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| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C0007054 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C1157216 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C1554080 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C1706198 | lld:lifeskim |
| pubmed-article:11877387 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11877387 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11877387 | pubmed:dateCreated | 2002-5-6 | lld:pubmed |
| pubmed-article:11877387 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11877387 | pubmed:abstractText | UDP-glucuronate decarboxylase (UGD) catalyzes the formation of UDP-xylose from UDP-glucuronate. UDP-xylose is then used to initiate glycosaminoglycan biosynthesis on the core protein of proteoglycans. In a yeast two-hybrid screen with the protein kinase Akt (protein kinase B), we detected interactions with a novel sequence, which we cloned and expressed. The expressed protein displayed UGD activity but did not display the activities of homologous nucleotide sugar epimerases or dehydratases. We did not detect phosphorylation of UGD by Akt nor did we detect any influence of Akt on UGD activity. Effects of UGD on Akt kinase activity were also absent. Northern blot and Western blot analyses revealed the presence of UGD in multiple tissues and brain regions. Subcellular studies and histochemistry localized UGD protein to the perinuclear Golgi where xylosylation of proteoglycan core proteins is known to occur. | lld:pubmed |
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| pubmed-article:11877387 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11877387 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11877387 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11877387 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11877387 | pubmed:month | May | lld:pubmed |
| pubmed-article:11877387 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:MoriarityJohn... | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:HurtK... | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:SnyderSolomon... | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:SchnaarRonald... | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:LaroyWouterW | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:ResnickAdam... | lld:pubmed |
| pubmed-article:11877387 | pubmed:author | pubmed-author:StormPhillip... | lld:pubmed |
| pubmed-article:11877387 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11877387 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:11877387 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11877387 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11877387 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11877387 | pubmed:pagination | 16968-75 | lld:pubmed |
| pubmed-article:11877387 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11877387 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11877387 | pubmed:articleTitle | UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization. | lld:pubmed |
| pubmed-article:11877387 | pubmed:affiliation | Department of Neurological Surgery, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:11877387 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11877387 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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