Articles tagged with Presenilins
A study found that targeting heparan sulfate-modified proteins improves cell repair, rescues neuron loss and reverses cellular changes associated with neurodegenerative diseases. Disrupting these proteins promotes autophagy-dependent cell repair and reverses early cellular problems in models of Alzheimer's.
Researchers from Peter the Great Saint-Petersburg Polytechnic University found a substance that reduces the negative effect of mutations in genes related to neuronal contact formation. The discovery suggests promising compounds for anti-Alzheimer's drugs.
Researchers studying axonal transport may uncover new avenues for treating or preventing Alzheimer's. The UB lab, led by Shermali Gunawardena, investigates the role of presenilin in regulating brain cell traffic.
A new study suggests an association between overactive and cytosolic BRCA1 and neurons death in Alzheimer's disease, linked to aberrant DNA damage response and presenilin 1 dysfunction. The findings support the hypothesis that genotoxic stress manifests in neuronal death.
Researchers at Georgia Tech and Oak Ridge National Laboratory use neutron beams to illuminate presenilin, an intramembrane protease that chops protein building blocks. The study reveals a simpler protein structure than expected, with two chemical knives for cutting peptides.
Researchers at MGH and BWH identified the exact mechanism by which presenilin mutations in inherited Alzheimer's disease produce devastating effects. They found that these mutations decrease, rather than increase, function of the presenilin-1 protein and gamma-secretase enzyme.
A new study reveals that presenilin works with enzyme GSK-3ß to control material transport through neurons. Low levels of presenilin or high levels of GSK-3ß can cause uncoordinated movement, resulting in dangerous blockages. Researchers propose a potential pathway for early intervention through drugs.
A study by University at Buffalo researchers has identified a novel function of the protein presenilin in controlling the speed of molecular motors along neuronal highways. This regulation may prevent deadly blockages in neurodegenerative diseases like Alzheimer's, offering hope for new treatments.
Researchers found that presenilin helps guide embryonic motor neurons through a maze of chemical cues, ensuring they reach their targets. Without it, motor neurons misread guidance signals and get stuck in the spinal cord.
Fruit fly males with reduced Alzheimer's disease protein activity showed impairments in learning and memory as they aged. Researchers prevented age-related deficits by treating the flies with drugs like lithium or genetic manipulations that reduced nerve-cell signaling.
Mutations in the presenilin 1 gene disrupt cellular protein-recycling, killing nerve cells and leading to neuronal loss. Alternative pathways can be targeted for therapies aimed at repairing toxic protein elimination mechanisms.
A study published in the Journal of Cell Biology reveals that a mutated Alzheimer's-related protein called presenilin helps form and maintain nerve cell connections. The findings suggest that failing nerve transmission might be an early step in the disease's pathology.
Researchers have discovered a moss protein that may play a crucial role in preventing Alzheimer's disease. The study found that the moss protein has an evolutionary conserved function with human presenilin, suggesting that it may provide clues to its primary role in mammalian systems.
Recent mouse breeds designed to mimic Alzheimer's disease symptoms may not accurately reflect the human condition, according to a new study. The researchers suggest using alternative mouse breeds with only APP mutations to improve the accuracy of drug testing.
Researchers discovered that presenilins act as calcium channels, controlling the balance of calcium within cells. This finding may suggest a new avenue for treating Alzheimer's disease by restoring normal calcium levels. The study also highlights the potential for combination therapies targeting both amyloid and calcium signaling.
Researchers used fruit fly models to study the effects of 14 different Presenilin mutations, finding a correlation between mutation severity and age of onset in human patients. The study supports the view that Presenilin activity affects clinical heterogeneity in early-onset Alzheimer's disease.
Researchers at Howard Hughes Medical Institute have identified a crucial protein called TMP21 that regulates amyloid-beta production. By controlling the specific cleavage of APP, TMP21 helps keep amyloid-beta levels in check, preventing the formation of toxic plaques. This discovery may lead to new treatments for Alzheimer's disease.
Researchers found one presenilin gene mutation associated with variable age of onset AD (from 35 to 85 years old) and two new presenilin gene mutations linked to early onset AD at age 49 to 54 years old. The study confirms the clinical manifestation of PS1 and PS2 gene mutations in Alzheimer's disease is similar to other dementias.
Researchers found that gamma-secretase cleaves both amyloid precursor protein (APP) and Notch interchangeably, treating them as interchangeable substrates. The study suggests a new approach to inhibiting gamma-secretase activity without interfering with its role in Notch signaling.
Researchers identified a specific mutation in the presenilin 1 gene that increases beta amyloid expression, a hallmark of Alzheimer's disease. The study found 18 unrelated families with the same mutation, suggesting a common ancestral origin.
Scientists at University of Maryland Biotechnology Institute discover ubiquilin controls levels of proteins central to early development of Alzheimer's disease. The molecule increases presenilin levels in cells, a key step in understanding the disease.
Scientists have discovered a biochemical connection between presenilin and Notch, a protein controlling crucial aspects of developmental biology. This link may lead to new insights into the causes of Alzheimer's disease.
Researchers at Johns Hopkins Medicine have identified a protein glitch as an early problem in inherited Alzheimer's disease. Presenilin normally cleaves in two, but a disease-causing mutation can prevent this crucial change. This study may lead to new treatments by targeting the point of cleavage with drugs or other interventions.