| Literature DB >> 26676362 |
Lydia Lamriben1, Jill B Graham1, Benjamin M Adams1, Daniel N Hebert1.
Abstract
Helenius and colleagues proposed over 20-years ago a paradigm-shifting model for how chaperone binding in the endoplasmic reticulum was mediated and controlled for a new type of molecular chaperone- the carbohydrate-binding chaperones, calnexin and calreticulin. While the originally established basics for this lectin chaperone binding cycle holds true today, there has been a number of important advances that have expanded our understanding of its mechanisms of action, role in protein homeostasis, and its connection to disease states that are highlighted in this review.Entities:
Keywords: N-glycans; endoplasmic reticulum; molecular chaperones; protein folding; quality control
Mesh:
Substances:
Year: 2016 PMID: 26676362 PMCID: PMC4805476 DOI: 10.1111/tra.12358
Source DB: PubMed Journal: Traffic ISSN: 1398-9219 Impact factor: 6.215