Novel Functions of Ubiquitin Ligase HRD1 With Transmembrane and Proline-Rich Domains
Journal of Pharmacological Sciences, 2008 Human ubiquitin ligase HRD1 is involved in endoplasmic reticulum-associated degradation (ERAD). We recently reported that HRD1 interacts with Parkin-associated endothelin receptor-like receptor (Pael-R), a substrate of Parkin, and promotes Pael-R ...
Tomohiro Omura +7 more
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Journal of Lipid Research, 2004 Apolipoprotein B (apoB)-48 contains a region termed the β1 domain that is predicted to be composed of extensive amphipathic β-strands. Analysis of truncated apoB variants revealed that sequences between the carboxyl termini of apoB-37 and apoB-42 ...
Louis R. Lapierre +4 more
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Lipopolysaccharide, high glucose and saturated fatty acids induce endoplasmic reticulum stress in cultured primary human adipocytes : salicylate alleviates this stress [PDF]
, 2010 Recent findings indicate that endoplasmic reticulum (ER) stress is significantly increased in adipose tissue of obese human subjects and is critical to the initiation and integration of pathways of inflammation and insulin action.
Saif Alhusaini +18 more
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The endoplasmic reticulum in plant immunity and cell death [PDF]
, 2012 The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells and a major production site of proteins destined for vacuoles, the plasma membrane, or apoplast in plants.
Ruth eEichmann +5 more
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Endoplasmic reticulum : shape and function in stress translation [PDF]
, 2014 The endoplasmic reticulum (ER) is a very versatile organelle. Besides its major role as the gateway to the secretory pathway the ER is central to adaptation against abiotic and biotic stress.
Stephen H. Howell +12 more
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Degradation of vasopressin precursor and pathogenic mutants in diabetes insipidus [PDF]
, 2007 The nonapeptide hormone, arginine vasopressin, plays a decisive role in the regulation of fluid balance by reducing free water clearance through reabsorption of water in the renal collecting ducts.
Friberg, Michael
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Correlation Between Decrease in Protein Levels of Ubiquitin Ligase HRD1 and Amyloid-β Production
Journal of Pharmacological Sciences, 2010 Endoplasmic reticulum–associated degradation (ERAD) is a quality control mechanism in which unfolded proteins are retro-translocated to the cytosol for degradation. Our recent study showed that suppression of expression of ubiquitin ligase HRD1, which is
Ryo Saito +3 more
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Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
Frontiers in Endocrinology, 2023 Misfolded proteins retained in the endoplasmic reticulum cause many human diseases. ER-associated degradation (ERAD) is one of the protein quality and quantity control system located at ER, which is responsible for translocating the misfolded proteins or
Hui Luo +7 more
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Polycystin-2 is regulated by endoplasmic reticulum-associated degradation [PDF]
Human Molecular Genetics, 2008 Endoplasmic reticulum(ER)-associated degradation (ERAD) is an essential process for cell homeostasis and remains not well understood. During ERAD, misfolded proteins are recognized, ubiquitinated on ER and subsequently retro-translocated/dislocated from ER to the 26S proteasome in the cytosol for proteolytic elimination. Polycystin-2 (PC2), a member of
Genqing, Liang +6 more
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Endoplasmic reticulum-associated degradation: exceptions to the rule
European Journal of Cell Biology, 2004 Quality control mechanisms in the endoplasmic reticulum (ER) ensure that misfolded proteins are recognized and targeted for degradation. According to the current view of ER-associated degradation (ERAD), the degradation does not occur in the ER itself but requires the retrotranslocation of the proteins to the cytosol where they are degraded by ...
Anton, Schmitz, Volker, Herzog
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