Gerardo Z. Lederkremer

Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2.

Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains.

A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins.

Transient arrest in proteasomal degradation during inhibition of translation in the unfolded protein response.

PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress.

Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation.

ER stress induces alternative nonproteasomal degradation of ER proteins but not of cytosolic ones.

Glycoprotein folding, quality control and ER-associated degradation.

Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps.

Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.

Protein quality control, retention, and degradation at the endoplasmic reticulum.

A secreted form of the asialoglycoprotein receptor, sH2a, as a novel potential noninvasive marker for liver fibrosis.

Constant serum levels of secreted asialoglycoprotein receptor sH2a and decrease with cirrhosis.