Shruthi S Vembar, Jeffrey L Brodsky. Nat Rev Mol Cell Biol 2008
Times Cited: 956
Times Cited: 956
Times Cited
Times Co-cited
Similarity
Signal integration in the endoplasmic reticulum unfolded protein response.
David Ron, Peter Walter. Nat Rev Mol Cell Biol 2007
David Ron, Peter Walter. Nat Rev Mol Cell Biol 2007
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Quality control: ER-associated degradation: protein quality control and beyond.
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Claudio Hetz. Nat Rev Mol Cell Biol 2012
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Cleaning up in the endoplasmic reticulum: ubiquitin in charge.
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The unfolded protein response: from stress pathway to homeostatic regulation.
Peter Walter, David Ron. Science 2011
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The eIF2α/ATF4 pathway is essential for stress-induced autophagy gene expression.
Wafa B'chir, Anne-Catherine Maurin, Valérie Carraro, Julien Averous, Céline Jousse, Yuki Muranishi, Laurent Parry, Georges Stepien, Pierre Fafournoux, Alain Bruhat. Nucleic Acids Res 2013
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Mechanisms, regulation and functions of the unfolded protein response.
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XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor.
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Protein misfolding in the endoplasmic reticulum as a conduit to human disease.
Miao Wang, Randal J Kaufman. Nature 2016
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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.
Yihong Ye, Yoko Shibata, Chi Yun, David Ron, Tom A Rapoport. Nature 2004
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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.
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Defining human ERAD networks through an integrative mapping strategy.
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IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA.
Marcella Calfon, Huiqing Zeng, Fumihiko Urano, Jeffery H Till, Stevan R Hubbard, Heather P Harding, Scott G Clark, David Ron. Nature 2002
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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase.
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Endoplasmic reticulum stress in disease pathogenesis.
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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.
Y Ye, H H Meyer, T A Rapoport. Nature 2001
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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation.
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The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.
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OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.
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Quality Control in the Endoplasmic Reticulum: Crosstalk between ERAD and UPR pathways.
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Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis.
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IRE1α cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2.
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Allosteric inhibition of the IRE1α RNase preserves cell viability and function during endoplasmic reticulum stress.
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Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3.
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The biology of proteostasis in aging and disease.
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Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system.
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Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.
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Proteostasis control by the unfolded protein response.
Claudio Hetz, Eric Chevet, Scott A Oakes. Nat Cell Biol 2015
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Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.