The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation

Sugar-binding activity of the MRH domain in the ER  -glucosidase II   subunit is important for efficient glucose trimming

(2009) D. Hu et al.   GLYCOBIOLOGY

Human OS-9, a Lectin Required for Glycoprotein Endoplasmic Reticulum-associated Degradation, Recognizes Mannose-trimmedN-Glycans

(2009) Nobuko Hosokawa et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum

(2009) Simone Clerc et al.   JOURNAL OF CELL BIOLOGY

Proteomic identification of differentially expressed genes in mouse neural stem cells and neurons differentiated from embryonic stem cells in vitro

(2008) Kuniko Akama et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

A Dual Task for the Xbp1-responsive OS-9 Variants in the Mammalian Endoplasmic Reticulum

(2008) Riccardo Bernasconi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation

(2008) Erin M. Quan et al.   MOLECULAR CELL

OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

(2008) John C. Christianson et al.   NATURE CELL BIOLOGY

Endoplasmic Reticulum (ER) Mannosidase I Is Compartmentalized and Required for N-Glycan Trimming to Man5–6GlcNAc2 in Glycoprotein ER-associated Degradation

(2007) Edward Avezov et al.   MOLECULAR BIOLOGY OF THE CELL