pubmed-article:2167312 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:2167312 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C0077732 | lld:lifeskim |
pubmed-article:2167312 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:2167312 | pubmed:issue | 24 | lld:pubmed |
pubmed-article:2167312 | pubmed:dateCreated | 1990-9-27 | lld:pubmed |
pubmed-article:2167312 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2167312 | pubmed:abstractText | UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase (GPT) catalyzes the initial reaction required for synthesis of dolichol-P-P-oligosaccharides. We report here on the sequence and expression of a full-length cDNA clone encoding hamster GPT. The cDNA predicts a protein of 408 amino acid residues including 10 hydrophobic segments. Several portions of the hamster GPT sequence constituting one-third of the protein have 60% or greater identity with yeast GPT, and one-half of the conserved sequence falls within the hydrophobic segments. In addition, hamster GPT has two copies of a putative dolichol recognition sequence recently identified in three yeast enzymes that interact with dolichol. The protein lacks KDEL or DEKKMP-type carboxyl-terminal ER sorting sequences. When expressed in COS-1 cells, the cDNA causes a 5-7-fold increase of GPT activity in membrane fractions. The activity was completely inhibitable by tunicamycin, and the primary product was shown to be GlcNAc-pyrophosphoryldolichol. This cDNA represents the first enzyme of the dolichol-oligosaccharide biosynthetic pathway to be cloned from a vertebrate source and demonstrates structural homology between the enzymes of the yeast and mammalian pathways. | lld:pubmed |
pubmed-article:2167312 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2167312 | pubmed:language | eng | lld:pubmed |
pubmed-article:2167312 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2167312 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2167312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2167312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2167312 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2167312 | pubmed:month | Aug | lld:pubmed |
pubmed-article:2167312 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2167312 | pubmed:author | pubmed-author:YehW SWS | lld:pubmed |
pubmed-article:2167312 | pubmed:author | pubmed-author:LehrmanM AMA | lld:pubmed |
pubmed-article:2167312 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2167312 | pubmed:day | 25 | lld:pubmed |
pubmed-article:2167312 | pubmed:volume | 265 | lld:pubmed |
pubmed-article:2167312 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2167312 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2167312 | pubmed:pagination | 14250-5 | lld:pubmed |
pubmed-article:2167312 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2167312 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2167312 | pubmed:articleTitle | Cloning, sequence, and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase. | lld:pubmed |
pubmed-article:2167312 | pubmed:affiliation | Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235. | lld:pubmed |
pubmed-article:2167312 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2167312 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2167312 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2167312 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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