Results 131 to 140 of about 1,143,124 (339)
Advanced Science, EarlyView.Pancreatic neuroendocrine tumors frequently silence MEN1 through epigenetic mechanisms. Here, SIRT7 recruits DNMT1 to the MEN1 promoter, drives hypermethylation, and enhances DNA repair. Inhibiting SIRT7 restores MEN1, reduces MRN complex abundance, impairs double‐strand break repair, and sensitizes PanNET models to radiation, supporting SIRT7 as a ...
Jianyun Jiang +11 more
wiley +1 more source
Virulence, 2019 Virus infection induces different cellular responses in infected cells. These include cellular stress responses like autophagy and unfolded protein response (UPR).
P. Mehrbod +10 more
semanticscholar +1 more source
Advanced Science, EarlyView.We propose the Full‐Body AI Agent, a multi‐scale collaborative framework with 7 biological‐layer agents. It unifies multi‐omics/clinical data via standardized protocols, enabling phenotype‐guided closed‐loop reasoning, quantitative evaluation, and LLM safeguards, with promising applications in tumor metastasis modeling and precision drug development ...
Aoqi Wang +11 more
wiley +1 more source
PLoS ONE, 2011 Bax inhibitor-1 (BI-1) is an anti-apoptotic gene whose expression is upregulated in a wide range of human cancers. Studies in both mammalian and plant cells suggest that the BI-1 protein resides in the endoplasmic reticulum and is involved in the ...
James Cebulski +4 more
doaj +1 more source
Signaling and Regulation of the Mitochondrial Unfolded Protein Response.
Cold Spring Harbor Perspectives in Biology, 2019 The mitochondrial proteome encompasses more than a thousand proteins, which are encoded by the mitochondrial and nuclear genomes. Mitochondrial biogenesis and network health relies on maintenance of protein import pathways and the protein-folding ...
N. U. Naresh, Cole M. Haynes
semanticscholar +1 more source
Intracellular signaling by the unfolded protein response
, 2020 The unfolded protein response (UPR) is an intracellular signaling pathway that is activated by the accumulation of unfolded proteins in the endoplasmic reticulum (ER).
Peter Walter +2 more
core
Characterisation of the oxidoreductase Erol-Lß and the misfolding of the secretory pathway substrate HLA-B27 [PDF]
, 2007 The endoplasmic reticulum (ER) is the site of oxidative folding for proteins entering the secretory pathway. Here, nascent polypeptides acquire disulfide bonds, which confer both stability and functionality on secretory and ER-resident proteins.
Lemin, Andrew James
core
Advanced Science, EarlyView.The ER's continuous tubular network is maintained by ER‐shaping proteins whose mutation or dysregulation contributes to neurodegenerative diseases. Here, we show that ER morphology sets the speed of Ca2+ store replenishment between firing events. Disrupting ER continuity slows intra‐ER Ca2+ redistribution from extracellular refill (SOCE) sites, driving
Valentina Davi +13 more
wiley +1 more source
A functional link between the co-translational protein translocation pathway and the UPR
eLife, 2015 Upon endoplasmic reticulum (ER) stress, the transmembrane endoribonuclease Ire1α performs mRNA cleavage reactions to increase the ER folding capacity. It is unclear how the low abundant Ire1α efficiently finds and cleaves the majority of mRNAs at the ER ...
Rachel Plumb +3 more
doaj +1 more source
Journal of the American College of Cardiology, 2019 Background The mitochondrial unfolded protein response (UPRmt) is activated when misfolded proteins accumulate within mitochondria and leads to increased expression of mitochondrial chaperones and proteases to maintain protein quality and mitochondrial ...
Ioannis Smyrnias +10 more
semanticscholar +1 more source