ERAD: the long road to destruction

By Birgit Meusser, Christian Hirsch, E. Jarosch, T. Sommer. Nature Cell Biology, 2005

1,304 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/c103d529e6e96c3a5101d6a65481b7f71db633d5

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In Cell Biology

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4. D. Ron
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In Epidemiology

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Citations in the corpus

• Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. (2007, background): “It is the degrading machine in the ER-associated degradation pathway.(2) Endoplasmic reticulum is an intracellular membranous structure that performs such important functions as protein post-translational modifications, protein folding and oligomerization, and synthesis of lipids and sterols.”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, background): “Protein disposal requires retrotranslocation into the cytosol, via a presumptive retrotranslocon channel, and subsequent degradation by the ubiquitin/proteasome pathway (107).”
• Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system (2012, background): “p97 has a key role in endoplasmic-reticulum-associated degradation (ERAD) as reviewed in detail elsewher”
• Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, neutral): “Thus, the examination of Nox biology reveals much about the cellular logic behind regulated oxidant production.”
• In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “lumen is instrumental to maintain ER homeostasis (256).”
• Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “In the process of ER-associated degradation, many misfolded proteins within the ER are retrotranslocated out of that compartment into the cytosol by a series of ER membrane–associated Ub conjugating proteins; these then are targeted to cytosolic proteasomes (16).”
• Selenoproteins: molecular pathways and physiological roles. (2014, background): “The ERAD machinery consists of multiprotein complexes that are involved in recognition, ubiquitination, and retrotranslocation of protein substrates from the ER to the cytosol, and their subsequent degradation by the ubiquitin/proteasome system (219, 252).”
• Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response (2006, background): “The ERAD pathway is thought to continually remove unfolded proteins from the ER and channel them to degradation by the proteasome.”
• Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. (2006, background): “This process is called ERAD (for ERassociated protein degradation), retrotranslocation, or dislocation (Meusser et al., 2005; Tsai et al., 2002), and it plays a role in many diseases.”
• Pathological roles of MAPK signaling pathways in human diseases. (2010, background): “SOD1 mutants including A4V, G85R, and G93A interact with Derlin-1, a component of the ER-associated degradation machinery [141], resulting in the activation of the ASK1-mediated cell death pathway in motor neurons [142] (Fig.”
• Protein sensors for membrane sterols. (2006, positive): “ERAD is the process by which denatured ER proteins are retrotranslocated across the ER membrane for degradation by cytosolic proteasomes (Meusser et al., 2005).”