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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1983-4-15
|
| pubmed:abstractText |
The biosynthesis of lysosomal enzymes entails a complex series of events. The nascent proteins enter the endoplasmic reticulum for glycosylation. Phosphorylation of the enzymes subsequently occurs in the Golgi area. Equipped with a phosphomannose recognition marker, the enzymes are bound to specific receptors and translocated to lysosomes. Mutations are known in the following steps: early glycosylation (CHO cells), phosphorylation (patients with I-cell disease and pseudo-Hurler polydystrophy), and receptor binding (CHO cells).
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0361-7742
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
103 Pt B
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
177-85
|
| pubmed:dateRevised |
2005-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:7163219-Animals,
pubmed-meshheading:7163219-Cell Line,
pubmed-meshheading:7163219-Cricetinae,
pubmed-meshheading:7163219-Cricetulus,
pubmed-meshheading:7163219-Enzymes,
pubmed-meshheading:7163219-Female,
pubmed-meshheading:7163219-Glycoproteins,
pubmed-meshheading:7163219-Humans,
pubmed-meshheading:7163219-Lysosomes,
pubmed-meshheading:7163219-Mucolipidoses,
pubmed-meshheading:7163219-Mutation,
pubmed-meshheading:7163219-Ovary
|
| pubmed:year |
1982
|
| pubmed:articleTitle |
Pleiotropic mutations of lysosomal function in human patients and in Chinese hamster ovary cells.
|
| pubmed:publicationType |
Journal Article
|