Matches in SemOpenAlex for { <https://semopenalex.org/work/W1497009792> ?p ?o ?g. }
- W1497009792 endingPage "344" @default.
- W1497009792 startingPage "303" @default.
- W1497009792 abstract "Publisher Summary This chapter describes how N-glycan processing participates in the folding and quality control mechanisms operating in the ER. Glycosylation of asparagine residues (N-glycosylation) in the endoplasmic reticulum (ER) presents two basic differences with respect to glycosylation of Ser/Thr residues (Ooglycosylation) in either the cytosol or the Golgi apparatus. In N-glycosylation, a preassembled oligosaccharide containing 14 monosaccharide units is transferred “en bloc” to nascent polypeptide chains, whereas in O-glycosylation, either a variable number of monosaccharide units are sequentially transferred (Golgi O-glycosylation) or a singlet of such units is added (cytosolic O-glycosylation). On the other hand, N-glycan processing in the ER is similar in all cells and these reactions relate to the process of proper folding and assembly common to all glycoproteins. Proteins entering the secretory pathway acquire their proper tertiary and in some cases also quaternary structures in the ER. Monoglucosylated glycans formed by partial deglucosylation by GI and GII of oligosaccharides transferred from lipid derivatives to proteins (Glc3ManoGlcNAc2) mediate the binding of glycoproteins to two ER resident lecfins, calnexin (CNX) and calreticulin (CRT). Incompletely folded species are prevented from transit to the Golgi apparatus and degraded by the proteasome. Understanding the interplay between the CNX/CRT pathways with other folding factors in the ER can advance the understanding of how N-glycosylation participates in the quality-control mechanisms and protein biogenesis in the secretory pathway." @default.
- W1497009792 created "2016-06-24" @default.
- W1497009792 creator A5031638977 @default.
- W1497009792 creator A5071112170 @default.
- W1497009792 date "2001-01-01" @default.
- W1497009792 modified "2023-09-23" @default.
- W1497009792 title "N-Glycan processing and glycoprotein folding" @default.
- W1497009792 cites W126395666 @default.
- W1497009792 cites W1489184797 @default.
- W1497009792 cites W1492419563 @default.
- W1497009792 cites W1495367630 @default.
- W1497009792 cites W1508005690 @default.
- W1497009792 cites W1509743989 @default.
- W1497009792 cites W1515472397 @default.
- W1497009792 cites W1518996810 @default.
- W1497009792 cites W1522422264 @default.
- W1497009792 cites W1543822556 @default.
- W1497009792 cites W1546558290 @default.
- W1497009792 cites W1557299747 @default.
- W1497009792 cites W1566142227 @default.
- W1497009792 cites W1569618923 @default.
- W1497009792 cites W1571379445 @default.
- W1497009792 cites W1584526531 @default.
- W1497009792 cites W1590438213 @default.
- W1497009792 cites W1590739555 @default.
- W1497009792 cites W1604225108 @default.
- W1497009792 cites W1607176255 @default.
- W1497009792 cites W1627330551 @default.
- W1497009792 cites W1631353300 @default.
- W1497009792 cites W1677744184 @default.
- W1497009792 cites W174468170 @default.
- W1497009792 cites W1893502939 @default.
- W1497009792 cites W1946018878 @default.
- W1497009792 cites W1954227846 @default.
- W1497009792 cites W1963770237 @default.
- W1497009792 cites W1965233966 @default.
- W1497009792 cites W1968124895 @default.
- W1497009792 cites W1968350043 @default.
- W1497009792 cites W1969809368 @default.
- W1497009792 cites W1970007744 @default.
- W1497009792 cites W1974309640 @default.
- W1497009792 cites W1976482695 @default.
- W1497009792 cites W1978986484 @default.
- W1497009792 cites W1979647784 @default.
- W1497009792 cites W1980261582 @default.
- W1497009792 cites W1982377248 @default.
- W1497009792 cites W1982421065 @default.
- W1497009792 cites W1986045763 @default.
- W1497009792 cites W1986129246 @default.
- W1497009792 cites W1987651883 @default.
- W1497009792 cites W1991213853 @default.
- W1497009792 cites W1991396089 @default.
- W1497009792 cites W1992189713 @default.
- W1497009792 cites W1992864681 @default.
- W1497009792 cites W1993023866 @default.
- W1497009792 cites W1994947913 @default.
- W1497009792 cites W1999456217 @default.
- W1497009792 cites W1999466952 @default.
- W1497009792 cites W1999501523 @default.
- W1497009792 cites W1999719904 @default.
- W1497009792 cites W2000617551 @default.
- W1497009792 cites W2001126396 @default.
- W1497009792 cites W2008395942 @default.
- W1497009792 cites W2010168633 @default.
- W1497009792 cites W2011239271 @default.
- W1497009792 cites W2012097474 @default.
- W1497009792 cites W2013727355 @default.
- W1497009792 cites W2016735583 @default.
- W1497009792 cites W2017035228 @default.
- W1497009792 cites W2028799740 @default.
- W1497009792 cites W2030085354 @default.
- W1497009792 cites W2031192254 @default.
- W1497009792 cites W2033482754 @default.
- W1497009792 cites W2034264764 @default.
- W1497009792 cites W2034384974 @default.
- W1497009792 cites W2036933725 @default.
- W1497009792 cites W2037053899 @default.
- W1497009792 cites W2038303530 @default.
- W1497009792 cites W2038857470 @default.
- W1497009792 cites W2039863802 @default.
- W1497009792 cites W2043945565 @default.
- W1497009792 cites W2045893780 @default.
- W1497009792 cites W2047474039 @default.
- W1497009792 cites W2048671779 @default.
- W1497009792 cites W2048984147 @default.
- W1497009792 cites W2051690692 @default.
- W1497009792 cites W2052504607 @default.
- W1497009792 cites W2053631103 @default.
- W1497009792 cites W2053654265 @default.
- W1497009792 cites W2054414232 @default.
- W1497009792 cites W2055166426 @default.
- W1497009792 cites W2055775098 @default.
- W1497009792 cites W2056811071 @default.
- W1497009792 cites W2061423054 @default.
- W1497009792 cites W2066653929 @default.
- W1497009792 cites W2068920418 @default.
- W1497009792 cites W2069015362 @default.
- W1497009792 cites W2071466320 @default.