ER Dysfunction and Protein Folding Stress in ALS by Soledad Matus, Vicente Valenzuela, Danilo B. Medinas, Claudio Hetz

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The Mitochondrial Disulfide Relay System: Roles in Oxidative Protein Folding and Beyond by Manuel Fischer, Jan Riemer

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Severe deviation in protein fold prediction by advanced AI: a case study by Jacinto López-Sagaseta, Alejandro Urdiciain

“…AlphaFold is remarkable in this arena for its outstanding accuracy in modelling proteins fold based solely on their amino acid sequences. …”
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Identification of Protein Folding Cores Using Charge Center Model of Protein Structure by Ivan Y. Torshin, Robert W. Harrison, Irene T. Weber, John M. Petock

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Revisiting 310-helices: biological relevance, mimetics and applications by Diego Núñez-Villanueva

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Endoplasmic Reticulum Stress in Intestinal Epithelial Cell Function and Inflammatory Bowel Disease by Katherine Luo, Stewart Siyan Cao

“…In eukaryotic cells, perturbation of protein folding homeostasis in the endoplasmic reticulum (ER) causes accumulation of unfolded and misfolded proteins in the ER lumen, which activates intracellular signaling pathways termed the unfolded protein response (UPR). …”
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Distinct patterns of prion strain deposition and toxicity in a novel whole brain organotypic slice culture system by Hailey Pineau, Valerie L. Sim

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Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy by Axel H. Schönthal

“…The endoplasmic reticulum (ER) is a multifunctional organelle required for lipid biosynthesis, calcium storage, and protein folding and processing. A number of physiological and pathological conditions, as well as a variety of pharmacological agents, are able to disturb proper ER function and thereby cause ER stress, which severely impairs protein folding and therefore poses the risk of proteotoxicity. …”
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Concentration-dependent effect of norfloxacin on iron toxicity in the intestine of large yellow croaker Larimichthys crocea (Richardson, 1846) by Lin Zeng, Yong-Hong Wang, Chun-Xiang Ai, Bin Liu, Bin Liu, Min-Hui Yu, Hui Zhang, Fei Li

“…Compared to Fe alone exposure, Fe plus LNOR exposure decreased MDA, PC, and mortality rate, and alleviated intestinal malformations by improving Fe transport, energy metabolism, anti-inflammatory response, and protein folding protective effect, and reducing pro-inflammatory response, indicating that LNOR had an antagonistic effect on Fe toxicity. …”
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Illuminating the impact of N-terminal acetylation: from protein to physiology by Nina McTiernan, Ine Kjosås, Thomas Arnesen

“…We also provide an overview of the impact of N-terminal acetylation, including its effects on protein folding, subcellular targeting, protein complex formation, and protein turnover. …”
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UPR-Mediated Membrane Biogenesis in B Cells by Joseph W. Brewer, Suzanne Jackowski

“…The unfolded protein response (UPR) can coordinate the regulation of gene transcription and protein translation to balance the load of client proteins with the protein folding and degradative capacities of the ER. …”
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Psychrophilic Enzymes: From Folding to Function and Biotechnology by Georges Feller

“…Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. …”
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AI, big data, and robots for the evolution of biotechnology by Haseong Kim

“…Additionally, AlphaFold, a technology resembling the AI AlphaGo for the game Go, has surpassed the limit on protein folding predictions—the most challenging problems in the field of protein biology. …”
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The known unknowns of the Hsp90 chaperone by Laura-Marie Silbermann, Benjamin Vermeer, Sonja Schmid, Katarzyna Tych

“…Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. …”
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From Interfacial Water to Macroscopic Observables: A Review by Alberto Striolo

“…Interfacial water plays an important role in a number of physical phenomena that include protein-folding, structure/function relationships in enzymes, the design of nano-fluidic devices, and even macroscopic effects including drag reduction. …”
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Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells by Rosa E. Hansen, Mieko Otsu, Ineke Braakman, Jakob R. Winther

“…To accommodate this load on the secretory machinery, the differentiation of resting B cells into antibody-secreting plasma cells is accompanied by a preferential expansion of the secretory compartments of the cells and by an up-regulation of enzymes involved in redox regulation and protein folding. We have quantified the absolute levels of protein thiols, protein disulfides, and glutathionylated proteins in whole cells. …”
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Linking ER Stress to Autophagy: Potential Implications for Cancer Therapy by Tom Verfaillie, Maria Salazar, Guillermo Velasco, Patrizia Agostinis

“…Different physiological and pathological conditions can perturb protein folding in the endoplasmic reticulum, leading to a condition known as ER stress. …”
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S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor α Stability and Function by Ying Xiong, Yefim Manevich, Kenneth D. Tew, Danyelle M. Townsend

“…We have shown that S-glutathionylation of protein disulfide isomerase (PDI) disrupts protein folding and leads to the activation of the unfolded protein response (UPR). …”
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Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy by Tjaša Goričan, Simona Golič Grdadolnik

“…Human heat shock protein 90 (Hsp90) is one of the most important chaperones that play a role in the late stages of protein folding. Errors in the process of the chaperone cycle can lead to diseases such as cancer and neurodegenerative diseases. …”
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Key Role of Phosphorylation in Small Heat Shock Protein Regulation via Oligomeric Disaggregation and Functional Activation by Zachary B. Sluzala, Angelina Hamati, Patrice E. Fort

“…Heat shock proteins (HSPs) are essential molecular chaperones that protect cells by aiding in protein folding and preventing aggregation under stress conditions. …”
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