Articles tagged with Proteasomes
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Researchers discovered that brain enzyme OTULIN regulates tau protein accumulation and has implications for treating neurodegenerative diseases. The study revealed OTULIN's role in controlling gene expression and RNA metabolism, suggesting a potential therapeutic target.
Increasing PI31 levels demonstrates neuroprotective effects in mice, preventing neuronal degeneration and restoring synaptic function. The study also shows promise for treating Alzheimer's and slowing age-related cognitive decline.
A study by the Center for Redox Processes in Biomedicine presents a valuable new experimental model for investigating the interaction between the proteasome and mitochondrial function. The proteasome plays a role in protein quality control, while mitochondrial metabolism affects protein degradation efficiency.
A new study reveals that protein sources in an animal's diet significantly alter the gut microbiome, with some having extreme effects. The researchers found that diets high in brown rice, yeast, or egg whites led to changes in amino acid metabolism and complex sugar degradation.
A new study from Weizmann Institute of Science reveals an immune mechanism involving proteasome products, which can kill bacteria and offer a promising treatment for infections. The researchers discovered that certain peptides produced by the proteasome have antibacterial properties and can be used to develop personalized treatments.
Scientists at Sanford Burnham Prebys have developed a clearer picture of how crucial machinery in the human cell's recycling process for obsolete and misshapen proteins—known as proteasomes—are formed. The research team shed new light on how two protein chaperones bind on the top of the alpha subunit ring as it is constructed.
Researchers found proteasomes in neurons near the skin that convey sensory signals from the central nervous system. The protein grinds down proteins and helps differentiate between pain and itch sensation.
A new study published in Nature Communications has provided structural insights into a potent antimalarial drug candidate's interaction with the malaria parasite Plasmodium falciparum. The research suggests that the drug, TDI-8304, can selectively target and kill resistant parasites, offering hope for more effective treatments against ...
Researchers develop a novel protein killer and discover a new ligase for PROTACs, which can specifically target and degrade pathological proteins in specific tissues. This breakthrough could enable the targeted degradation of proteins in tumors.
Researchers at Mass General Brigham have developed a new class of proteasome inhibitors that specifically target the β2 active site in cancer cells. The newly synthesized compounds effectively inhibit multiple myeloma cell growth and show promise for reducing therapeutic resistance and side effects when combined with existing drugs.
Researchers have uncovered the intricate molecular mechanism used by parasitic phytoplasma bacteria to manipulate plants. The discovery sheds light on a peculiar phenomenon in nature, where plants exhibit 'zombie-like' effects due to bacterial infection.
A recent study reveals that the transcription factor NRF1 activates aggrephagy, a protein clearance process, in response to proteasome dysfunction. This mechanism helps maintain proteostasis and has major implications for treating degenerative diseases such as Alzheimer's, Parkinson's, and dementia with Lewy bodies.
Researchers identified midnolin as a protein that degrades short-lived nuclear proteins by directly grabbing them and pulling them into the proteasome. This mechanism is crucial for genes related to brain function, immune system, and development.
Research reveals that cold activates cellular cleansing mechanisms that break down protein clumps, preventing age-related diseases like Alzheimer's and Parkinson's. By modulating proteasome activity, scientists have found a potential therapeutic target for aging and related neurodegenerative disorders.
Researchers at CNIO have identified epigenetic changes, specifically DNA methylation, as a key mechanism behind resistance to proteasome inhibitor drugs in multiple myeloma. This finding suggests that methylation levels in the PSMD5 gene can predict treatment response and potentially reverse resistance.
Researchers uncover critical shape-change in cereblon protein that CELMoD drugs must cause to work effectively. The finding enables the development of more effective cancer-fighting treatments.
Heidelberg University researchers have identified a key protein HYPK that regulates N-terminal acetylation, prolonging plant protein life and enhancing drought resistance. This mechanism appears to be ancient, retained across various organisms.
A research team led by Professor Youdong Mao has developed a new method using time-resolved cryo-electron microscopy and machine learning-based 4D reconstruction to visualize the USP14-proteasome system in atomic detail. This reveals a 'multiverse' of parallel reality pathways, allowing for targeted inhibition of cancer cells.
Researchers discovered that under stress conditions, proteasome molecules assemble into structures that induce cell death, a process linked to apoptosis and potentially preventing cancer. The study highlights the importance of understanding the normal functioning of cells and their connections to cancer development.
The study reveals that FBS2 protein is responsible for the lethality in NGLY1-knockout mice, causing cell growth suppression and accumulation of ubiquitinated glycoproteins. The absence of NGLY1 leads to proteasome inhibition, resulting in cell death.
Researchers have clarified the regulatory mechanism of the ubiquitin-proteasome system in recognizing and repairing DNA damaged by ultraviolet light. The study reveals that proteasomes' protein degradation activity and architectural integrity are involved in regulating DDB2 protein-mediated DNA damage repair.
A team of researchers has discovered how an enzyme called UCH37 helps cells get rid of damaged proteins. By removing branchpoints from ubiquitin chains, UCH37 allows proteins to be degraded more efficiently, which could lead to new cancer treatments.
Scientists have created a light-activated chemical inhibitor that can control two fundamental cellular processes: cell division and cell death. This innovation has significant implications for studying cellular functions, understanding medical disorders, and designing new therapeutic strategies.
Research suggests that different α-synuclein aggregate conformations lead to distinct pathologies in neurodegenerative diseases. Suzuki et al. found that α-synuclein fibrils (-) inhibit proteasome activity, leading to accumulation of phosphorylated α-synuclein and ubiquitinated proteins.
Researchers efficiently synthesized cepafungin I, a natural compound with promise as an anti-cancer agent, using a lean new process that overcame its complex molecular structure. The compound targets the proteasome, a strategy used by many existing cancer medications.
Researchers found that PDE5 inhibitors like sildenafil can enhance the activity of the proteasome, a cell's garbage disposal system, to reduce misfolded proteins. This approach may help combat neurodegenerative diseases such as Alzheimer's and Parkinson's.
Researchers discovered a novel mode of protein degradation by the UPS under hyperosmotic stress. The proteasome forms nuclear foci that exhibit liquid-like behavior and contain ubiquitylated substrates, facilitating protein degradation. RAD23B is identified as a key molecule that induces phase separation of ubiquitylated proteins.
Researchers identified mutations that improve photosynthesis in Arabidopsis thaliana by reducing protein degradation and increasing chlorophyll production. The findings suggest a potential mechanism to enhance plant energy efficiency and biomass production.
Researchers found that protein clumps in the brain are caused by transportation failures of proteasomes, a molecular machinery that breaks down proteins. Without proper transport, damaged proteins accumulate and disrupt cell function, leading to degeneration and cell death.
Researchers identified two P. falciparum-selective proteasome inhibitors with potent antimalarial activity against drug-resistant parasites. The inhibitors exhibited low propensity for generating resistance and synergized with multiple antimalarial agents.
Scientists have discovered a previously unknown mechanism by which cells sense proteasome dysfunction and respond by editing the amino acid sequence of a key sensing protein. This finding has important applications for treating cancer, aging, and neurodegenerative diseases.
Researchers at Florida State University have found a critical missing step in proteasome assembly, which could be targeted to treat certain types of cancers. By manipulating this step, scientists may be able to regulate proteasome assembly and mitigate cancer-causing effects.
Researchers used cryo-EM to visualize the dynamic process of substrate processing in the human proteasome at unprecedented resolution, revealing single magnesium ions bound to ATP and ADP. The study provides novel insights into the complete cycle of substrate processing and suggests distinct modes of ATP hydrolysis.
A study from Harvard Medical School reveals that intense exercise, fasting, and hormones can activate the body's built-in protein disposal system, enhancing its ability to remove toxic, misfolded proteins. This mechanism is triggered by fluctuations in hormone levels, allowing cells to adapt to changing conditions.
Biologists have visualized the inner workings of cellular 'undertaker' proteasomes using cryo-electron microscopy. The study reveals how ATP powers movements within the motor that enable it to pull in proteins, providing insights into neurogenerative diseases like Parkinson's and Alzheimer's, as well as cancer therapy.
A novel technology for profiling protein turnover and degradation has been developed, revealing distinct evidence of a signature pattern in autoimmune disorders. The technique focuses on degraded proteins, providing clues about the state of protein monitoring and potentially leading to better diagnostic techniques.
Researchers found specialized proteasomes target specific proteins involved in neuronal signaling and regulation. These proteins include Fos and Npas4, critical for active neurons, suggesting a connection between protein synthesis and degradation with independent roles in the cell.
The proteasome complex has been found to regulate DNA packing in the nucleus, influencing gene expression. In yeast cells, the proteasome can induce heterochromatin formation but prevent its spread, suggesting an alternative mechanism of action beyond proteolysis.
Researchers have discovered a way to activate the proteasome in CD8+ T cells, generating more long-lived memory cells that can provide lifelong protection. This approach could be used as an adjuvant therapy to enhance vaccine and immunotherapy effectiveness.
Researchers discovered proteasomes embedded in nerve cell membranes, degrading proteins and expelling peptides that carry essential signals. This finding suggests a new role for proteasomes in cell-to-cell communications and raises questions about neurological disease.
A new compound developed by the Deshaies group inhibits Rpn11 activity, causing massive accumulation of dysfunctional proteins in cancer cells. This leads to catastrophic stress and cell death, making it a promising alternative to existing cancer drugs.
Researchers at UC Davis have made significant discoveries about the complex process of meiosis, where chromosomes undergo a intricate dance to produce sperm and eggs. The team found that SUMO and ubiquitin proteins play a crucial role in selecting crossover sites, allowing for accurate chromosome distribution.
Researchers at Brown University have developed a new compound that can render Mycobacterium tuberculosis susceptible to the immune system. The compound inhibits the bacterial proteasome, making proteins damaged by nitric oxide accumulate and cause bacteria death.
Scientists at TUM have determined the molecular mechanisms of inhibitors that can selectively thwart the human immunoproteasome. This could lead to the development of new drugs for autoimmune diseases like rheumatoid arthritis and type 1 diabetes.
MGH researchers discovered the role of DDI-1 and PNG-1 in sensing proteasome stress, with potential applications in cancer treatment and Alzheimer's disease. The findings suggest boosting proteasome activity could help treat conditions characterized by abnormal protein deposits.
A team of scientists has determined the 3D structure of the human proteasome in unprecedented detail, revealing its exact mechanism and a crucial role for a previously unknown chemical reaction. This knowledge will pave the way to develop more effective cancer therapies by optimizing inhibitor design and efficacy.
Cells have two disposal systems: proteasomes, which handle smaller proteins, and autophagy, a process that removes larger complexes. Researchers discovered a smart bin liner-like system in autophagy, involving Cue5 receptors and Hsp42 chaperones.
Researchers at Scripps Research Institute and UC Berkeley have made a breakthrough in understanding the proteasome, a molecular machine responsible for breaking down toxic proteins. The new study reveals how a crucial enzyme, Rpn11, is activated to remove harmful proteins from cells, providing potential new therapies for diseases such ...
Researchers discover a new treatment approach to neurodegenerative diseases like Alzheimer's, Huntington's and Parkinson's. A drug called rolipram boosts the activity of the proteasome, which clears out toxic proteins from the brain.
A study published in Nature Medicine found that enhancing proteasome activity with drugs during early stages of Alzheimer's disease may prevent dementia and reduce brain damage. Researchers identified a potential therapeutic target, rolipram, which activates the proteasome system to clear out toxic proteins.
Researchers at Helmholtz Munich have discovered that increased protein turnover by the 26S proteasome is responsible for the activation of myofibroblasts, leading to pulmonary fibrosis. Inhibiting the 26S proteasome can prevent differentiation of primary human lung fibroblasts into myofibroblasts.
A Kansas State University-led study identified an 'affinity switch' that regulates the formation of proteasomes, complexes responsible for protein degradation. This discovery may provide new target sites for drugs and improve human health by understanding how cells assemble these molecular machines.
Scientists have visualized protein degradation in intact nerve cells for the first time, shedding light on how proteasomes remove defective proteins. The study reveals that only a minority of proteasomes are actively degrading proteins in quiescent cells.
Researchers have visualized protein degradation in intact nerve cells for the first time, using electron cryo-tomography to distinguish single proteasomes within the cell. The study reveals that only a minority of proteasomes are actively degrading proteins, with most remaining idle.
Researchers have discovered a new mechanism for inhibiting the immunoproteasome, a protein complex involved in autoimmune disorders such as rheumatism and multiple sclerosis. The found mechanism involves a novel compound that selectively targets and deactivates the immunoproteasome without affecting other proteasomes.
Researchers discovered a new mechanism to inhibit proteasomes, a target for cancer therapy, paving the way for more effective and less toxic chemotherapy drugs. A series of molecules based on this mechanism have been developed, and their potential is being tested.
A Wayne State University professor has received a nearly $1.7 million grant from the National Institutes of Health to investigate proteasome and parkin as potential pharmaceutical drug targets for treating methamphetamine-abuse related neurotoxicity.
Researchers at Duke University Medical Center have identified a potential treatment approach for ciliopathies, a group of rare genetic disorders. The study found that bolstering the function of the proteasome system can correct physical damage caused by defective cilia, offering new hope for therapies.
Researchers have discovered novel compounds that fine-tune the activity of cells' protein-disposing machinery, which can help target solid tumors. These 'allosteric regulators' show promise as anti-cancer therapies without inducing drug resistance.
Researchers have identified a key proteasome regulatory mechanism that affects cellular protein balance and may hold promise for treating neurodegenerative diseases. Decreased insulin/IGF-1 signalling increases proteasome activity, accelerating protein degradation and cell death.