pubmed-article:15866176 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15866176 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:15866176 | lifeskim:mentions | umls-concept:C0525021 | lld:lifeskim |
pubmed-article:15866176 | lifeskim:mentions | umls-concept:C1514916 | lld:lifeskim |
pubmed-article:15866176 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:15866176 | pubmed:dateCreated | 2005-5-3 | lld:pubmed |
pubmed-article:15866176 | pubmed:abstractText | Primary sequences of proteins often contain motifs that serve as "signatures" for subcellular targeting, such as a nuclear localization signal (NLS). However, many nuclear proteins do not harbor a recognizable NLS, and the pathways that mediate their nuclear translocation are unknown. This work focuses on CRABP-II, a cytosolic protein that moves to the nucleus upon binding of retinoic acid. While CRABP-II does not contain an NLS in its primary sequence, such a motif could be recognized in the protein's tertiary structure. We map the retinoic acid-induced structural rearrangements that result in the presence of this NLS in holo- but not apo-CRABP-II. The signal, whose three-dimensional configuration aligns strikingly well with a "classical" NLS, mediates ligand-induced association of CRABP-II with importin alpha and is critical for nuclear localization of the protein. The ligand-controlled NLS "switch" of CRABP-II may represent a general mechanism for posttranslational regulation of the subcellular distribution of a protein. | lld:pubmed |
pubmed-article:15866176 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:language | eng | lld:pubmed |
pubmed-article:15866176 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15866176 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15866176 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15866176 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15866176 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15866176 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:15866176 | pubmed:author | pubmed-author:AYY | lld:pubmed |
pubmed-article:15866176 | pubmed:author | pubmed-author:SesslerRichar... | lld:pubmed |
pubmed-article:15866176 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15866176 | pubmed:day | 29 | lld:pubmed |
pubmed-article:15866176 | pubmed:volume | 18 | lld:pubmed |
pubmed-article:15866176 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15866176 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15866176 | pubmed:pagination | 343-53 | lld:pubmed |
pubmed-article:15866176 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:15866176 | pubmed:meshHeading | pubmed-meshheading:15866176... | lld:pubmed |
pubmed-article:15866176 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15866176 | pubmed:articleTitle | A ligand-activated nuclear localization signal in cellular retinoic acid binding protein-II. | lld:pubmed |
pubmed-article:15866176 | pubmed:affiliation | Division of Nutritional Sciences, Cornell University, Ithaca, New York 14853, USA. | lld:pubmed |
pubmed-article:15866176 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15866176 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15866176 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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