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Endoplasmic Reticulum Is at the Crossroads of Autophagy, Inflammation, and Apoptosis Signaling Pathways and Participates in the Pathogenesis of Diabetes Mellitus
Published 2013-01-01“…The endoplasmic reticulum (ER) is a central component of cellular functions and is involved in protein folding and trafficking, lipid synthesis, and maintenance of calcium homeostasis. …”
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22
Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice
Published 2015-01-01“…Multiple extracellular (pH, heat, oxidants, and detergents) or intracellular (DNA damage and Ca2+ overload) stress conditions trigger various types of the nuclear, endoplasmic reticulum (ER), cytoplasmatic, and mitochondrion-centered signaling events that allow cells to preserve the DNA integrity, protein folding, energetic, ionic and redox homeostasis, thus escaping from injury. …”
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23
Synthesis and Experimental Validation of New PDI Inhibitors with Antiproliferative Activity
Published 2017-01-01“…Besides acting as a protein folding catalyst, several evidences have suggested that PDI can bind small molecules containing, for example, a phenolic structure, which includes the estrogenic one. …”
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Influence of Acute High Glucose on Protein Abundance Changes in Murine Glomerular Mesangial Cells
Published 2016-01-01“…Additional studies confirmed the regulation of proteasomal subunit alpha-type 2 and the endoplasmic reticulum chaperone and oxidoreductase PDI (protein disulfide isomerase), suggesting altered ER protein folding capacity and proteasomal function in response to acute HG. …”
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25
Gene expression signatures between Limia perugiae (Poeciliidae) populations from freshwater and hypersaline habitats, with comparisons to other teleosts.
Published 2024-01-01“…We also found differences in gene expression patterns associated with cell-cycle and protein-folding processes between the hypersaline and freshwater L. perugiae. …”
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26
The Passage of Chaperonins to Extracellular Locations in <i>Legionella pneumophila</i> Requires a Functional Dot/Icm System
Published 2025-01-01“…Although chaperonins have an essential cytoplasmic function in protein folding, HtpB exits the cytoplasm to perform extracellular virulence-related functions that support <i>L. pneumophila</i>’s lifestyle. …”
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Lipid Oxidation at the Crossroads: Oxidative Stress and Neurodegeneration Explored in <i>Caenorhabditis elegans</i>
Published 2025-01-01“…In this review, we explore the role of lipid oxidation in protein folding and its associated pathological implications, with a particular focus on findings in neurodegeneration from <i>Caenorhabditis elegans</i> studies, an animal model that remains underutilized. …”
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Hyperthermia and targeting heat shock proteins: innovative approaches for neurodegenerative disorders and Long COVID
Published 2025-02-01“…HSPs such as HSP70 and HSP90 play pivotal roles in protein folding, aggregation prevention, and cellular protection, directly targeting pathological processes seen in NDs like Alzheimer's, Parkinson's, and Huntington's disease. …”
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29
Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
Published 2025-01-01“…Further spectroscopic experiments and molecular docking simulations showed that OPEs could entered the pocket structure of GB1 and induced secondary structural changes and protein folding through non-covalent interactions dominated by hydrogen bonding and van der Waals forces. …”
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INTRASPECIFIC VARIABILITY OF THE Sus1 SUCROSE SYNTHASE GENE IN Pisum sativum ACCESSIONS
Published 2018-03-01“…Six of them were deleterious and may potentially influence protein folding and stability. All the conservative motifs and active sites were detected in the translated amino acid sequences. …”
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31
Nanoplastics induces arrhythmia in human stem-cells derived cardiomyocytes
Published 2025-01-01“…Complementing these in vitro findings, transcriptome profiling of mice exposed to NPs for 8 weeks revealed disrupted RNA splicing, dysregulated protein translation, and defective protein folding. These molecular changes led to ER stress, apoptosis, and impaired transmembrane ion conductance, contributing to the arrhythmic phenotype. …”
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Unravelling the transcriptomic symphony of muscle ageing: key pathways and hub genes altered by ageing and caloric restriction in rat muscle revealed by RNA sequencing
Published 2025-01-01“…Upregulated genes were commonly involved in protein folding and immune responses; meanwhile, downregulated genes were often related to developmental biology. …”
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Insight into the role of antioxidant in microbial lignin degradation: Ascorbic acid as a fortifier of lignin-degrading enzymes
Published 2025-02-01“…Proteomics analysis suggested that the enhancement in enzyme activity was more likely to attributed to the reinforcement of AA on oxidative protein folding and transportation, rather than changes in enzyme expression. …”
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Identification of Host–Protein Interaction Network of Canine Parvovirus Capsid Protein VP2 in F81 Cells
Published 2025-01-01“…The results showed that CPV VP2 protein participated mainly in cell metabolism, cell biosynthesis, protein folding and various signal transduction processes. …”
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The DnaJ-Hsp70-Hsp90 co-chaperon networks in scallops under toxic Alexandrium dinoflagellates exposure
Published 2025-01-01“…A large set of co-chaperons comprising J-domain proteins (DnaJs) regulate the ATPase cycle of Hsp70s with Hsp90s, together constituting a dynamic and functionally versatile network for protein folding/unfolding and regulation. Marine bivalves could accumulate and tolerate paralytic shellfish toxins (PSTs), the well-noted neurotoxins generated during harmful algal blooms. …”
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Genetic and biochemical characterization of a radical SAM enzyme required for post-translational glutamine methylation of methyl-coenzyme M reductase
Published 2025-02-01“…Structural characterization of the Ni(II) form of Gln-methylated M. acetivorans MCR revealed no significant differences in the protein fold between the modified and unmodified enzyme; however, the purified enzyme contained the heterodisulfide reaction product, as opposed to the free cofactors found in eight prior M. acetivorans MCR structures, suggesting that substrate/product binding is altered in the modified enzyme. …”
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