| pubmed-article:1637863 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0003284 | lld:lifeskim |
| pubmed-article:1637863 | lifeskim:mentions | umls-concept:C0035728 | lld:lifeskim |
| pubmed-article:1637863 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1637863 | pubmed:dateCreated | 1992-9-1 | lld:pubmed |
| pubmed-article:1637863 | pubmed:abstractText | Yeast tRNA(Phe), containing the photoreactive nucleoside 2-azidoadenosine at position 37 within the anticodon loop, has been cross-linked to the aminoacyl-tRNA (A) and peptidyl-tRNA (P) binding sites of the Escherichia coli ribosome. The 30S subunit was exclusively labeled in each case, and cross-linking occurred to both protein and 16S rRNA. Electrophoretic and immunological analyses demonstrated that S7 was the only 30S-subunit protein covalently attached to the tRNA. However, digestion of the A and P site-labeled S7 with trypsin revealed a unique pattern of cross-linked peptide(s) at each site. Thus, while the anticodon loop of tRNA is in close proximity to protein S7 at both the A and P sites, it neighbors a different portion of the protein molecule in each. The placement of the aminoacyl- and peptidyl-tRNA binding sites is discussed in relationship to recent models of the 30S ribosomal subunit. | lld:pubmed |
| pubmed-article:1637863 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1637863 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1637863 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1637863 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1637863 | pubmed:issn | 0300-9084 | lld:pubmed |
| pubmed-article:1637863 | pubmed:author | pubmed-author:WowerJJ | lld:pubmed |
| pubmed-article:1637863 | pubmed:author | pubmed-author:KopylovA MAM | lld:pubmed |
| pubmed-article:1637863 | pubmed:author | pubmed-author:ZimmermannR... | lld:pubmed |
| pubmed-article:1637863 | pubmed:author | pubmed-author:HixsonS SSS | lld:pubmed |
| pubmed-article:1637863 | pubmed:author | pubmed-author:SylversL ALA | lld:pubmed |
| pubmed-article:1637863 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1637863 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:1637863 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1637863 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1637863 | pubmed:pagination | 381-9 | lld:pubmed |
| pubmed-article:1637863 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:meshHeading | pubmed-meshheading:1637863-... | lld:pubmed |
| pubmed-article:1637863 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1637863 | pubmed:articleTitle | Photochemical cross-linking of the anticodon loop of yeast tRNA(Phe) to 30S-subunit protein S7 at the ribosomal A and P sites. | lld:pubmed |
| pubmed-article:1637863 | pubmed:affiliation | Program in Molecular and Cellular Biology, University of Massachusetts, Amherst 01003. | lld:pubmed |
| pubmed-article:1637863 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1637863 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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