14 research outputs found
Not Available
Not AvailableFisheries resources of Nagaland: status and perspectivesNot Availabl
Bi-allelic variants in MTMR5/SBF1 cause Charcot-Marie-Tooth type 4B3 featuring mitochondrial dysfunction
Use of Spent Mushroom Substrate as an Inoculant Carrier and an Organic Fertilizer and Their Impacts on Roselle Growth (Hibiscus sabdariffa L.) and Soil Quality
Organic lettuce, rye/vetch, and Swiss chard growth and nutrient uptake response to lime and horse manure compost
Response of the population size and community structure of Paenibacillus spp. to different fertilization regimes in a long-term experiment of red soil
Hairy vetch, compost and chemical fertilizer management effects on red pepper yield, quality, and soil microbial population
Variation in the Phosphate Solubilizing Bacteria from Virgin and the Agricultural Soils of Punjab
Molecular modelling of mitofusin 2 for a prediction for Charcot-Marie-Tooth 2A clinical severity
Role of HSPB8 in the Proteostasis Network: From Protein Synthesis to Protein Degradation and Beyond
Proper protein folding is crucial for protein stability and function; when folding fails, due to stress or genetic mutations, proteins may become toxic. Cells
have evolved a complex protein quality control (PQC) system to protect against the toxicity exerted by aberrantly folded proteins, that may aggregate accumulating in various cellular compartments perturbing essential cellular activities, ultimately leading to cell and neuron death. The PQC comprises molecular chaperones, degradative systems (proteasome and autophagy) and components of the unfolded protein response. Prevention of protein aggregation, clearance of misfolded substrates and attenuation of translation, which decreases the amount of misfolding clients to levels manageable by the molecular chaperones, are all key steps for the maintenance of proteostasis and cell survival. In parallel, alterations of proteostasis may also (indirectly) influence RNA homeostasis; in fact, RNA-containing aggregates, known as stress granules, accumulate in cells with impaired PQC and
autophagy colocalizing with proteinaceous aggregates in several neurodegenerative diseases. Among the different molecular chaperones, here we will focus on the small heat shock protein HSPB8, which is expressed in neurons in basal conditions and upregulated in response to misfolded protein accumulation. HSPB8 exerts protective functions in several models of protein conformation neurodegenerative diseases. The putative sites of action of HSPB8 that confer HSPB8 pro-survival and anti-aggregation functions are discussed, as well as its potential role at the crossroad between proteostasis and ribostasis