1987&gt. "Cysteine-Based Redox Modifications in the Regulation of Calvin-Benson Cycle Enzymes from Chlamydomonas Reinhartdtii." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2016. http://amsdottorato.unibo.it/7647/.

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In photosynthetic organisms the redox-dependent modification of thiols belonging to enzymes of the photosynthetic cycle, plays a prominent role in the regulation of metabolism and signalling. An important regulatory mechanism is represented by light that acts through a ferredoxin-thioredoxin system. The system permits the reduction/oxidation of disulfide bridges of the target enzymes. Moreover, cysteines residues can undergo other modifications such as glutathionylation and nitrosylation. Proteomic studies have allowed the identification of new putative targets of redox modifications, includin
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Feng, Jian. "Effect of redox potential, sulfide ions and a persulfide forming cysteine residue on carbon monoxide dehydrogenase." Diss., Texas A&M University, 2003. http://hdl.handle.net/1969.1/2197.

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The Ni-Fe-S C-cluster of carbon monoxide dehydrogenases (CODH), which catalyzes the reversible oxidation of CO to CO2, can be stabilized in four redox states: Cox, Cred1, Cint, and Cred2. The best-supported mechanism of catalysis involves a one-electron reductive activation of Cox to Cred1 and a catalytic cycle in which Cred1 binds and oxidizes CO, forming Cred2 and releasing CO2. Recently reported experiments appear to have disqualified this mechanism, as activation was concluded to require reduction to a C-cluster state more reduced than Cred1. The results presented in this dissertation sugg
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Igbaria, Aeid. "Functional redox compartmentation of GSH in the yeast Saccharomyces cerevisiae." Thesis, Paris 11, 2011. http://www.theses.fr/2011PA112189.

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L'oxydation des résidus cystéines est une modification biochimique très répandue survenant dans tous les compartiments des cellules eucaryotes. Ce phénomène sert le repliement oxydatif des protéines dans le réticulum endoplasmique (RE), l'importation de protéines dans l'espace intermembranaire de la mitochondrie (IMS). De plus, il a un rôle régulateur dans la matrice mitochondriale et dans le cytosol où il contrôle l’activité des enzymes et des protéines de signalisation et de régulation. Dans tous ces procédés, la réversibilité de l'oxydation des résidus Cys est une caractéristique essentiell
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Tokarew, Jacqueline M. "A Novel Role for the Parkinson Disease-Linked and Neuromelanin-Associated Parkin Protein as a Cysteine-Dependent Redox-State Regulator." Thesis, Université d'Ottawa / University of Ottawa, 2021. http://hdl.handle.net/10393/42389.

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Parkinson disease (PD) is an incurable disease, second only to Alzheimer’s disease as the most common neurodegenerative disease in adults. Unfortunately, the course of disease is significantly longer for individuals diagnosed at an early age (20-40 years of age). Although early-onset, recessively inherited cases represent a small subset of individuals with PD (~5- 10%), their clinical presentation is unique, with symptoms being almost exclusively motor-related. The expressivity of early-onset PD is partially explained by post-mortem neuropathological findings, which demonstrate a specific loss
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Schneider, Alex [Verfasser], L. A. [Akademischer Betreuer] Wessjohann, and C. [Akademischer Betreuer] Jacob. "Studies of redox and exchange reactions of (seleno)cysteine peptides and model compounds / Alex Schneider. Betreuer: L. A. Wessjohann ; C. Jacob." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2011. http://d-nb.info/1025135393/34.

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Prioretti, Laura. "Sulfur metabolism in microalgae." Doctoral thesis, Università Politecnica delle Marche, 2015. http://hdl.handle.net/11566/243011.

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La concentrazione media di SO4 2- in oceano è 28-30 mmol L-1. Essa ha subito notevoli variazioni nel corso della storia della Terra e potrebbe aver facilitato la radiazione delle alghe della linea rossa (alghe con chl a+c quali diatomee, dinoflagellate e coccolitoforidi) a discapito di quelle della linea verde (alghe con chl a+b) e dei cianobatteri. È ancora da chiarire se gli enzimi responsabili dell’assimilazione del SO4 2- negli organismi fotosintetici abbiano svolto un ruolo nel controllare l’adattamento delle alghe alle variazioni di concentrazione del SO4 2-. In accordo con stud
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García, Santamarina Sarela 1978. "Control of redox homeostasis : environmental and genetic regulation of oxidative protein damage in Schizosaccharomyces pombe." Doctoral thesis, Universitat Pompeu Fabra, 2013. http://hdl.handle.net/10803/666989.

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Oxidation of specific cysteines in proteins by hydrogen peroxide (H2O2) is a cellular mechanism that triggers signalling pathways, such as the antioxidant responses in microbial systems. However, H2O2 can be transformed to the more reactive radical hydroxyl OH▪ species, through the Fenton reaction, the main causative of protein carbonylations. These modifications can not be repaired, and constitute classical marks of oxidative damage. Along this thesis we were interested in studying and understand the consequences of reactive oxygen species (ROS) reactivity on proteins. Thus, we developed pr
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Books on the topic "Cysteine redox"

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Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (U
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Book chapters on the topic "Cysteine redox"

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Zhang, Yanhong, and Neil Hogg. "S-Nitrosation of Cysteine Thiols as a Redox Signal." In Redox Proteomics. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/0471973122.ch6.

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Bohle, Finja, Andreas J. Meyer, and Stefanie J. Mueller-Schuessele. "Quantification of Redox-Sensitive GFP Cysteine Redox State via Gel-Based Read-Out." In Methods in Molecular Biology. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2667-2_13.

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Fujii, Junichi, Sho Kobayashi, and Takujiro Homma. "Regulation of Ferroptosis Through the Cysteine-Glutathione Redox Axis." In Ferroptosis in Health and Disease. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-26780-3_11.

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Morimoto, Kyoko, Monika Stegmann, Farnusch Kaschani, Shabaz Mohammed, and Renier A. L. van der Hoorn. "Cysteine Reactivity Profiling to Unveil Redox Regulation in Phytopathogens." In Methods in Molecular Biology. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2079-3_9.

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Vogelsang, Lara, Jürgen Eirich, Iris Finkemeier, and Karl-Josef Dietz. "Thiol Redox Proteomics for Identifying Redox-Sensitive Cysteine Residues Within the Protein of Interest During Stress." In Methods in Molecular Biology. Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3973-3_7.

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Chan, Hong-Lin, John Sinclair, and John F. Timms. "Proteomic Analysis of Redox-Dependent Changes Using Cysteine-Labeling 2D DIGE." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-573-2_8.

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Habich, Markus, and Jan Riemer. "Detection of Cysteine Redox States in Mitochondrial Proteins in Intact Mammalian Cells." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6824-4_8.

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Wani, Revati, and Brion W. Murray. "Analysis of Cysteine Redox Post-Translational Modifications in Cell Biology and Drug Pharmacology." In Protein Bioinformatics. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6783-4_9.

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Muslin, Elizabeth H., and Louise E. Anderson. "Identification of One Pair of Domain-Locking, Redox-Sensitive Cysteine Residues in Maize Chloroplast Malate Dehydrogenase." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_836.

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Denoncin, Katleen, Valérie Nicolaes, Seung-Hyun Cho, Pauline Leverrier, and Jean-François Collet. "Protein Disulfide Bond Formation in the Periplasm: Determination of the In Vivo Redox State of Cysteine Residues." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-245-2_20.

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Conference papers on the topic "Cysteine redox"

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Roman Rodriguez, J., J. Greenwell, J. Ritzenthaler, E. Torres-Gonzalez, Y. Zheng, and W. Watson. "Impact of Sex, Age, Diets, and Fasting in the Redox Potential of the Thiol Disulfide Couple Cysteine and Cysteine (Eh Cys/CySS) and Lung Cancer in Mice." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4095.

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Zhou, Bingsen, Leila Su, Shuya Hu, and Yun Yen. "Abstract 4755: The role of a pair of cysteine residues in the redox properties of human ribonucleotide reductase small subunits hp53R2 and hRRM2." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4755.

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Reports on the topic "Cysteine redox"

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Kim, Chongwoo A. Potential Cysteine Redox Regulation of the Polycomb Group. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada521853.

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