Quick Search:

uzh logo
Browse by:

Zurich Open Repository and Archive

Maintenance: Tuesday, July the 26th 2016, 07:00-10:00

ZORA's new graphical user interface will be relaunched (For further infos watch out slideshow ZORA: Neues Look & Feel). There will be short interrupts on ZORA Service between 07:00am and 10:00 am. Please be patient.

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: Elsevier, 163-82.

Accepted Version (English)
View at publisher


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.


6 citations in Web of Science®
7 citations in Scopus®
Google Scholar™



221 downloads since deposited on 27 Jan 2012
23 downloads since 12 months

Detailed statistics

Additional indexing

Item Type:Book Section, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
Dewey Decimal Classification:570 Life sciences; biology
Deposited On:27 Jan 2012 21:46
Last Modified:05 Apr 2016 15:23
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

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page