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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-55146

Hülsmeier, A J; Welti, M; Hennet, T (2011). Glycoprotein maturation and the UPR. In: Conn, P M. The unfolded protein response and cellular stress. Part C. Amsterdam, NL, 163-82. ISBN 978-0-12-385928-0.

Accepted Version (English)


Glycosylation is a complex form of protein modification occurring in the secretory pathway. The addition of N- and O-glycans affects intracellular processes like the folding and trafficking of most glycoproteins. To better understand the impact of glycosylation in protein folding and maturation, parameters like glycosylation site occupancy and oligosaccharide structure must be measured quantitatively. In this chapter, we describe current methods enabling the determination of N-glycosylation by assessment of cellular dolichol phosphate levels, dolichol-linked oligosaccharides, and the occupancy of N-glycosylation sites. We also provide detailed methods for the analysis of O-glycosylation, whose role in intracellular protein maturation is often overlooked.

Item Type:Book Section, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
DDC:570 Life sciences; biology
Deposited On:27 Jan 2012 21:46
Last Modified:29 Nov 2013 12:10
Series Name:Methods in Enzymology
ISSN:0076-6879 (P) 1557-7988 (E)
Publisher DOI:10.1016/B978-0-12-385928-0.00010-9
Related URLs:http://opac.nebis.ch/F/?local_base=NEBIS&CON_LNG=GER&func=find-b&find_code=SYS&request=006440764
PubMed ID:21329800
Citations:Web of Science®. Times Cited: 4
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Scopus®. Citation Count: 4

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