213 Structures and interactions of proteins involved in ER-associated protein degradation

Volume: 31, Issue: sup1, Pages: 139 - 139
Published: Jan 1, 2013
Abstract
Proteins are translocated into the endoplasmic reticulum (ER) of cells in an unfolded state, and acquire their native conformation in the ER lumen after signal peptide cleavage. ER-associated degradation (ERAD) of folding-incompetent protein chains is mediated by the protein complexes residing in the ER membrane. We study the architecture and function of one of these, the HRD complex assembled around the E3 ubiquitin ligase Hrd1. The recognition...
Paper Details
Title
213 Structures and interactions of proteins involved in ER-associated protein degradation
Published Date
Jan 1, 2013
Volume
31
Issue
sup1
Pages
139 - 139
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