Endoplasmic reticulum stress signaling in disease.
By S. Marciniak, D. Ron. Physiological Reviews, 2006
959 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/b3640968649d9dab793d1c624546baef97a36dda
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Citations in the corpus
- Initiation and execution of lipotoxic ER stress in pancreatic β-cells (2008, background): “Spliced XBP1 (XBP1s) induces genes involved in ER expansion, in protein folding and in the degradation of misfolded proteins (Lee et al., 2005; Lee et al., 2003; Marciniak and Ron, 2006).”
- Aberrant Mucin Assembly in Mice Causes Endoplasmic Reticulum Stress and Spontaneous Inflammation Resembling Ulcerative Colitis (2008, background): “GRP78 is a heat shock protein that chaperones proteins in the ER during folding and is up-regulated in ER stress when it accumulates with misfolded proteins, ensuring they do not exit the ER normally but are removed for degradation [33].”
- Adiponectin Regulation and Function (2018, unknown): “Obesity, diabetes, and other disease states are associated with ER stress and the unfolded protein response (UPR), designed to remove incorrectly folded proteins which may interfere with normal cell function (199,239).”
- Saturated Fatty Acids Produce an Inflammatory Response Predominantly through the Activation of TLR4 Signaling in Hypothalamus: Implications for the Pathogenesis of Obesity (2009, background): “One of the outcomes of the activation of UPR is the induction of the expression of cytokines and proteins involved in immune surveillance (Krappmann et al., 2004; Marciniak and Ron, 2006).”
- Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “The UPR includes upregulation of ER-located chaperones to assist folding of aggregationprone proteins; a selective inhibition of overall protein synthesis to reduce the ER work load, while selectively favoring synthesis of proteins that augment the UPR; and transport of misfolded proteins to the ubi”
- Endoplasmic reticulum stress plays a central role in development of leptin resistance. (2009, background): “The endoplasmic reticulum (ER) is a sophisticated luminal network in which protein synthesis, maturation, folding, and transport take place (Marciniak and Ron, 2006; Schroder and Kaufman, 2005).”
- Diabetic cardiomyopathy: a hyperglycaemia- and insulin-resistance-induced heart disease (2017, background): “In diabetes, hyperglycaemia and insulin resistance induce ER stress, involving impaired Ca handling and accumulation of unfolded proteins [29] (Fig.”
- Inflammation and metabolic disorders (2006, background): “Unfolded or misfolded proteins are detected, removed from the ER and degraded by the 26S proteasome syste”