| pubmed-article:11258942 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11258942 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
| pubmed-article:11258942 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:11258942 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11258942 | pubmed:dateCreated | 2001-3-22 | lld:pubmed |
| pubmed-article:11258942 | pubmed:abstractText | The publication of atomic resolution crystal structures for the large ribosomal subunit from Haloarcula marismortui and the small ribosomal subunit from Thermus thermophilus has permanently altered the way protein synthesis is conceptualized and experiments designed to address its unresolved issues. The impact of these structures on RNA biochemistry is certain to be no less profound. The background and substance of these developments are reviewed here. | lld:pubmed |
| pubmed-article:11258942 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258942 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11258942 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258942 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11258942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258942 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11258942 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11258942 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:11258942 | pubmed:author | pubmed-author:MooreP BPB | lld:pubmed |
| pubmed-article:11258942 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11258942 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:11258942 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:11258942 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11258942 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11258942 | pubmed:pagination | 3243-50 | lld:pubmed |
| pubmed-article:11258942 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:meshHeading | pubmed-meshheading:11258942... | lld:pubmed |
| pubmed-article:11258942 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11258942 | pubmed:articleTitle | The ribosome at atomic resolution. | lld:pubmed |
| pubmed-article:11258942 | pubmed:affiliation | Department of Chemistry, Yale University, New Haven, Connecticut 06520, USA. | lld:pubmed |
| pubmed-article:11258942 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11258942 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11258942 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:11258942 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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