Results 71 to 80 of about 19,138 (225)
Unique evolution of the UPR pathway with a novel bZIP transcription factor, Hxl1, for controlling pathogenicity of Cryptococcus neoformans. [PDF]
In eukaryotic cells, the unfolded protein response (UPR) pathway plays a crucial role in cellular homeostasis of the endoplasmic reticulum (ER) during exposure to diverse environmental conditions that cause ER stress. Here we report that the human fungal
Seon Ah Cheon +5 more
doaj +1 more source
ABSTRACT Particulate matter (PM) is a major global health threat, linked to millions of deaths annually. Beyond inhalation, PM components reach the gastrointestinal tract through the mucociliary escalator or contaminated food and water. Among PM's organic fraction, redox‐active quinones such as 1,2‐naphthoquinone (NQ) and 9,10‐phenanthrenequinone (PQ ...
Franco Cervellati +6 more
wiley +1 more source
ABSTRACT Metabolic dysfunction‐associated steatotic liver disease (MASLD) has emerged as the most prevalent chronic liver disease worldwide, closely linked to the global rising incidence of obesity and metabolic syndrome. This review synthesizes current evidence on the pathogenesis, gut–liver axis, and multidisciplinary management of MASLD within the ...
Beom Kyung Kim
wiley +1 more source
Ubiquitination of Inositol-requiring Enzyme 1 (IRE1) by the E3 Ligase CHIP Mediates the IRE1/TRAF2/JNK Pathway [PDF]
Deciphering the inositol-requiring enzyme 1 (IRE1) signaling pathway is fundamentally important for understanding the unfolded protein response (UPR). The ubiquitination of proteins residing on the endoplasmic reticulum (ER) membrane has been reported to be involved in the UPR, although the mechanism has yet to be fully elucidated.
Xu, Zhu +10 more
openaire +2 more sources
Extracellular vesicles (EVs) are a diverse population of membrane nanoparticles secreted by nearly all cell types, playing a key role in intercellular communication by transferring bioactive macromolecular cargo. In cancer, EVs shape both the local tumour microenvironment and distant premetastatic niches.
Evangelia Pantazaka +3 more
wiley +1 more source
IRE1 functions and inhibition by M50 and UL50.
Accumulation of unfolded proteins in the ER leads to recruitment of chaperones such as BiP and activation of ER stress sensors such as IRE1. (A) IRE1 dimerizes, autophosphorylates itself, and activates an endoribonuclease activity, which mediates Xbp1 ...
Julia M. Burkhart (443213) +9 more
core +1 more source
Regulated Ire1-dependent decay of messenger RNAs in mammalian cells [PDF]
Maintenance of endoplasmic reticulum (ER) function is achieved in part through Ire1 (inositol-requiring enzyme 1), a transmembrane protein activated by protein misfolding in the ER. The cytoplasmic nuclease domain of Ire1 cleaves the messenger RNA (mRNA)
Peter Walter +11 more
core +1 more source
Proper protein folding in the endoplasmic reticulum (ER) is vital in all eukaryotes. When misfolded proteins accumulate in the ER lumen, the transmembrane kinase/endoribonuclease Ire1 initiates splicing of HAC1 mRNA to generate the bZIP transcription ...
Taiga Miyazaki +4 more
doaj +1 more source
A schematic diagram illustrating how 3′tiRNA‐GlyGCC promotes the endoplasmic reticulum stress (ERS) and proliferation in hypoxic pulmonary artery smooth muscle cells (PASMCs) by inhibiting the expression of myelin regulatory factor (Myrf), ultimately leading to pulmonary hypertension (PH).
Lixin Zhang +11 more
wiley +1 more source
IRE1-mediated miRNA maturation in macrophage phosphoinositide signaling
International audienceEndoplasmic reticulum (ER) stress signaling has long been associated with various pathological states in particular with the development of diseases with an underlying inflammation, such as diabetes, liver or cardiovascular ...
Tony Avril +3 more
core +1 more source

