| pubmed-article:3056714 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0018557 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0021270 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0553257 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0024369 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C0021699 | lld:lifeskim |
| pubmed-article:3056714 | lifeskim:mentions | umls-concept:C1870042 | lld:lifeskim |
| pubmed-article:3056714 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:3056714 | pubmed:dateCreated | 1989-1-4 | lld:pubmed |
| pubmed-article:3056714 | pubmed:abstractText | BHK cells transfected with human lysosomal acid phosphatase (LAP) cDNA (CT29) expressed 70-fold higher enzyme activities of acid phosphatase than non-transfected BHK cells. The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated. Transfer to the trans-Golgi was associated with a small increase in size (approximately 7 kd) and partial processing of the oligosaccharides to complex type structures. CT29-LAP was transferred into lysosomes as shown by subcellular fractionation, immunofluorescence and immunoelectron microscopy. Lack of mannose-6-phosphate residues suggested that transport does not involve mannose-6-phosphate receptors. Part of the membrane-associated CT29-LAP was processed to a soluble form. The mechanism that converts CT29-LAP into a soluble form was sensitive to NH4Cl, and reduced the size of the polypeptide by 7 kd. In vitro translation of CT29-derived cRNA in the presence of microsomal membranes yielded a CT29-LAP precursor that is protected from proteinase K except for a small peptide of approximately 2 kd. In combination with the sequence data available for LAP, these observations suggest that CT29-LAP is synthesized and transported to lysosomes as a transmembrane protein. In the lysosomes, CT29-LAP is released from the membrane by proteolytic cleavage, which removes a C-terminal peptide including the transmembrane domain and the cytosolic tail of 18 amino acids. | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3056714 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3056714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3056714 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3056714 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3056714 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:HauserHH | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:WaheedAA | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:von FiguraKK | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:HilleAA | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:GottschalkSS | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:GeuzeHH | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:BraulkeTT | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:PohlmannRR | lld:pubmed |
| pubmed-article:3056714 | pubmed:author | pubmed-author:KrentlerCC | lld:pubmed |
| pubmed-article:3056714 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3056714 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:3056714 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3056714 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3056714 | pubmed:pagination | 2351-8 | lld:pubmed |
| pubmed-article:3056714 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:meshHeading | pubmed-meshheading:3056714-... | lld:pubmed |
| pubmed-article:3056714 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3056714 | pubmed:articleTitle | Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells. | lld:pubmed |
| pubmed-article:3056714 | pubmed:affiliation | Zentrum Biochemie, Universität Göttingen, FRG. | lld:pubmed |
| pubmed-article:3056714 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3056714 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3056714 | lld:pubmed |
