EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex.

@article{Cormier2009EDEM1RA,
  title={EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex.},
  author={James H Cormier and Taku Tamura and Johan C. Sunryd and Daniel N Hebert},
  journal={Molecular cell},
  year={2009},
  volume={34 5},
  pages={627-33}
}
Terminally misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently cleared by the ER-associated degradation (ERAD) pathway. The degradation of ERAD substrates involves mannose trimming of N-linked glycans; however, the mechanisms of substrate recognition and sorting to the ERAD pathway are poorly defined. EDEM1 (ER degradation-enhancing alpha-mannosidase-like 1 protein) has been proposed to play a role in ERAD substrate signaling or… CONTINUE READING
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