| pubmed-article:15933718 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15933718 | lifeskim:mentions | umls-concept:C0162540 | lld:lifeskim |
| pubmed-article:15933718 | lifeskim:mentions | umls-concept:C0039259 | lld:lifeskim |
| pubmed-article:15933718 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15933718 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:15933718 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:15933718 | pubmed:dateCreated | 2005-6-15 | lld:pubmed |
| pubmed-article:15933718 | pubmed:abstractText | The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation. | lld:pubmed |
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| pubmed-article:15933718 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15933718 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15933718 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15933718 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15933718 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:15933718 | pubmed:author | pubmed-author:TangLiangL | lld:pubmed |
| pubmed-article:15933718 | pubmed:author | pubmed-author:JohnsonJohn... | lld:pubmed |
| pubmed-article:15933718 | pubmed:author | pubmed-author:CingolaniGino... | lld:pubmed |
| pubmed-article:15933718 | pubmed:author | pubmed-author:PreveligePete... | lld:pubmed |
| pubmed-article:15933718 | pubmed:author | pubmed-author:MarionWilliam... | lld:pubmed |
| pubmed-article:15933718 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15933718 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15933718 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:15933718 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15933718 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15933718 | pubmed:pagination | 2087-95 | lld:pubmed |
| pubmed-article:15933718 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15933718 | pubmed:meshHeading | pubmed-meshheading:15933718... | lld:pubmed |
| pubmed-article:15933718 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15933718 | pubmed:articleTitle | Three-dimensional structure of the bacteriophage P22 tail machine. | lld:pubmed |
| pubmed-article:15933718 | pubmed:affiliation | Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:15933718 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15933718 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15933718 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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