pubmed-article:12615067 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0205378 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0751383 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C1823885 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
pubmed-article:12615067 | lifeskim:mentions | umls-concept:C1520210 | lld:lifeskim |
pubmed-article:12615067 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12615067 | pubmed:dateCreated | 2003-3-4 | lld:pubmed |
pubmed-article:12615067 | pubmed:abstractText | Btn2p is a novel coiled coil cytosolic protein in Saccharomyces cerevisiae. We report that Btn2p interacts with Yif1p, a component of a protein complex at the Golgi that functions in ER to Golgi transport. Deletion of Btn2p, btn2-delta, results in mis-localiztion of Yif1p to the vacuole. Therefore, Btn2p may have an apparent role in intracellular trafficking of proteins. Btn2p was originally identified as being up-regulated in a btn1-delta strain, which exhibits dysregulation of vacuolar pH, and this up-regulation of Btn2p was presumed to contribute to maintaining a stable vacuolar pH [Pearce et al. Nat. Genet. 22 (1999) 55]. We propose that up-regulation of Btn2p in btn1-delta is an indicator of altered trafficking within the cell, and as btn1-delta serves as a model for the lysosomal storage disorder Batten disease, that altered intracellular trafficking may contribute to some of the cellular pathological hallmarks of this disease. | lld:pubmed |
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pubmed-article:12615067 | pubmed:language | eng | lld:pubmed |
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pubmed-article:12615067 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12615067 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12615067 | pubmed:month | Mar | lld:pubmed |
pubmed-article:12615067 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:12615067 | pubmed:author | pubmed-author:Chattopadhyay... | lld:pubmed |
pubmed-article:12615067 | pubmed:author | pubmed-author:PearceDavid... | lld:pubmed |
pubmed-article:12615067 | pubmed:author | pubmed-author:RobertsPaul... | lld:pubmed |
pubmed-article:12615067 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12615067 | pubmed:day | 14 | lld:pubmed |
pubmed-article:12615067 | pubmed:volume | 302 | lld:pubmed |
pubmed-article:12615067 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12615067 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12615067 | pubmed:pagination | 534-8 | lld:pubmed |
pubmed-article:12615067 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:12615067 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12615067 | pubmed:articleTitle | The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p. | lld:pubmed |
pubmed-article:12615067 | pubmed:affiliation | Center for Aging and Developmental Biology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA. subrata_chattopadhyay@urmc.rochester.edu | lld:pubmed |
pubmed-article:12615067 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12615067 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12615067 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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