| pubmed-article:3512269 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0017963 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0059036 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C1879746 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C1547011 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:3512269 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
| pubmed-article:3512269 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3512269 | pubmed:dateCreated | 1986-4-16 | lld:pubmed |
| pubmed-article:3512269 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3512269 | pubmed:abstractText | The primary structure of the alpha subunit of elongation factor 1 (EF-1 alpha) from human MOLT 4 cells was determined by cDNA sequencing. The data show that the conservation of the amino acid sequence is more than 80% when compared with yeast and Artemia EF-1 alpha. An inventory of amino acid sequences around the guanine-nucleotide-binding site in elongation factor Tu from Escherichia coli and homologous amino acid sequences in G proteins, initiation and elongation factors and proteins from the RAS family shows two regions containing conserved sequence elements. Region I has the sequence apolar-Xaa-Xaa-Xaa-Gly-Xaa-Xaa-Yaa-Xaa-Gly-LYs-Thr(Ser)- -Xaa-Xaa-Xaa-Xaa-X-apolar. Except for RAS proteins, Yaa is always an acidic amino acid residue. Region II is characterized by the invariant sequence apolar-apolar-Xaa-Xaa-Asn-Lys-Xaa-Asp. In order to facilitate sequence comparison we have used a graphic display, which is based on the hydrophilicity values of individual amino acids in a sequence. | lld:pubmed |
| pubmed-article:3512269 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3512269 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3512269 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3512269 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3512269 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3512269 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:3512269 | pubmed:author | pubmed-author:MöllerWW | lld:pubmed |
| pubmed-article:3512269 | pubmed:author | pubmed-author:AmonsRR | lld:pubmed |
| pubmed-article:3512269 | pubmed:author | pubmed-author:MaassenJ AJA | lld:pubmed |
| pubmed-article:3512269 | pubmed:author | pubmed-author:van HemertF... | lld:pubmed |
| pubmed-article:3512269 | pubmed:author | pubmed-author:BrandsJ HJH | lld:pubmed |
| pubmed-article:3512269 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3512269 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:3512269 | pubmed:volume | 155 | lld:pubmed |
| pubmed-article:3512269 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3512269 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3512269 | pubmed:pagination | 167-71 | lld:pubmed |
| pubmed-article:3512269 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:3512269 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3512269 | pubmed:articleTitle | The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. | lld:pubmed |
| pubmed-article:3512269 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3512269 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3512269 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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