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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Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function. by Melody D Fulton, Danielle J Yama, Ella Dahl, Jill L Johnson

“…Our results provide further evidence that Hsp90 contributes to proteostasis not just by assisting protein folding, but also by enabling accurate translation of newly synthesized proteins. …”
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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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Endoplasmic Reticulum Is at the Crossroads of Autophagy, Inflammation, and Apoptosis Signaling Pathways and Participates in the Pathogenesis of Diabetes Mellitus by Jing Su, Lei Zhou, Xiaoxia Kong, Xiaochun Yang, Xiyan Xiang, Yu Zhang, Xiaoning Li, Liankun Sun

“…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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Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice by José Belizário, Luiz Vieira-Cordeiro, Sylvia Enns

“…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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Magnetic tweezers to capture the fast-folding λ6-85 in slow motion by César Augusto Quintana-Cataño, Ann Mukhortava, Mordjane A. Boukhet, Andreas Hartmann, Karl-Ludwig Schumann, Michael Schlierf

“…Abstract Force spectroscopy gives access to the underlying free energy landscape of protein folding. Proteins exhibit folding rates between microseconds and hours. …”
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Synthesis and Experimental Validation of New PDI Inhibitors with Antiproliferative Activity by Mariateresa Badolato, Gabriele Carullo, Francesca Aiello, Antonio Garofalo

“…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 by Michelle T. Barati, James C. Gould, Sarah A. Salyer, Susan Isaacs, Daniel W. Wilkey, Michael L. Merchant

“…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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Gene expression signatures between Limia perugiae (Poeciliidae) populations from freshwater and hypersaline habitats, with comparisons to other teleosts. by Elizabeth J Wilson, Nick Barts, John L Coffin, James B Johnson, Carlos M Rodríguez Peña, Joanna L Kelley, Michael Tobler, Ryan Greenway

“…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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The Passage of Chaperonins to Extracellular Locations in <i>Legionella pneumophila</i> Requires a Functional Dot/Icm System by Peter Robertson, David S. Allan, Rafael A. Garduño

“…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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Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy by Atta Mohammed Alzebari, Amjad Mahmood Qadir, Mahmood Sherzad Rafaat, Abbas Salihi

“…The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape. …”
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Lipid Oxidation at the Crossroads: Oxidative Stress and Neurodegeneration Explored in <i>Caenorhabditis elegans</i> by Julia Tortajada-Pérez, Andrea del Valle Carranza, Cristina Trujillo-del Río, Mar Collado-Pérez, José María Millán, Gema García-García, Rafael Pascual Vázquez-Manrique

“…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 by David M. Smadja, David M. Smadja, M. Marc Abreu, M. Marc Abreu

“…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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Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions by Zeming Wang, Wei Zhang, Xiaojie Hu, Yanzheng Gao

“…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 by E. A. Dyachenko, M. A. Slugina

“…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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Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis by Célia Alecki, Javeria Rizwan, Phuong Le, Suleima Jacob-Tomas, Mario Fernandez Comaduran, Morgane Verbrugghe, Jia Ming Stella Xu, Sandra Minotti, James Lynch, Jeetayu Biswas, Tad Wu, Heather D. Durham, Gene W. Yeo, Maria Vera

“…Abstract Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. …”
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Nanoplastics induces arrhythmia in human stem-cells derived cardiomyocytes by Shirley Pei Shan Chia, Jeremy Kah Sheng Pang, Winanto Winanto, Boon-Seng Soh

“…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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Review on the Injury and Repair Mechanism of Skeletal Muscle Contusions by LIN Jianping, WANG Hao, GUO Mingling, WANG Shizhong, CHEN Shaoqing

“…Ca²⁺ dysregulation contributes to abnormal protein production by promoting mitochondrial reactive oxygen species (ROS) production and disrupting protein folding in the ER, thus, the abnormal folding protein in the ER is increased. …”
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Comprehensive analysis of heat shock protein 110, 90, 70, 60 families and tumor immune microenvironment characterization in clear cell renal cell carcinoma by Wenjing Liao, Mao Huang, Xiaoyi Du, Liangdan Tang, Junwu Li, Qin Tang

“…Abstract Heat shock proteins (HSPs) are a kind of molecular chaperone that helps protein folding, which is closely related to cancer. However, the association between HSPs and clear cell renal clear cell carcinoma (ccRCC) is uncertain. …”
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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 by Gulam Altab, Brian J. Merry, Charles W. Beckett, Priyanka Raina, Inês Lopes, Katarzyna Goljanek-Whysall, João Pedro de Magalhães

“…Upregulated genes were commonly involved in protein folding and immune responses; meanwhile, downregulated genes were often related to developmental biology. …”
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