Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5508013 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2017 | 31 Pages |
Abstract
Proposed model for the folding events of nascent LPH. In the ER, partially folded LPH is interacting with calnexin/calreticulin chaperone system at domains II and IV. This interaction promotes functional folding of the whole protein which can then be arranged in a dimeric conformation mediated by regions in cytoplasmic and transmembrane sections as well as domains II and IV. The dimeric structure will then leave the ER to the Golgi apparatus.137
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Lena Diekmann, Marc Behrendt, Mahdi Amiri, Hassan Y. Naim,