Results 141 to 150 of about 67,514 (293)
Mechanisms of selenomethionine developmental toxicity and the impacts of combined hypersaline conditions on Japanese medaka (Oryzias latipes). [PDF]
Selenium (Se) is an essential micronutrient that can cause embryotoxicty at levels 7-30 times above essential concentrations. Exposure to hypersaline conditions and 50 μM selenomethionine (SeMet) decreased embryo hatch and depleted glutathione in ...
Kupsco, Allison, Schlenk, Daniel
core +1 more source
This review explores pathological disulfide‐crosslinking as a key driver of amyloidogenic protein misfolding and aggregation. Oxidative and ER stress pathways contributing to disease progression are discussed and emerging therapeutic strategies targeting disulfide‐linked aggregates in neurodegenerative and systemic amyloid diseases are examined ...
Dong Min Kang+4 more
wiley +1 more source
Endoplasmic reticulum stress as target for treatment of hearing loss
The endoplasmic reticulum (ER) plays pivotal roles in coordinating protein biosynthesis and processing. Under ER stress, when excessive misfolded or unfolded proteins are accumulated in the ER, the unfolded protein response (UPR) is activated.
Yanfei Wang, Zhigang Xu
doaj +1 more source
Endoplasmic reticulum stress, degeneration of pancreatic islet β-cells, and therapeutic modulation of the unfolded protein response in diabetes. [PDF]
BackgroundMyriad challenges to the proper folding and structural maturation of secretory pathway client proteins in the endoplasmic reticulum (ER) - a condition referred to as "ER stress" - activate intracellular signaling pathways termed the unfolded ...
Colon-Negron, Kevin+2 more
core +1 more source
The role of the Amyloid Precursor Protein mutations and PERK-dependent signaling pathways in the pathogenesis of Alzheimer’s disease [PDF]
Alzheimer’s disease (AD) is a highly complex, progressive, age-related neurodegenerative human disease entity. The genetic basis of AD is strictly connected with occurrence of mutations in Amyloid Precursor (APP) gene on chromosome 21.
Diehl, J. Alan+5 more
core +1 more source
Unfolded Protein Response (UPR): Cellular control for our errors in life
The unfolding protein response (UPR) is critical for the maintenance of cellular function under endoplasmic reticulum (ER) stress. Under stress conditions, proteins in the ER may misfold and accumulate into aggregates. To prevent aggregate accumulation, BiP is released from ATF6, IRE1 or PERK to bind to the misfolded proteins and assist in ATP mediated
openaire +2 more sources
ABSTRACT Calreticulin is a multifunctional protein found in the endoplasmic reticulum lumen that is important for calcium homeostasis and glycoprotein folding. Mutations in exon 9 of the CALR gene are the second most common genetic cause of myeloproliferative neoplasms.
Mifra Faiz+2 more
wiley +1 more source
The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity.
Christopher J. Adams+4 more
semanticscholar +1 more source
Proteostasis and ageing: insights from long-lived mutant mice [PDF]
The global increase in life expectancy is creating significant medical, social and economic challenges to current and future generations. Consequently, there is a need to identify the fundamental mechanisms underlying the ageing process.
Page, Melissa M.+2 more
core +1 more source
DCC enables the formation of glycocluster libraries through reversible disulfide exchange. Nanomolar ligands for multiple lectins (ConA, LecA, and LecB) were identified in a simple experimental set up, purified, and displayed nanomolar affinity with anti‐infectious properties.
Fanny Demontrond+13 more
wiley +1 more source