| Summary: | The folding and assembly of proteins in the endoplasmic reticulum (ER) lumen and membrane are monitored by ER quality control (ERQC) mechanisms. This thesis focuses on two elements of ERQC: the unfolded protein response (UPR) and ER-associated degradation (ERAD), essential processes that prevent the accumulation of misfolded proteins in the cell. The mechanisms of both are well studied but only partially characterized and additional pathways are conjectured to exist. We have created the ERQC database that contains protein interactions, gene expression data, sub-cellular localization and orthologies for all genes involved in the UPR and ERAD. Using this highly curated database, we have built a probabilistic protein interaction model that integrates this data in a statistically coherent fashion. The model allows us to both predict a set of proteins likely to be involved in these processes and to describe their likely roles therein.
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