| pubmed-article:1409665 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0031713 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0917783 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0599748 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:1409665 | lifeskim:mentions | umls-concept:C0073869 | lld:lifeskim |
| pubmed-article:1409665 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:1409665 | pubmed:dateCreated | 1992-11-17 | lld:pubmed |
| pubmed-article:1409665 | pubmed:abstractText | The primary structure of the alpha and beta subunits of phosphorylase kinase reveals that both proteins contain a carboxyl-terminal CA1A2X motif (where C is cysteine, A1 and A2 are aliphatic amino acids, and X is an uncharged amino acid), the recognition signal for a protein polyisoprenyltransferase. The product, a polyisoprenylated cysteine, can be detected by phenylthiocarbamoylamino acid analysis and by microsequencing following conversion to S-ethylcysteine. Mass spectrometry confirms a covalently linked farnesyl residue in both subunits. Tandem mass spectrometry localizes these modifications at the cysteine residues present in the carboxyl-terminal CAMQ and CLVS sequences of the alpha and beta subunits, respectively. Membrane association of phosphorylase kinase, probably mediated by these farnesyl residues, is discussed. | lld:pubmed |
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| pubmed-article:1409665 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1409665 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1409665 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1409665 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1409665 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:HeilmeyerL... | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:MetzgerJJ | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:WeberCC | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:MeyerH EHE | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:Hoffmann-Poso... | lld:pubmed |
| pubmed-article:1409665 | pubmed:author | pubmed-author:SerweMM | lld:pubmed |
| pubmed-article:1409665 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1409665 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1409665 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:1409665 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1409665 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1409665 | pubmed:pagination | 9554-8 | lld:pubmed |
| pubmed-article:1409665 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1409665 | pubmed:meshHeading | pubmed-meshheading:1409665-... | lld:pubmed |
| pubmed-article:1409665 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1409665 | pubmed:articleTitle | Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletal muscle phosphorylase kinase: localization by conversion to S-ethylcysteine and by tandem mass spectrometry. | lld:pubmed |
| pubmed-article:1409665 | pubmed:affiliation | Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1409665 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1409665 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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