Ontology highlight
ABSTRACT:
SUBMITTER: Galligan JJ
PROVIDER: S-EPMC3501204 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Galligan James J JJ Fritz Kristofer S KS Tipney Hannah H Smathers Rebecca L RL Roede James R JR Shearn Colin T CT Hunter Lawrence E LE Petersen Dennis R DR
Journal of proteome research 20110307 4
Alcoholic liver disease (ALD) is a prominent cause of morbidity and mortality in the United States. Alterations in protein folding occur in numerous disease states, including ALD. The endoplasmic reticulum (ER) is the primary site of post-translational modifications (PTM) within the cell. Glycosylation, the most abundant PTM, affects protein stability, structure, localization, and activity. Decreases in hepatic glycosylation machinery have been observed in rodent models of ALD, but specific prot ...[more]