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10.3109/10409238.2015.1085826

http://scihub22266oqcxt.onion/10.3109/10409238.2015.1085826
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suck abstract from ncbi


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pmid26362261
      Crit+Rev+Biochem+Mol+Biol 2015 ; 50 (6 ): 477-88
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  • A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease #MMPMID26362261
  • He K ; Ravindran MS ; Tsai B
  • Crit Rev Biochem Mol Biol 2015[]; 50 (6 ): 477-88 PMID26362261 show ga
  • A dedicated network of cellular factors ensures that proteins translocated into the endoplasmic reticulum (ER) are folded correctly before they exit this compartment en route to other cellular destinations or for secretion. When proteins misfold, selective ER-resident enzymes and chaperones are recruited to rectify the protein-misfolding problem in order to maintain cellular proteostasis. However, when a protein becomes terminally misfolded, it is ejected into the cytosol and degraded by the proteasome via a pathway called ER-associated degradation (ERAD). Strikingly, toxins and viruses can hijack elements of the ERAD pathway to access the host cytosol and cause infection. This review focuses on emerging data illuminating the molecular mechanisms by which these toxic agents co-opt the ER-to-cytosol translocation process to cause disease.
  • |*Bacterial Physiological Phenomena [MESH]
  • |*Endoplasmic Reticulum-Associated Degradation [MESH]
  • |*Host-Pathogen Interactions [MESH]
  • |Animals [MESH]
  • |Bacterial Infections/*metabolism [MESH]
  • |Bacterial Toxins/*metabolism [MESH]
  • |Cytosol/metabolism/microbiology/virology [MESH]
  • |Endoplasmic Reticulum/metabolism/microbiology/virology [MESH]
  • |Humans [MESH]
  • |Polyomavirus Infections/*metabolism [MESH]
  • |Polyomavirus/*physiology [MESH]


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