| pubmed-article:10191114 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10191114 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10191114 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:10191114 | lifeskim:mentions | umls-concept:C1413495 | lld:lifeskim |
| pubmed-article:10191114 | lifeskim:mentions | umls-concept:C0033666 | lld:lifeskim |
| pubmed-article:10191114 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10191114 | pubmed:dateCreated | 1999-6-22 | lld:pubmed |
| pubmed-article:10191114 | pubmed:abstractText | The CLN3 gene associated with Batten disease and encoding a novel protein of a predicted 438 amino acids was cloned in 1995 by the International Batten Disease Consortium. The function of CLN3 protein remains unknown. Computer-based analysis predicted that CLN3 may contain several posttranslational modifications. Thus, to study the posttranslational modification of CLN3 protein, we have expressed a full-length CLN3 protein as a C-terminal fusion with green fluorescent protein of the jellyfish Aequerea victoria in a Chinese hamster ovary cell line. Previously, we have shown that CLN3 is a glycosylated protein from lysosomal compartment, and now, by using in vivo labeling with 32P, detection with anti-phosphoamino acid antibodies, and phosphoamino acid analysis, we demonstrate that CLN3 is a phosphorylated protein. We demonstrate that CLN3 protein does not undergo mannose 6-phosphate modification and that it is a membrane protein. Furthermore, we show that the level of CLN3 protein phosphorylation may be modulated by several protein kinases and phosphatases activators or inhibitors. | lld:pubmed |
| pubmed-article:10191114 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10191114 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191114 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10191114 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10191114 | pubmed:issn | 1096-7192 | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:KaczmarskiWW | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:KidaEE | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:WisniewskiK... | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:GolabekA AAA | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:KaczmarskiAA | lld:pubmed |
| pubmed-article:10191114 | pubmed:author | pubmed-author:MichalewskiM... | lld:pubmed |
| pubmed-article:10191114 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10191114 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10191114 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:10191114 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10191114 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10191114 | pubmed:pagination | 272-6 | lld:pubmed |
| pubmed-article:10191114 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10191114 | pubmed:meshHeading | pubmed-meshheading:10191114... | lld:pubmed |
| pubmed-article:10191114 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10191114 | pubmed:articleTitle | Posttranslational modification of CLN3 protein and its possible functional implication. | lld:pubmed |
| pubmed-article:10191114 | pubmed:affiliation | Department of Pathological Neurobiology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York 10314, USA. | lld:pubmed |
| pubmed-article:10191114 | pubmed:publicationType | Journal Article | lld:pubmed |
