Articles tagged with Unfolded Protein Response
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Scientists have created a high-potency IRE1 inhibitor with a unique inhibition mode that targets the unfolded protein response in cancer cells. This compound binds to the kinase pocket of IRE1, allosterically suppressing its RNAse activity and restoring proper protein folding.
Researchers identify three primary UPR pathways and their downstream cascades, which play a crucial role in the differentiation of osteoblasts and osteoclasts. Targeting these pathways with emerging drugs may alleviate bone-related events and kill tumors localized in bones.
Three Sanford Burnham Prebys faculty members, David A. Brenner, Randal J. Kaufman, and Tariq M. Rana, are recognized for their significant scientific influence. Their publications have been cited top 1% globally by number of citations.
A study from the University of California, Berkeley, shows that nematodes react to pathogenic bacteria by destroying mitochondria to protect against iron-stealing bacteria. This protective response suggests that humans may also respond to the smell of pathogens to prepare their gut for infection.
Researchers found that impaired mitochondrial unfolded protein response causes accelerated telomere shortening in both oocytes and somatic cells of aging mice. This study highlights the link between loss of mitochondrial protein homeostasis, infertility, and somatic aging.
Research found that nematodes can sense danger by smell, triggering a neural circuit that induces a response in other tissues, leading to a longer lifespan and less protein aggregation. The study suggests that manipulating perceptions of chemical substances could be a route to intervention in neurodegenerative diseases.
A team of researchers from Goethe University Frankfurt has discovered a central switch point in the mitochondrial signaling chain under misfolding stress. The mitochondria send two chemical signals to the cell when protein misfolding stress occurs, triggering a protective response that reduces misfolded proteins and stabilizes membranes.
Researchers discuss chemotherapeutic resistance in recurring ovarian cancer, focusing on the unfolded protein response and its effect on polyploid giant cancer cells. Understanding this mechanism could lead to investigating cancer cell molecular mechanisms and potential therapeutic strategies.
A new study by researchers at Florida Atlantic University explored the effects of resistance training on older adults' cellular level. The study found that resistance training did not significantly affect inflammatory proteins or redox balance markers, but showed a significant reduction in a specific protein ratio. This may support the...
Scientists at NTU Singapore have found that a stress response in cells, when 'switched on' at a post-reproductive age, could be the key to slowing down aging. The study showed that this stress response extended the lifespan of roundworms fed a high-glucose diet.
SLFN11 acts as a surveillance factor for protein homeostasis by alleviating proteotoxic stress derived from protein synthesis and maturation. Its lack makes cells vulnerable to anticancer drugs inducing ER and proteotoxic stress, leading to chemoresistance. SLFN11 is also involved in regulating immune response and inflammation.
Researchers discovered a novel form of gene regulation altered in bladder cancer, which boosts the unfolded protein response pathway to help cancer cells survive during rapid growth. Elevated TRMT6/61A enzyme levels prevent tRF-3bs from silencing genes in this pathway.
A team of scientists has identified a compound that shows promise in easing COVID-19 symptoms by targeting the cellular quality-control system damaged by coronaviruses. The compound, AMG PERK 44, was found to halt virus replication and boost lung function in mice infected with MERS.
Researchers describe how cancer cells exploit genetic and cellular processes to promote tumor survival and growth. The study found that aneuploidy, a condition of abnormal chromosome number, intersects with the stress response mechanism in cancer cells, leading to immune cell dysregulation.
Researchers discovered periplocin, a potent inhibitor of the IRE1-XBP1 axis, which suppresses the unfolded protein response (UPR). Cardiac glycosides, commonly used for cardiac insufficiency therapy, also exhibited similar UPR-suppressing effects.
A recent study published in Nature Communications reveals the Unfolded Protein Response (UPR) regulon, a comprehensive list of genes activated to promote cell survival under stress. The researchers discovered that changes in one-carbon metabolism, relying on vitamin folate as a cofactor, contribute to chemoresistance in cancer cells.
Non-syndromic Dentinogenesis Imperfecta is characterized by discolored teeth with a blue-gray or yellow-brown color and translucent appearance. Chronic Unfolded Protein Response (UPR) may be associated with the disorder, caused by mutant dentin sialophosphoprotein (DSPP) gene mutations.
An international team of researchers identified a specific mechanism leading to Zika virus-associated microcephaly, involving protein misfolding and endoplasmic reticulum stress. This triggers the unfolded protein response, promoting apoptosis in neuronal cells and reducing cortical neuron development.
Researchers discovered that corals activate ancient genes when exposed to stressful conditions, which could serve as an early warning sign for coral bleaching events. This study provides a new way to monitor coral health and predict bleaching events, potentially helping scientists identify and map survivor coral colonies worldwide.
Researchers at the University of Tokyo identified a novel biomarker to monitor acute kidney injury, while a study found that the unfolded protein response contributes to nerve cell death in Alzheimer's Disease. Additionally, a bacterial toxin disrupts intestinal epithelial barrier function, leading to systemic infection.
Researchers at Scripps Research Institute identify a mutation in the Mbtps1 gene that increases susceptibility to inflammatory bowel disease. The study reveals how the mutated gene disrupts the unfolded protein response, leading to cellular stress and inflammation.
Research from Rockefeller University reveals that unfolded protein response serves a protective role, shielding cells from death. The study focuses on autosomal dominant retinitis pigmentosa, where unfolded proteins accumulate in the endoplasmic reticulum, indicating their protective mechanism.