Articles tagged with Misfolded Proteins
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A new study at Stanford University found a previously unknown cellular pathway for clearing misfolded proteins from the nucleus. This pathway could be a target for therapies of age-related diseases like Alzheimer's, Parkinson's, and Huntington's. Cells use this pathway to manage misfolded proteins in both the cytoplasm and nucleus.
Researchers discovered a misfolded alpha-synuclein protein as a potential biomarker for early detection of Parkinson's disease. The test was accurate in detecting the disease 87% of the time and identifying its absence 96% of the time.
Scientists have used gene therapy to increase 'cold shock protein' levels in mice brains, protecting them against prion disease. The approach could lead to a safer treatment for acute brain injury and prevention of neurodegenerative diseases like Alzheimer's.
Researchers found that gene therapy approach and small molecule treatment can calm the destructive cells of ALS by preserving upper motor neurons. Improving mitochondrial health also reduces astrocyte attack on diseased neurons, offering new hope for treating ALS.
Researchers modeled how genetic changes affecting protein synthesis speed can lead to misfolding and altered activity levels in proteins. This finding suggests the importance of kinetics alongside sequence for determining protein structure and function, with potential implications for fields such as biopharmaceutics and medicine.
Researchers found that synonymous mutations can lead to misfolding and reduced protein activity due to kinetic partitioning. The study suggests a new mechanism of action for these genetic changes, which could have implications in fields like biopharmaceutics.
Researchers have discovered that a specific mutation in the misfolding protein causing Parkinson's disease can also protect against multiple system atrophy (MSA), another fatal neurodegenerative disorder. The findings provide a promising lead for developing targeted treatments using personalized medicine approaches.
Researchers at University of Cambridge found that a thin shell of water surrounding proteins can determine aggregation, with slower movement leading to more clumping. The discovery has significant implications for treating protein misfolding diseases like Parkinson's and Alzheimer's.
Amanda Woerman's research aims to disrupt tau misfolding, a common thread in fatal neurodegenerative disorders PSP and CBD. The grant-funded study seeks to test a proof-of-concept gene therapy for these conditions, potentially leading to personalized medicine breakthroughs.
A new study reveals the molecular mechanism that causes prion proteins to take on their pathological form, paving the way for possible therapeutic options. The discovery highlights the structure of the human prion protein and its intermediate forms, enabling the design of new organic molecules to block disease progression.
Scientists at the Francis Crick Institute discovered how a build-up of harmful protein starts to happen within neurons in Parkinson's disease. The research found that misfolded alpha-synuclein clumps on the surface of mitochondria, causing holes and interfering with energy production.
A new study reveals that the protein CHIP can regulate insulin receptor signals more efficiently alone than in a paired state. This finding suggests that maintaining a balance between monomeric and dimeric states of CHIP is crucial for proper cellular function.
Researchers developed an immuno-infrared sensor that detects Alzheimer's disease biomarkers, including amyloid-beta misfolding, up to 17 years before clinical symptoms. The sensor shows high accuracy in identifying individuals at risk of developing Alzheimer's dementia.
A new study from UTHealth Houston found that whole blood exchange treatments decreased amyloid plaque formation in mice with Alzheimer's disease-causing amyloid precursor proteins. This approach has the advantage of treating the disease in the circulation instead of the brain, potentially bypassing the blood-brain barrier.
Scientists found a connection between the SARS-CoV-2 virus and the production of misfolded proteins called amyloids, which can cause complex symptoms and damage in organs such as the heart and kidneys. The researchers' discovery may help explain why COVID-19 often affects multiple parts of the body.
A Johns Hopkins Medicine study found that a protein called STING responds to clean-up signals in brain cells damaged by Parkinson’s disease by creating a cycle of inflammation that accelerates the disease’s progression. In mice with deactivated STING proteins, there was less microglial activity and brain cell death.
Researchers analyzed brain volumes of 37 Parkinson’s patients and 27 controls over 8.8 years, finding accelerated grey matter decline in temporal and occipital lobes. The study’s findings support Braak's disease stage scheme and provide new insights into Parkinson’s progression.
Researchers at the University of Cambridge have identified a new mechanism that appears to reverse the build-up of aggregates in neurodegenerative diseases, such as Alzheimer's and Parkinson's. By stressing cells, they found that protein misfolding was eliminated, potentially allowing for the refolding of correctly folded proteins.
Researchers have discovered a common thread between multiple neurodegenerative diseases, including Alzheimer's, dementia with Lewy bodies, and frontotemporal lobar degeneration. A protein called TMEM106B forms fibrils in diseased brain tissue, potentially hobbling cells.
Multiple system atrophy (MSA) is a fatal neurodegenerative movement disorder with no effective treatments, progressing rapidly and impairing critical physiological functions. The researchers will investigate how misfolded protein aggregates contribute to disease pathogenesis using the NIH grant.
Researchers at the University of Illinois used sonification to analyze data and teach protein folding, leading to a new discovery about protein folding mechanisms. Musicians collaborated with chemists to create audio-mapped visualizations that complemented traditional views, increasing intuition for experts.
Researchers found that non-mutated Apolipoprotein E was strongly enriched in dementia patients' brains, correlating with dementia diagnosis. Even those without the disease-driving APOE ε4 allele showed significant levels of ApoE peptides.
Aging leads to protein misfolding, which overwhelms the cell's quality control system. Ribosome dysfunction causes a snowball effect of dysfunction, leading to disease. Insights from yeast and roundworm models suggest a two-pronged situation where aging increases stalling and collisions, but the safety net is lost.
Researchers at the University of Bath have optimised a peptide that prevents alpha-synuclein misfolding, a key feature of Parkinson's disease. The new molecule, 4654W(N6A), has shown significant promise in lab experiments and could lead to the development of a disease-modifying treatment.
Researchers at Rice University have discovered a new mechanism by which prions can regulate protein synthesis in cells. The model proposes that prion aggregates and their monomers play a role in channeling RNA messages into new proteins, forming organized protein synthesis factories. This discovery has implications for our understandin...
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.
DZNE researchers found that viral molecules facilitate the intercellular spreading of protein aggregates, which are hallmarks of brain diseases like Alzheimer's. The presence of viral ligands increases protein aggregate spreading between cells, potentially contributing to neurodegeneration.
Researchers have discovered key insights into how toxic proteins are regulated in neurodegenerative diseases such as Alzheimer's and Parkinson's. Fasting has been found to dramatically increase the production of exophers, a type of neurotoxic protein, and three cellular pathways that contribute to this process have been identified.
A study found that boosting a cellular response to misfolded proteins actually shortens lifespan, contradicting previous research. The discovery highlights the complexity of aging and suggests new targets for disease prevention.
Scientists have found that misfolded tau protein accumulates RNA tags called N6-Methyladenosine (m6A) in nerve cells, leading to neurodegeneration. Inhibiting this RNA-tagging pathway shows promise as a potential approach to treat Alzheimer's disease.
Researchers at Penn Medicine discovered that restoring DAXX protein levels can prevent the misfolding of proteins associated with Alzheimer's disease and certain cancers. This finding could lead to new targeted approaches for treating these diseases, including reducing neurodegeneration and tumor growth.
Scientists developed a new mouse line to study protein balance and quality control in the mammalian brain. The research revealed that different neurodegenerative diseases have distinct protein misfolding patterns, offering insights into potential therapeutic options.
A study from Lund University reveals that Alzheimer's protein accumulates inside nerve cells, leading to increased production and potentially devastating effects. The research suggests that targeting misfolded amyloid-beta within cells may be a more effective approach than focusing on plaques outside the brain.
Researchers discovered that yeast changes hundreds of proteins' expression patterns and subcellular localizations after adapting to a higher temperature. The proteome's plasticity allows the cells to adapt by reducing thermolabile protein load, changing protein conformation, and adopting new functions.
Researchers mapped misfolded tau proteins' brain journey, finding they resist spread in certain areas. This discovery could lead to new therapies targeting specific brain regions.
University of Guelph researchers have discovered how entangled proteins in brain cells enable Parkinson's disease to spread. Misfolded alpha-synuclein aggregates spread to other parts of the brain, impairing areas responsible for motor function and cognition.
Research from CUHK reveals the counteracting relationship between Prpf19 and Exoc7, two crucial proteins in nerve cells. The study found that potentiating Prpf19's function degrades toxic SCA3-polyQ protein, alleviating neurodegeneration.
Scientists have found evidence of protein folding at the site of intracellular droplets, which are formed when fluids separate into microscopic droplets. This phenomenon is linked to increased potential for protein aggregation and misfolding, a hallmark of neurological diseases like Alzheimer's and ALS.
The study used thermal proteome profiling to analyze SARS-CoV-2 infection's impact on human proteins. Hundreds of cellular proteins showed changes in abundance and thermal stability, suggesting the virus hijacks them for replication.
The study describes a dynamic link between correct protein folding and amyloid fibril formation, highlighting the threshold of supersaturation that must be overcome. Supersaturation is a fundamental concept that advances the field of protein folding and may contribute to therapeutic strategies for neurodegenerative diseases.
Researchers have developed a simple skin test that can accurately diagnose Parkinson's disease by detecting clumping of the protein alpha-synuclein. The assay was tested on 50 skin samples from patients with Parkinson's disease, achieving high sensitivity and specificity rates, promising an earlier diagnosis and better clinical trials.
Researchers discovered a novel cellular mechanism for disposing of misfolded proteins in a rare condition called alpha1-antitrypsin deficiency, which can also affect neurological disorders like Alzheimer's. The study identified the human enzyme Man1b1 as key to degrading these proteins.
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.
Chinese researchers identify RNF126 as a key enzyme in the reubiquitination process, targeting misfolded membrane proteins for degradation. The study highlights the importance of this mechanism in maintaining normal cell physiology and potentially serving as a therapeutic target for cancer treatment.
A new study suggests that misfolded protein build-up in the gut may contribute to Alzheimer's-like symptoms in mice, potentially leading to a new treatment approach targeting the gut. The researchers found that beta amyloid proteins injected into the gut traveled to the nervous system and brain, causing cognitive impairments.
Researchers have created new antiviral molecules by designing synthetic amyloid peptides that can inactivate viral proteins, thereby interfering with viral replication. These 'Pept-ins' specifically target the influenza A and Zika virus proteins.
Researchers found that acetylation at lysine 16 leads to disordered aggregates with high toxicity, highlighting the importance of protein shape in amyloid beta toxicity. The study aims to better understand the complexity of misfolded proteins and their role in neurodegenerative diseases like Alzheimer's.
A new class of proteins, dubbed 'Hero', has been discovered that protects vulnerable proteins from aggregation and denaturation under extreme heat and other stresses. These flexible proteins may help prevent neurodegenerative diseases such as ALS and Huntington's disease by preserving molecular order.
Researchers identified a key strategy of cells to deal with misfolded proteins, where cells form aggregates to protect them from degradation. This approach is favored over fixing folding or destroying proteins, allowing for recovery under optimal conditions.
Researchers have discovered a new quality control system that allows cells to clear misfolded proteins from their surroundings. The Clusterin protein and heparan sulfate proteoglycans work together to bring misfolded proteins into cells for degradation, potentially leading to new therapeutic targets for neurodegenerative disorders like...
Researchers have developed a technology that can distinguish between Parkinson's disease and multiple system atrophy with high accuracy. The Protein Misfolding Cyclic Amplification (PMCA) test targets misfolded alpha-synuclein aggregates, allowing doctors to identify the correct disease and pursue timely treatment.
Researchers create two-modal fluorogenic probe to monitor protein aggregation, enabling detailed assessment of polarity and unfolded protein load. The NTPAN-MI probe offers a sharper picture of cellular stress responses, allowing for more accurate knowledge of crosstalk between components.
A team of scientists has developed a synthetic-molecule-based approach to isolate prion proteins in body fluids, paving the way for quick, noninvasive detection. The test also detects misfolded proteins associated with Alzheimer's and Parkinson's diseases.
Researchers add archaeal DNA to mouse models' genes to assess resistance to retinal degeneration and potentially develop new methods to prevent incurable eye diseases. The goal is to understand how molecular chaperones can help avoid misfolded proteins that cause blindness.
A new skin test using ultrasensitive technology may provide an early diagnosis of Alzheimer's and Parkinson's diseases, detecting misfolded proteins in skin samples. The RT-QuIC test is highly sensitive and specific, offering a promising tool for diagnosing and characterizing these neurodegenerative diseases.
A novel molecular mechanism has been discovered that underlies several genetic disorders, including MUC1 kidney disease, which results in a 'traffic jam' at the cellular shipping network. Researchers identified a compound called BRD4780 that can clear this traffic jam and prevent protein misfolding.
Researchers at the University of Toronto discovered a protein called HRI that can sense and respond to misfolded proteins in all mammalian cells. This finding opens promising research avenues for neurodegenerative disorders such as Parkinson's, Alzheimer's, and ALS.
Researchers detected and measured specific prion forms of amyloid beta (A-β) and tau proteins in human brain tissue, strongly associated with early-onset Alzheimer's disease. The findings suggest that active A-β and tau prions could drive the disease and prompt exploration of new therapies targeting prions.
A team of researchers has identified a protein complex called Lubac that marks misfolded proteins, stopping them from interacting with other proteins and directing them towards disposal. This discovery holds promise for the development of new therapeutic approaches to treat neurodegenerative diseases such as Alzheimer's and Parkinson's.