| pubmed-article:8232542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C0012408 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1524062 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1883712 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1720086 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:8232542 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:8232542 | pubmed:issue | 6450 | lld:pubmed |
| pubmed-article:8232542 | pubmed:dateCreated | 1993-12-2 | lld:pubmed |
| pubmed-article:8232542 | pubmed:abstractText | Three different prenyltransferases have been identified in yeast and higher cells, the farnesyltransferase and the type I and type II geranylgeranyltransferases (GGTase). The farnesyltransferase and GGTase-I modify peptides in vitro with the CAAX (C, Cys; A, aliphatic residue; X, terminal amino acid) consensus motif. These enzymes are heterodimers that have different beta-subunits and a shared alpha-subunit. In yeast, the RAM2 gene encodes this alpha-subunit. RAM2 is also homologous to MAD2, a yeast gene whose product has been implicated in the feedback control of mitosis. We have shown that Bet2p is a component of the yeast GGTase-II (refs 6, 12) that geranylgeranylates Ypt1p, a small GTP-binding protein that mediates transport from the endoplasmic reticulum to the Golgi complex. Here we report that Mad2p is a component of this enzyme. Bet2p forms a complex with Mad2p that appears to bind geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate. The efficient transfer of geranylgeranyl onto small GTP-binding proteins requires the presence of an additional activity. | lld:pubmed |
| pubmed-article:8232542 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8232542 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8232542 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8232542 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8232542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8232542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8232542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8232542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8232542 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8232542 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:8232542 | pubmed:author | pubmed-author:RossiGG | lld:pubmed |
| pubmed-article:8232542 | pubmed:author | pubmed-author:JiangYY | lld:pubmed |
| pubmed-article:8232542 | pubmed:author | pubmed-author:Ferro-NovickS... | lld:pubmed |
| pubmed-article:8232542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8232542 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:8232542 | pubmed:volume | 366 | lld:pubmed |
| pubmed-article:8232542 | pubmed:geneSymbol | RAM2 | lld:pubmed |
| pubmed-article:8232542 | pubmed:geneSymbol | MAD2 | lld:pubmed |
| pubmed-article:8232542 | pubmed:geneSymbol | BET2 | lld:pubmed |
| pubmed-article:8232542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8232542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8232542 | pubmed:pagination | 84-6 | lld:pubmed |
| pubmed-article:8232542 | pubmed:dateRevised | 2009-7-14 | lld:pubmed |
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| pubmed-article:8232542 | pubmed:meshHeading | pubmed-meshheading:8232542-... | lld:pubmed |
| pubmed-article:8232542 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8232542 | pubmed:articleTitle | Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p. | lld:pubmed |
| pubmed-article:8232542 | pubmed:affiliation | Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510. | lld:pubmed |
| pubmed-article:8232542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8232542 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8232542 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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