Sökning: "Bri2"
Visar resultat 1 - 5 av 10 avhandlingar innehållade ordet Bri2.
1. Of spiders, bugs, and men : Structural and functional studies of proteins involved in assembly
Sammanfattning : Protein assembly enables complex machineries while being economical with genetic information. However, protein assembly also constitutes a potential threat to the host, and needs to be carefully regulated.Sulfate is a common source of sulfur for cysteine synthesis in bacteria. LÄS MER
2. Islet Amyloid Polypeptide: Interaction with Amyloid Beta, Alpha-Synuclein and BRICHOS
Sammanfattning : Amyloid, the congophilic deposits of misfolded protein, are pathological hallmarks of many common diseases, among others, Alzheimer’s disease (AD), Parkinson’s disease (PD), and type 2 diabetes (T2D). Amyloid beta (Aβ) forms senile plaques in AD, alpha-synuclein (aSyn) forms Lewy bodies and Lewy neurites in PD, islet amyloid polypeptide (IAPP) forms islet amyloid in T2D. LÄS MER
3. Recombinant BRICHOS domains delivered over the blood-brain barrier : a possible way to treat Alzheimer’s disease
Sammanfattning : One of the current major challenges to treat neurological diseases is the ability of drug candidates to cross the blood-brain barrier (BBB). Alzheimer´s disease (AD) is the most common form of dementia worldwide, affecting more people every year due to a world where the average lifespan is increasing. LÄS MER
4. Molecular basis for chaperone activities of the BRICHOS domain against different types of clumpy clients : a route to prevent amyloid toxicity
Sammanfattning : Protein aggregation is a hallmark of a wide range of human disorders, including Alzheimer’s disease and type II diabetes, and are often associated with imbalances in the cellular protein homeostasis. Molecular chaperones play an important role in modulating proteostasis and thereby counteract toxic consequences of misfolded or aggregated proteins. LÄS MER
5. Studies of amyloid toxicity in Drosophila models and effects of the BRICHOS domain
Sammanfattning : Amyloid diseases involve specific protein misfolding events and formation of fibrillar deposits. The symptoms of these diseases are broad and dependent on site of accumulation, with different amyloid proteins depositing in specific tissues or systematically. LÄS MER