N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding.

Wang, Hao; Li, Shuo; Wang, Juejin; Chen, Shenghan; Sun, Xue-Long; Wu, Qingyu

Wang, Hao; Li, Shuo; Wang, Juejin; Chen, Shenghan; Sun, Xue-Long; Wu, Qingyu.

Affiliation

Wang H; Molecular Cardiology, Cleveland Clinic, Cleveland, United States.
Li S; Department of Chemistry, Cleveland State University, Cleveland, United States.
Wang J; Molecular Cardiology, Cleveland Clinic, Cleveland, United States.
Chen S; Molecular Cardiology, Cleveland Clinic, Cleveland, United States.
Sun XL; Molecular Cardiology, Cleveland Clinic, Cleveland, United States.
Wu Q; Molecular Cardiology, Cleveland Clinic, Cleveland, United States.

Elife ; 72018 06 11.

Article in En | MEDLINE | ID: mdl-29889025

Subject(s)

Calnexin/chemistry; Protein Domains; Protein Folding; Serine Endopeptidases/chemistry; Animals; Binding Sites/genetics; Calnexin/genetics; Calnexin/metabolism; Cell Line; Glycosylation; HEK293 Cells; Hep G2 Cells; Humans; Mutation; Phylogeny; Polysaccharides/metabolism; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism

Key words

N-glycosylation; biochemistry; calnexin; cell biology; chemical biology; corin; human; protein folding; serine protease

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Serine Endopeptidases / Protein Folding / Calnexin / Protein Domains Limits: Animals / Humans Language: En Journal: Elife Year: 2018 Document type: Article Affiliation country: United States Country of publication: United kingdom

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