Results 21 to 30 of about 225,463 (263)
Lighting Up the Stressed ER [PDF]
Cell, 2008 Balancing the capacity for protein maturation with changes in protein flux through the endoplasmic reticulum (ER) is crucial for maintaining ER homeostasis. In this issue, Merksamer et al. (2008) exploit a redox-sensitive fluorescent protein to monitor the environment inside the ER of living yeast, illuminating how this organelle responds to different ...
Kang, Sang-Wook, Hegde, Ramanujan S.
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Frontiers in Neuroscience, 2020 Studies demonstrated that spinal autophagy was impaired in spinal nerve ligation (SNL) rats. However, the relationship of endoplasmic reticulum (ER) stress and ER-phagy and whether dexmedetomidine (DEX) modulates ER-phagy remain unclear.
Yongda Liu +14 more
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Endoplasmic Reticulum Stress and Reactive Oxygen Species in Plants
Antioxidants, 2022 The endoplasmic reticulum (ER) is a key compartment responsible for protein processing and folding, and it also participates in many signal transduction and metabolic processes. Reactive oxygen species (ROS) are important signaling messengers involved in
Jiajian Cao +4 more
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Journal of Translational Medicine, 2023 Bone regeneration therapy is clinically important, and targeted regulation of endoplasmic reticulum (ER) stress is important in regenerative medicine. The processing of proteins in the ER controls cell fate.
Tingyu Wu +4 more
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ERK1/2 signalling protects against apoptosis following endoplasmic reticulum stress but cannot provide long-term protection against BAX/BAK-independent cell death. [PDF]
PLoS ONE, 2017 Disruption of protein folding in the endoplasmic reticulum (ER) causes ER stress. Activation of the unfolded protein response (UPR) acts to restore protein homeostasis or, if ER stress is severe or persistent, drive apoptosis, which is thought to proceed
Nicola J Darling +2 more
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Antioxidants, 2021 In different pathological states that cause endoplasmic reticulum (ER) calcium depletion, altered glycosylation, nutrient deprivation, oxidative stress, DNA damage or energy perturbation/fluctuations, the protein folding process is disrupted and the ER ...
Yan Zhou +4 more
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MFN2 mediates ER-mitochondrial coupling during ER stress through specialized stable contact sites
Frontiers in Cell and Developmental Biology, 2022 Endoplasmic reticulum (ER) functions critically depend on a suitable ATP supply to fuel ER chaperons and protein trafficking. A disruption of the ability of the ER to traffic and fold proteins leads to ER stress and the unfolded protein response (UPR ...
Benjamin Gottschalk +6 more
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Stress management at the ER: Regulators of ER stress-induced apoptosis
Pharmacology & Therapeutics, 2012 The endoplasmic reticulum (ER) is an elaborate cellular organelle essential for cell function and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins which are detected by ER transmembrane receptors that initiate the unfolded protein response (UPR) to restore normal ER function.
Gorman, Adrienne M. +3 more
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A NODding acquaintance with ER stress [PDF]
Cell Death Discovery, 2016 Accumulation of unfolded or misfolded proteins in the lumen of the endoplasmatic reticulum (ER) results in ER stress and induces the unfolded protein response (UPR). The UPR consists of distinct cellular processes, such as increased transcription of repair proteins and chaperones, cell death and the induction of an inflammatory response resulting in ...
Stafford, CA, Nachbur, U
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MicroRNA-494 Regulates Endoplasmic Reticulum Stress in Endothelial Cells
Frontiers in Cell and Developmental Biology, 2021 Defects in stress responses are important contributors in many chronic conditions including cancer, cardiovascular disease, diabetes, and obesity-driven pathologies like non-alcoholic steatohepatitis (NASH).
Namita Chatterjee +5 more
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