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Dissertations / Theses on the topic 'Cysteine redox'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Hitron, John Andrew. "AN OPTIMIZED SOLID-PHASE REDUCTION AND CAPTURE STRATEGY FOR THE STUDY OF REVERSIBLY-OXIDIZED CYSTEINES AND ITS APPLICATION TO METAL TOXICITY." UKnowledge, 2018. https://uknowledge.uky.edu/toxicology_etds/22.

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The reversible oxidation of cysteine by reactive oxygen species (ROS) is both a mechanism for cellular protein signaling as well as a cause of cellular injury and death through the generation of oxidative stress. The study of cysteine oxidation is complicated by the methodology currently available to isolate and enrich oxidized-cysteine containing proteins. We sought to simplify this process by reducing the time needed to process samples and reducing sample loss and contamination risk. We accomplished this by eliminating precipitation steps needed for the protocol by (a) introducing an in-solu

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12

Guo, Liang. "Structural and functional studies of mitochondrial small Tim proteins." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/structural-and-functional-studies-of-mitochondrial-small-tim-proteins(03dde6fd-6692-4af5-9023-b85a33803fcd).html.

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Most mitochondrial proteins are encoded by nuclear DNA, and synthesised in the cytosol, then imported into the different mitochondrial subcompartments. To reach their destination, mitochondrial inner membrane proteins require import across the outer mitochondrial membrane, and through the intermembrane space. This passage through the IMS is assisted by the small Tim proteins. This family is characterised by conserved cysteine residues arranged in a twin CX3C motif. They can form Tim9-Tim10 and Tim8-Tim13 complexes, while Tim12 appears to form part of a Tim9-Tim10-Tim12 complex that is associat

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13

Oliveira, Fernando Castro Mota de. "Mecanismos redox e aplicações analíticas de L-Cisteína e L-Glutationa ancoradas sobre eletrodos de ouro recobertos com camadas auto-arranjadas de ácido 3-mercaptopropiônico." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/46/46136/tde-15012014-151210/.

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Moléculas de L-cisteína (CSH) e L-glutationa (GSH) foram ancoradas na superfície de eletrodos de ouro, previamente modificados com uma camada autoarranjada de ácido 3-mercaptopropiônico (MPA). Esta arquitetura molecular foi importante para preservar a atividade redox dos grupos tiólicos da CSH e GSH na interface eletrodo/solução. A identificação do par redox R-S-S-R/R-SH, bem como a determinação do pKa dos grupos -SH superficiais, foram efetuadas usando voltametria cíclica em soluções de eletrólito em diferentes pH contedo ferricianeto de potássio. A presença dos grupos -SH e -S-S- na superfíc

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14

Zecchin, Paolo. "Mobilisation et incorporation enzymatique du soufre lors de réactions non-redox impliquant un centre [4Fe-4S] : étude biochimique et structurale d’une cystéine désulfidase et d’une sulfurtransférase." Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS667.pdf.

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Les composés soufrés, tels que la cystéine et certains cofacteurs, jouent un rôle essentiel dans les processus cellulaires. Cette thèse se concentre sur deux enzymes dépendantes d’un centre [4Fe-4S], impliquées dans le métabolisme du soufre chez l'archée anaérobie Methanococcus maripaludis : MmCyuA, une L-cystéine désulfidase, et MmLarE, une sulfurtransférase dépendante de l'ATP. La première partie porte sur MmCyuA, qui catalyse la conversion de la L-cystéine en sulfure d’hydrogène et 2-aminoacrylate, ultérieurement transformé en pyruvate et ammoniac. Les structures cristallographiques de MmCy

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15

Tong, Grace C. "Characterization of Cys-34 in serum albumin." Columbus, Ohio : Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc%5fnum=osu1061473878.

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Thesis (Ph. D.)--Ohio State University, 2003.<br>Title from first page of PDF file. Document formatted into pages; contains xxiii, 325 p.; also contains graphics (some col.). Includes abstract and vita. Advisor: Gary E. Means, Dept. of Biochemistry. Includes bibliographical references (p. 206-225).

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16

Hagedorn, Tara Dawn. "Reactive Sulfur: Redox Reactions of Cysteines and Methionines in the Cytoskeletal Protein Tubulin." W&M ScholarWorks, 2011. https://scholarworks.wm.edu/etd/1539626916.

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17

Pan, Kuan-Ting, and 潘冠廷. "Mass spectrometry-based quantitative proteomic strategies for dissecting multiplex cysteine redox modifications." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/87417378131849201159.

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博士<br>國立臺灣大學<br>生化科學研究所<br>101<br>Distinctive states of redox-dependent cysteine (Cys) modifications, such as sulfenation (SOH), S-nitrosylation (SNO) and S-glutathionylation (SSG), are known to regulate signaling homeostasis under various pathophysiological conditions, including myocardial injury or protection in response to ischemic stress. Recent evidence further implicates a dynamic interplay among these modified forms following changes in cellular redox environment. Simultaneous monitoring of the dynamics of various reversible cysteine modifications is required to obtain a systems view of

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18

Huang, Lu. "The Role of Redox-dependent Reactions with Kras Cysteine 118 in Tumorigenesis." Diss., 2015. http://hdl.handle.net/10161/9806.

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<p>The Ras family of small GTPases, comprised of the KRAS, NRAS, and HRAS genes, are mutated to encode constitutively-active, GTP-bound, oncogenic proteins in upwards of one quarter or more of all human cancers, which is well established to promote tumorigenesis. Despite the prominent role these genes play in human cancer, the encoded proteins have proven difficult to pharmacologically inhibit. Therefore, it is important to understand how Ras proteins are activated. </p><p>RAS proteins cycle between a GDP-bound inactive state and a GTP-bound active state through guanine nucleotide exchange fa

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19

Joshi, Manisha. "Comparative redox proteomics to investigate role of Nox mediated redox signaling in Fusarium graminearum pathogenesis." 2011. http://hdl.handle.net/1993/4750.

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Fusarium graminearum causes Fusarium Head Blight, (one of) the most destructive cereal diseases in Canada. Yield loss, quality degradation and mycotoxin production make Fusarium a multifaceted threat. Regulated production of reactive oxygen species by Nox enzymes is indispensable for fungal pathogenesis. F. graminearum Nox mutant ∆noxAB produced equivalent mycotoxin but caused reduced virulence than wild-type. We hypothesized that Nox mediated redox signaling may participate in F. graminearum pathogenicity. Two-DE and gel-free biotin affinity chromatography, followed by LC-MS/MS analysis were

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20

Behring, Jessica Belle. "Evaluating changes in reversible cysteine oxidation of cardiac proteins as metabolic syndrome develops into cardiovascular disease." Thesis, 2016. https://hdl.handle.net/2144/19057.

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Oxidative stress is commonly associated with diet-induced metabolic syndrome (MetS) and left ventricular cardiac remodeling, but much remains unknown about the role of redox signaling, sensors, and switches in mediating the effects of high fat and sugar intake. In this work, I describe and apply an optimized method for quantifying changes in reversible protein-cysteine oxidation in the heart. This method uses isobaric tagging of cysteine thiols and mass spectrometry in a modified biotin switch on whole tissue lysate. Analyzing the resulting data with systems biology approaches helped delineate

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21

Thompson, Melissa Danielle. "Redox regulation of cysteine-674 of SERCA 2 is critical for growth factor- and ischemia-induced angiogenesis." Thesis, 2014. https://hdl.handle.net/2144/14664.

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Ischemic cardiovascular disease shows trends of increasing morbidity and mortality in the United States and around the world. Current therapeutic options are limited, but the identification of key disease mechanisms and targets will inform novel therapeutic development to help decrease disease burden. One potential target is the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA), a key regulator of Ca2+ homeostasis which plays multiple roles in the cardiovascular system. SERCA catalyzes the hydrolysis of ATP and couples it to the translocation of free cytosolic Ca2+ into SR/ER stores. SERCA i

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22

Veeravalli, Karthik. "Engineering of de novo pathways for biosynthesis of glutathione analogues in Escherichia coli." Thesis, 2010. http://hdl.handle.net/2152/ETD-UT-2010-05-999.

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The low molecular weight (L.M.W.) thiol redox couple formed by γ-L-glutamyl-L-cysteinyl glycine, also called glutathione (reduced and oxidized), is present in most eukaryotes and a few species of bacteria. Glutathione plays a role in numerous cellular processes by providing a means of shuttling electrons to different enzymatic systems. As a result, thiol-dependent redox metabolic processes are highly coupled. Due to tight coupling of redox reactions, it is difficult to understand how changes in the concentration of glutathione would affect a specific glutathione-dependent process. Interesting

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23

Singh, Simranjit. "Redox regulation of protein phosphatase-1 and ER stress regulation of connective tissue growth factor in cardiomyocytes." Doctoral thesis, 2017. http://hdl.handle.net/11858/00-1735-0000-0023-3E92-5.

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24

Schaefer, Moritz. "Cysteine residues of the mammalian GET receptor: Essential for tail-anchored protein insertion?" Doctoral thesis, 2017. http://hdl.handle.net/11858/00-1735-0000-0023-3E49-D.

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25

Lai, Wen-Chung, and 賴文忠. "A Web-based Server for Predicting the Secondary Structures of Proteins and Redox States of Cysteine by Using 2D NMR Chemical Shifts." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/40226315729373404145.

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碩士<br>國立成功大學<br>製造工程研究所碩博士班<br>94<br>2DCSi predicts the secondary structures of 20 amino acids and the redox states of cysteine residues in proteins by using their NMR chemical shifts. We use 2D cluster analyses of 1Hα, 1HN, 13Cα, 13C’, and 15NH versus 13Cβ NMR chemical shifts which were constructed from BioMagResBank (BMRB) entries. A database of 20 amino acids’ 1Hα, 1HN, 13Cα, 13C’, 15NH, and 13Cβ NMR chemical shifts were obtained and then used to produce the scoring matrices. Applying the prediction rules, the 2DCSi server enables users to submit NMR chemical shifts data and to request prot

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26

Kannappan, Ramakrishnan. "Design and analysis of an electronically switchable ion exchange system." 2009. http://hdl.handle.net/2152/7834.

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Metal contamination is a considerable environmental problem because metals are persistent contaminants. Ion exchange is one of the most commonly used treatment options for trace metal removal. This research develops and evaluates a redox active modified ion exchange system that has the potential to reduce the ionic strength of ion exchange regeneration streams. Poly-L-cysteine (PLC) was selected as the redox active, adsorbing functional group on the surface of a reticulated vitreous carbon (RVC) electrode. PLC is an excellent soft acid metal chelator and is unique in that its thiol groups can

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27

Shee, Somnath. "Manipulating Bacterial and Host Reactive Oxygen Species (ROS)- based mechanisms to potentiate killing of Mycobacterium tuberculosis (Mtb)." Thesis, 2021. https://etd.iisc.ac.in/handle/2005/5680.

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Mycobacterium tuberculosis (Mtb) is evolutionarily equipped to resist exogenous reactive oxygen species but shows vulnerability to an increase in endogenous ROS (eROS). Since eROS is an unavoidable consequence of aerobic metabolism, understanding how eROS levels are controlled is essential yet remains uncharacterized. By combining the Mrx1-roGFP2 redox biosensor with transposon mutagenesis, we identified 368 genes (redoxosome) responsible for maintaining non-toxic levels of eROS in Mtb. Integrating redoxosome with a global network of protein-protein interactions and transcriptional regulators

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