Back to search

Article

The carboxy-terminal ER-retention motif, SEKDEL, influences the N-linked glycosylation of recombinant human α-l-iduronidase but has little effect on enzyme activity in seeds of Brassica napus and Nicotiana tabacum

2010-05-01

Abstract excerpt

One of the potential drawbacks of the use of plant-based systems for production of human glycoproteins is the presence of immunogenic sugars within the protein's glycans, especially xylose. This can occur as a consequence of the protein undergoing transit through the plant Golgi complex, in which modifying enzymes may convert the high-mannose N-glycans of the recombinant protein to complex forms. In an effort to m...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
e676009a-1c65-5187-bae7-d44ce318dfa9
DOI
10.1016/j.plantsci.2010.02.004
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
The carboxy-terminal ER-retention motif, SEKDEL, influences the N-linked glycosylation of recombinant human α-l-iduronidase but has little effect on enzyme activity in seeds of Brassica napus and Nicotiana tabacumDOI 10.1016/j.plantsci.2010.02.004
Select a neighboring publication to make it the new centre.