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| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C0206755 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7664745 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:7664745 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:7664745 | pubmed:dateCreated | 1995-10-10 | lld:pubmed |
| pubmed-article:7664745 | pubmed:abstractText | The structures of the two domains of translational initiation factor IF3 from Bacillus stearothermophilus have been solved by X-ray crystallography using single wavelength anomalous scattering and multiwavelength anomalous diffraction. Each of the two domains has an alpha/beta topology, with an exposed beta-sheet that is reminiscent of several ribosomal and other RNA binding proteins. An alpha-helix that protrudes out from the body of the N-terminal domain towards the C-terminal domain suggests that IF3 consists of two RNA binding domains connected by an alpha-helix and that it may bridge two regions of the ribosome. This represents the first high resolution structural information on a translational initiation factor. | lld:pubmed |
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| pubmed-article:7664745 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7664745 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7664745 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7664745 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7664745 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7664745 | pubmed:author | pubmed-author:RamakrishnanV... | lld:pubmed |
| pubmed-article:7664745 | pubmed:author | pubmed-author:SirZZ | lld:pubmed |
| pubmed-article:7664745 | pubmed:author | pubmed-author:BiouVV | lld:pubmed |
| pubmed-article:7664745 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7664745 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7664745 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:7664745 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7664745 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7664745 | pubmed:pagination | 4056-64 | lld:pubmed |
| pubmed-article:7664745 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7664745 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7664745 | pubmed:articleTitle | X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. | lld:pubmed |
| pubmed-article:7664745 | pubmed:affiliation | Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA. | lld:pubmed |
| pubmed-article:7664745 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7664745 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7664745 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7664745 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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