| pubmed-article:2506440 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C0030943 | lld:lifeskim |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C1706204 | lld:lifeskim |
| pubmed-article:2506440 | lifeskim:mentions | umls-concept:C1555721 | lld:lifeskim |
| pubmed-article:2506440 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:2506440 | pubmed:dateCreated | 1989-10-26 | lld:pubmed |
| pubmed-article:2506440 | pubmed:abstractText | Eucaryotic initiation factor 4A (eIF-4A) is a member of a family of proteins believed to be involved in the ATP-dependent melting of RNA secondary structure. These proteins contain a derivative of the consensus ATP-binding site AXXGXGKT. To assess the importance of the consensus amino acid sequence in eIF-4A for ATP binding, we mutated the consensus amino-proximal glycine and lysine to isoleucine and asparagine, respectively. The effect of the mutations was examined by UV-induced cross-linking of [alpha-32P]dATP to eIF-4A. Mutation of the lysine residue (but not of the glycine residue) resulted in the loss of [alpha-32P]dATP cross-linking to eIF-4A, suggesting that the lysine is an important determinant in ATP binding to eIF-4A. | lld:pubmed |
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| pubmed-article:2506440 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2506440 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2506440 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2506440 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2506440 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2506440 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2506440 | pubmed:author | pubmed-author:PelletierJJ | lld:pubmed |
| pubmed-article:2506440 | pubmed:author | pubmed-author:TrachselHH | lld:pubmed |
| pubmed-article:2506440 | pubmed:author | pubmed-author:SonenbergNN | lld:pubmed |
| pubmed-article:2506440 | pubmed:author | pubmed-author:RozekCC | lld:pubmed |
| pubmed-article:2506440 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2506440 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2506440 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2506440 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2506440 | pubmed:pagination | 4061-3 | lld:pubmed |
| pubmed-article:2506440 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2506440 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2506440 | pubmed:articleTitle | A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity. | lld:pubmed |
| pubmed-article:2506440 | pubmed:affiliation | Department of Biochemistry, McGill University, Montreal, Quebec, Canada. | lld:pubmed |
| pubmed-article:2506440 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2506440 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2506440 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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