Results 41 to 50 of about 1,308,915 (353)

ER stress and neurodegenerative diseases [PDF]

Cell Death & Differentiation, 2006
Endoplasmic reticulum (ER) stress is caused by disturbances in the structure and function of the ER with the accumulation of misfolded proteins and alterations in the calcium homeostasis. The ER response is characterized by changes in specific proteins, causing translational attenuation, induction of ER chaperones and degradation of misfolded proteins.
D, Lindholm, H, Wootz, L, Korhonen
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ER stress boosts respiration [PDF]

Nature Reviews Molecular Cell Biology, 2019
Glucose deprivation induces ER stress, which enhances mitochondrial respiration by promoting the assembly of respiratory supercomplexes.
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Chemical chaperone treatment reduces intracellular accumulation of mutant collagen IV and ameliorates the cellular phenotype of a COL4A2 mutation that causes haemorrhagic stroke [PDF]

, 2013
Haemorrhagic stroke accounts for approximately 20% of stroke cases and porencephaly is a clinical consequence of perinatal cerebral haemorrhaging. Here we report the identification of a novel dominant G702D mutation in the collagen domain of COL4A2 ...
Aislynn Taggart, Bateman, Brazel, Catheline Vilain, de Clerck, Engin, Favor, Geesin, Gould, Gould, Gould, Hostikka, Ishida, Jeanne, Kalluri, Karl E. Kadler, Khoshnoodi, Lydia S. Murray, Marc Abramowicz, Muthukumaran, Nicole Van Regemorter, Ozcan, Plaisier, Plaisier, Poschl, Ron, Taylor, Tom Van Agtmael, Vahedi, Van Agtmael, Van Agtmael, Van Agtmael, Verbeek, Vilain, Woo, Yinhui Lu   +35 more
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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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Endoplasmic reticulum stress and the protein degradation system in ophthalmic diseases [PDF]

PeerJ, 2020
Objective Endoplasmic reticulum (ER) stress is involved in the pathogenesis of various ophthalmic diseases, and ER stress-mediated degradation systems play an important role in maintaining ER homeostasis during ER stress. The purpose of this review is to
Jing-Yao Song, Xue-Guang Wang, Zi-Yuan Zhang, Lin Che, Bin Fan, Guang-Yu Li   +5 more
doaj   +2 more sources

Rab7a modulates ER stress and ER morphology

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2018
The Endoplasmic Reticulum (ER) is a membranous organelle with diverse structural and functional domains. Peripheral ER includes interconnected tubules, and dense tubular arrays called "ER matrices" together with bona fide flat cisternae. Transitions between these states are regulated by membrane-associated proteins and cytosolic factors.
Duarte, Mateus, Elettra Sara, Marini, Cinzia, Progida, Oddmund, Bakke   +3 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., Healy, Sandra J. M., Jäger, Richard, Samali, Afshin   +3 more
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The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance

, 2019
Misfolded proteins in the endoplasmic reticulum (ER) activate the unfolded protein response (U PR), which enhances protein folding to restore homeostasis.
Aviram, Barlowe, Berner, Bicknell, Bonilla, Boos, Bosis, Braakman, Chen, Christiano, Conz, Cox, Cox, Cox, Dohmen, Finger, Foresti, Foresti, Gasch, Gething, Goldberg, Görner, Hahn, Hahn, Hahn, Hallstrom, Hampton, Hanssum, Hao, Harbison, Higuchi-Sanabria, Hitchcock, Ho, Hou, Huebert, Itzhak, Janke, Jelinsky, Jonikas, Kawaguchi, Khmelinskii, Kim, Knop, Kostova, Leber, Lee, Liu, Longtine, Mannhaupt, Martínez-Pastor, Meiners, Metzger, Mitsiades, Mumberg, Nasmyth, Ng, Ng, Nishitoh, Obeng, Owsianik, Patil, Pincus, Pincus, Prasad, Radhakrishnan, Rapoport, Rousseau, Schuck, Sikorski, Spear, Spear, Sprouffske, Steffen, Stirling, Szoradi, Tkach, Travers, Tyanova, Verghese, Vogel, Walter, Wang, Wang, Wrobel, Xie, Yamamoto, Young, Zheng   +87 more
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Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts. [PDF]

, 2015
Organelle contact sites perform fundamental functions in cells, including lipid and ion homeostasis, membrane dynamics, and signaling. Using a forward proteomics approach in yeast, we identified new ER-mitochondria and ER-vacuole contacts specified by an
Murley, Andrew, Nunnari, Jodi, Prinz, William A, Sarsam, Reta D, Toulmay, Alexandre, Yamada, Justin   +5 more
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ER stress modulates cellular metabolism [PDF]

Biochemical Journal, 2011
Changes in metabolic processes play a critical role in the survival or death of cells subjected to various stresses. In the present study, we have investigated the effects of ER (endoplasmic reticulum) stress on cellular metabolism. A major difficulty in studying metabolic responses to ER stress is that ER stress normally leads to apoptosis and ...
Xiaoli, Wang, Colins O, Eno, Brian J, Altman, Yanglong, Zhu, Guoping, Zhao, Kristen E, Olberding, Jeffrey C, Rathmell, Chi, Li   +7 more
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