title: ER stress response: getting the UPR hand on misfolded proteins.
abstract: Unfolded proteins are constantly delivered to the ER lumen, where they must be removed by folding or degradation. Recent studies show that the 'unfolded protein response' controls essentially all aspects of ER function, coordinating these two fates for misfolded proteins in a process necessary for normal cell life.
authors.affiliation: Department of Biology, University of California San Diego, 2100E Pacific Hall, La Jolla, CA 92093-0347, USA. rhampton@biomail.ucsd.edu.
authors.forename: R Y
authors.initials: RY
authors.lastname: Hampton
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008954:Models, Biological; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction; D013312:Stress, Physiological / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D011506:Proteins