Structural insights into N-linked glycan-mediated protein folding from chemical and biological perspectives

Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases

“…However, misfolded glycoproteins should be degraded to maintain cellular homeostasis, because the accumulation of misfolded glycoproteins in the ER causes stress to cells, namely ER stress. Therefore, cells have a quality control system named ER glycoprotein quality control (glycoprotein ERQC) (described in more detail in Section 2 ) [ 3 , 4 , 5 , 6 ].…”

Structure, Function and Mechanism of N‐Glycan Processing Enzymes: endo‐α‐1,2‐Mannanase and endo‐α‐1,2‐Mannosidase

“…Within the ER, key steps in this pathway include the trimming of glucose residues by α‐ exo‐ glucosidases I and II, which allow monoglucosylated glycoproteins to engage with the calnexin/calreticulin folding lectins, the release of correctly folded deglucosylated glycoproteins and their transport to the Golgi apparatus. Quality control of folding is achieved by the glucosyltransferase UGGT1, which acts as a folding sensor by reglucosylating unfolded proteins, and allowing them to reengage with calnexin/calreticulin and additional attempts at folding [9] . Folding incompetent and misfolded N‐glycoproteins are degraded through the ER‐associated degradation pathway (ERAD), which involves recognition of glycoproteins with delayed exit from the ER through the slow degradation of the B and C mannose branches through the action of the EDEM α‐mannosidases, [10] their retrotranslocation to the cytosol, ubiquitinylation and proteasomal degradation [11] …”

Preparation of tannic acid and l-cysteine functionalized magnetic composites for synergistic enrichment of N-glycopeptides followed by mass spectrometric analysis

“…As one of the most essential post-translational modications, protein N-glycosylation is vital to various biological activities, e.g., intercellular recognition, 24 cell differentiation, 25,26 and protein folding. 27 Therefore, it is of great signicance to comprehensively study N-glycoproteins for understanding the correlations between N-glycoproteins and the pathological mechanism and detecting special disease biomarkers or drug targets. Although mass spectrometry (MS) has been the most commonly used method for glycoproteomics research, 28,29 it suffers from the disadvantages of lowabundance N-glycoproteins and a great deal of interferences in biological specimens, as well as low ionization efficiency of Nglycopeptides.…”