Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F15%3A43900181" target="_blank" >RIV/60461373:22340/15:43900181 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1093/glycob/cwv058" target="_blank" >http://dx.doi.org/10.1093/glycob/cwv058</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/glycob/cwv058" target="_blank" >10.1093/glycob/cwv058</a>

Result language
angličtina
Original language name
Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi
Original language description
The hallmark of N-linked protein glycosylation is the generation of diverse glycan structures in the secretory pathway. Dynamic, non-template-driven processes of N-glycan remodeling in the endoplasmic reticulum and the Golgi provide the cellular settingfor structural diversity. We applied newly developed mass spectrometry-based analytics to quantify site-specific N-glycan remodeling of the model protein Pdi1p expressed in insect cells. Molecular dynamics simulation, mutational analysis, kinetic studiesof in vitro processing events and glycan flux analysis supported the defining role of the protein in N-glycan processing.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CI - Industrial chemistry and chemical engineering
OECD FORD branch
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Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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