Matches in UGent Biblio for { <https://biblio.ugent.be/publication/3087415#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B377825.
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- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 3087415.bibtex.
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- aggregation isPartOf urn:issn:1087-0156.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes".
- aggregation abstract "Lysosomal storage diseases are treated with human lysosomal enzymes produced in mammalian cells. Such enzyme therapeutics contain relatively low levels of mannose-6-phosphate, which is required to target them to the lysosomes of patient cells. Here we describe a method for increasing mannose-6-phosphate modification of lysosomal enzymes produced in yeast. We identified a glycosidase from C. cellulans that 'uncaps' N-glycans modified by yeast-type mannose-Pi-6-mannose to generate mammalian-type N-glycans with a mannose-6-phosphate substitution. Determination of the crystal structure of this glycosidase provided insight into its substrate specificity. We used this uncapping enzyme together with alpha-mannosidase to produce in yeast a form of the Pompe disease enzyme alpha-glucosidase rich in mannose-6-phosphate. Compared with the currently used therapeutic version, this form of alpha-glucosidase was more efficiently taken up by fibroblasts from Pompe disease patients, and it more effectively reduced cardiac muscular glycogen storage in a mouse model of the disease.".
- aggregation authorList BK682299.
- aggregation endPage "1231".
- aggregation issue "12".
- aggregation startPage "1225".
- aggregation volume "30".
- aggregation aggregates 3087438.
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