| pubmed-article:18292779 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18292779 | lifeskim:mentions | umls-concept:C0162340 | lld:lifeskim |
| pubmed-article:18292779 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
| pubmed-article:18292779 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18292779 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18292779 | pubmed:dateCreated | 2008-2-22 | lld:pubmed |
| pubmed-article:18292779 | pubmed:abstractText | Ribosomes, which are central to protein synthesis and convert transcribed mRNAs into polypeptide chains, have been the focus of structural and biochemical studies for more than 50 years. The structure of its larger subunit revealed that the ribosome is a ribozyme with RNA at the heart of its enzymatic activity that catalyses peptide bond formation. Numerous initiation, elongation and release factors ensure that protein synthesis occurs progressively and with high specificity. In the past few years, high-resolution structures have provided molecular snapshots of different intermediates in ribosome-mediated translation in atomic detail. Together, these studies have revolutionized our understanding of the mechanism of protein synthesis. | lld:pubmed |
| pubmed-article:18292779 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18292779 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18292779 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18292779 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18292779 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18292779 | pubmed:issn | 1471-0080 | lld:pubmed |
| pubmed-article:18292779 | pubmed:author | pubmed-author:SteitzThomas... | lld:pubmed |
| pubmed-article:18292779 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18292779 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:18292779 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18292779 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18292779 | pubmed:pagination | 242-53 | lld:pubmed |
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| pubmed-article:18292779 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18292779 | pubmed:articleTitle | A structural understanding of the dynamic ribosome machine. | lld:pubmed |
| pubmed-article:18292779 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Department of Chemistry, Yale University, and the Howard Hughes Medical Institute, New Haven, Connecticut 06520-8114, USA. peggy.eatherton@yale.edu | lld:pubmed |
| pubmed-article:18292779 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18292779 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:18292779 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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