Mechanisms, regulation and functions of the unfolded protein response
Cellular stress induced by the abnormal accumulation of unfolded or misfolded proteins at
the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases …
the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases …
The unfolded protein response and cell fate control
C Hetz, FR Papa - Molecular cell, 2018 - cell.com
The secretory capacity of a cell is constantly challenged by physiological demands and
pathological perturbations. To adjust and match the protein-folding capacity of the …
pathological perturbations. To adjust and match the protein-folding capacity of the …
Endoplasmic reticulum stress signalling and the pathogenesis of non-alcoholic fatty liver disease
The global epidemic of obesity has been accompanied by a rising burden of non-alcoholic
fatty liver disease (NAFLD), with manifestations ranging from simple steatosis to non …
fatty liver disease (NAFLD), with manifestations ranging from simple steatosis to non …
Proteostasis control by the unfolded protein response
Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is
observed in many physiological and pathological conditions. To cope with endoplasmic …
observed in many physiological and pathological conditions. To cope with endoplasmic …
Ca2+ homeostasis and endoplasmic reticulum (ER) stress: An integrated view of calcium signaling
Cellular Ca 2+ homeostasis is maintained through the integrated and coordinated function
of Ca 2+ transport molecules, Ca 2+ buffers and sensors. These molecules are associated …
of Ca 2+ transport molecules, Ca 2+ buffers and sensors. These molecules are associated …
Calcium signaling and endoplasmic reticulum stress
Cellular homeostasis is essential for healthy functioning of cells and tissues as well as
proper organ development and maintenance. A disruption in cellular homeostasis triggers …
proper organ development and maintenance. A disruption in cellular homeostasis triggers …
Activation of goblet-cell stress sensor IRE1β is controlled by the mucin chaperone AGR2
E Cloots, P Guilbert, M Provost, L Neidhardt… - The EMBO …, 2024 - embopress.org
Intestinal goblet cells are secretory cells specialized in the production of mucins, and as
such are challenged by the need for efficient protein folding. Goblet cells express Inositol …
such are challenged by the need for efficient protein folding. Goblet cells express Inositol …
Mechanism of endoplasmic reticulum stress in cerebral ischemia
Y Han, M Yuan, YS Guo, XY Shen, ZK Gao… - Frontiers in Cellular …, 2021 - frontiersin.org
Endoplasmic reticulum (ER) is the main organelle for protein synthesis, trafficking and
maintaining intracellular Ca2+ homeostasis. The stress response of ER results from the …
maintaining intracellular Ca2+ homeostasis. The stress response of ER results from the …
Interactome screening identifies the ER luminal chaperone Hsp47 as a regulator of the unfolded protein response transducer IRE1α
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a dynamic
signaling network known as the unfolded protein response (UPR). IRE1α is a major UPR …
signaling network known as the unfolded protein response (UPR). IRE1α is a major UPR …
Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview
E Dufey, D Sepúlveda… - American Journal of …, 2014 - journals.physiology.org
Increased demand on the protein folding capacity of the endoplasmic reticulum (ER)
engages an adaptive reaction known as the unfolded protein response (UPR). The UPR …
engages an adaptive reaction known as the unfolded protein response (UPR). The UPR …