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Filename: drivers/Session_files_driver.php
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Function: require_once
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Function: _error_handler
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Filename: controllers/Detail.php
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File: /var/www/html/application/controllers/Detail.php
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Function: _error_handler
File: /var/www/html/index.php
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Function: _error_handler
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Filename: controllers/Detail.php
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Filename: models/Detail_model.php
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Function: insertAPISummary
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Function: formatAIDetailSummary
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Filename: controllers/Detail.php
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Thioredoxin (Trx), a small redox protein, controls multiple processes in eukaryotes and bacteria by changing the thiol redox status of selected proteins. The function of Trx in archaea is, however, unexplored. To help fill this gap, we have investigated this aspect in methanarchaea--strict anaerobes that produce methane, a fuel and greenhouse gas. Bioinformatic analyses suggested that Trx is nearly universal in methanogens. Ancient methanogens that produce methane almost exclusively from H2 plus CO2 carried approximately two Trx homologs, whereas nutritionally versatile members possessed four to eight. Due to its simplicity, we studied the Trx system of Methanocaldococcus jannaschii--a deeply rooted hyperthermophilic methanogen growing only on H2 plus CO2. The organism carried two Trx homologs, canonical Trx1 that reduced insulin and accepted electrons from Escherichia coli thioredoxin reductase and atypical Trx2. Proteomic analyses with air-oxidized extracts treated with reduced Trx1 revealed 152 potential targets representing a range of processes--including methanogenesis, biosynthesis, transcription, translation, and oxidative response. In enzyme assays, Trx1 activated two selected targets following partial deactivation by O2, validating proteomics observations: methylenetetrahydromethanopterin dehydrogenase, a methanogenesis enzyme, and sulfite reductase, a detoxification enzyme. The results suggest that Trx assists methanogens in combating oxidative stress and synchronizing metabolic activities with availability of reductant, making it a critical factor in the global carbon cycle and methane emission. Because methanogenesis developed before the oxygenation of Earth, it seems possible that Trx functioned originally in metabolic regulation independently of O2, thus raising the question whether a complex biological system of this type evolved at least 2.5 billion years ago.
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http://dx.doi.org/10.1073/pnas.1324240111 | DOI Listing |
Epigenomics
December 2024
Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, Pakistan.
Aim: The hypoxic tumor microenvironment (TME) in oral squamous cell carcinoma (OSCC) is primarily regulated by hypoxia-inducible factor-1 alpha (HIF-1α), impacting histone acetylation and methylation, which contribute to drug resistance. Vorinostat, a histone deacetylase inhibitor (HDACi), de-stabilizes HIF-1α, while PX-12, a thioredoxin-1 (Trx-1) inhibitor, prevents HIF-1α accumulation. Combining HDACi with a Trx-1 inhibitor may enhance efficacy and reduce resistance by increasing reactive oxygen species (ROS) in cancer cells.
View Article and Find Full Text PDFJ Plant Res
December 2024
Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Thiol/disulfide-based redox regulation is a key mechanism for modulating protein functions in response to changes in cellular redox status. Two thioredoxin (Trx)-like proteins [atypical Cys His-rich Trx (ACHT) and Trx-like2 (TrxL2)] have been identified as crucial for oxidizing and deactivating several chloroplast enzymes during light-to-dark transitions; however, their roles remain to be fully understood. In this study, we investigated the functions of Trx-like proteins in seed development.
View Article and Find Full Text PDFComput Struct Biotechnol J
December 2024
Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, School of Agriculture, Biomedicine and Environment, La Trobe University, Bundoora, Australia.
In bacteria the formation of disulphide bonds is facilitated by a family of enzymes known as the disulphide bond forming (Dsb) proteins, which, despite low sequence homology, belong to the thioredoxin (TRX) superfamily. Among these enzymes is the disulphide bond-forming protein A (DsbA); a periplasmic thiol oxidase responsible for catalysing the oxidative folding of numerous cell envelope and secreted proteins. Pathogenic bacteria often contain diverse Dsb proteins with distinct functionalities commonly associated with pathogenesis.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Department of Microbiology and Immunology, Showa University School of Medicine, Tokyo 1428555, Japan.
Intranasal immunization is one of the most effective methods for eliciting lung mucosal immunity. Multiple intranasal immunization with bacterial polypeptide, termed as a modified PnxIIIA (MP3) protein, is known to elicit production of a specific antibody in mice. In this study, a nasal immuno-inducible sequence (NAIS) was designed to remove the antigenicity of the MP3 protein that can induce mucosal immunity by intranasal immunization, and was examined to induce antigen-specific antibodies against the fused bacterial thioredoxin (Trx) as a model antigen.
View Article and Find Full Text PDFChem Biodivers
December 2024
Qinghai University, Department of Pharmacy, Faculty of Medicine, No.16 Kunlun Road, Chengxi District, Xining City, Qinghai Province, China, 810001, Xining, CHINA.
Background Ischemia-reperfusion damage to cardiomyocytes is one of the main directions of cardiovascular disease research, and Bawei Chenxiang powder (BWCX) is a traditional ethnomedicinal compound preparation mainly used in the treatment of cardiovascular diseases. Based on serum pharmacology, the present study aimed to explore the potential mechanism of BWCX against myocardial ischemia-reperfusion damage to cardiomyocytes. Materials and Methods We prepared BWCX-serum containing.
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