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Functional role of the disulfide isomerase ERp57 in axonal regeneration
(2015)
ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle. ERp57 is markedly upregulated in most common ...
Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
(American Society for Cell Biology, 2009-07)
Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) ...
Functional Role of the Disulfide Isomerase ERp57 in Axonal Regeneration
(Public Library Science, 2015)
ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes
disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.
ERp57 is markedly upregulated in most common ...
Quality Control in Glycoprotein Folding
(Wiley-VCH, 2005)
The concept of quality control of protein folding in the secretory pathway emerged in the late 1970s and early 1980s when it was noticed that not in all cases did insertion of proteins in the endoplasmic reticulum (ER) ...
Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo
(American Society for Cell Biology, 2011-06)
Glucosidase II (GII) sequentially removes the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to proteins. GII also participates in cycles involving the lectin/chaperones calnexin (CNX) and ...
Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition
(American Chemical Society, 2015-07)
N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are ...
The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein
(Amer Soc Biochemistry Molecular Biology, 2015)
Although the accumulation of a misfolded and protease-resistant form of the prion protein (PrP) is a key event in prion pathogenesis, the cellular factors involved in its folding and quality control are poorly understood. ...