| pubmed-article:2846524 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C0015278 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C1414899 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C0599814 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2846524 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:2846524 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2846524 | pubmed:dateCreated | 1988-12-22 | lld:pubmed |
| pubmed-article:2846524 | pubmed:abstractText | Intracellular transport of two lysosomal enzymes, acid alpha-glucosidase and beta-hexosaminidase, was analyzed in human fibroblasts. The precursors of beta-hexosaminidase in normal fibroblasts were released from the membrane fraction by treatment with mannose 6-phosphate, but the precursor of alpha-glucosidase was not. Percoll density gradient centrifugation revealed a normal amount of acid alpha-glucosidase activity in heavy lysosomes in I-cell disease fibroblasts despite impaired maturation and defective phosphorylation, and beta-hexosaminidase activity was markedly reduced in lysosomes. It was concluded that the membrane-bound precursor of acid alpha-glucosidase is transported to lysosomes by a phosphomannosyl receptor-independent system although the enzyme lacks the recognition marker for the phosphomannosyl receptor and processing of an intermediate form to mature forms does not occur in this disease. | lld:pubmed |
| pubmed-article:2846524 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2846524 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2846524 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2846524 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2846524 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2846524 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2846524 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2846524 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2846524 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2846524 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:2846524 | pubmed:author | pubmed-author:SuzukiYY | lld:pubmed |
| pubmed-article:2846524 | pubmed:author | pubmed-author:TsujiAA | lld:pubmed |
| pubmed-article:2846524 | pubmed:author | pubmed-author:OmuraKK | lld:pubmed |
| pubmed-article:2846524 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2846524 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:2846524 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2846524 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2846524 | pubmed:pagination | 276-8 | lld:pubmed |
| pubmed-article:2846524 | pubmed:dateRevised | 2008-8-22 | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:meshHeading | pubmed-meshheading:2846524-... | lld:pubmed |
| pubmed-article:2846524 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2846524 | pubmed:articleTitle | Intracellular transport of acid alpha-glucosidase in human fibroblasts: evidence for involvement of phosphomannosyl receptor-independent system. | lld:pubmed |
| pubmed-article:2846524 | pubmed:affiliation | Division of Inherited Metabolic Disease, National Institute of Neuroscience, Tokyo. | lld:pubmed |
| pubmed-article:2846524 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2846524 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2846524 | lld:pubmed |
