Scientists have identified a conserved aging-related protein, EPS8, that promotes toxic protein aggregation linked to neurodegenerative diseases.
An Oregon State University scientist and a team of undergraduate students have uncovered real-time insights into a chemical process linked with Alzheimer's disease, paving the way toward better drug ...
Clearance mechanisms are key to removing aggregates and maintaining metastability.
Raghu R. Chivukula, MD, Ph.D., a physician-investigator in the Departments of Medicine & Surgery and the Center for Genomic Medicine at Massachusetts General Hospital and Harvard Medical School, is ...
A new large-scale study has mapped the first molecular events that drive the formation of harmful amyloid protein aggregates found in Alzheimer’s disease, pointing towards a new potential therapeutic ...
The accumulation of misfolded proteins in the brain is central to the progression of neurodegenerative diseases like Huntington’s, Alzheimer’s and Parkinson’s. But to the human eye, proteins that are ...
Neurodegenerative diseases, such as Alzheimer's disease and dementia, are medical conditions that entail the progressive loss of neurons and a decline in brain function. Past studies have found a link ...
Protein-based therapeutics have transformed treatments for numerous diseases, yet their production remains highly complex and cost-intensive [1][2],[3][4]. Downstream processing (DSP), including ...
Coacervates are dense protein droplets that form spontaneously in cells through a process called phase separation 1. These droplets have key roles in various biological phenomena, but an understanding ...
An AI tool has made a step forward in translating the language proteins use to dictate whether they form sticky clumps similar to those linked to Alzheimer's Disease and around fifty other types of ...
CGSchNet, a fast machine-learned model, simulates proteins with high accuracy, enabling drug discovery and protein engineering for cancer treatment. Operating significantly faster than traditional all ...