| pubmed-article:11474115 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11474115 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:11474115 | lifeskim:mentions | umls-concept:C0001459 | lld:lifeskim |
| pubmed-article:11474115 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:11474115 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:11474115 | pubmed:issue | 5530 | lld:pubmed |
| pubmed-article:11474115 | pubmed:dateCreated | 2001-7-27 | lld:pubmed |
| pubmed-article:11474115 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11474115 | pubmed:abstractText | The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5'-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5'-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin. | lld:pubmed |
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| pubmed-article:11474115 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11474115 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11474115 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11474115 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11474115 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:11474115 | pubmed:author | pubmed-author:DominguezRR | lld:pubmed |
| pubmed-article:11474115 | pubmed:author | pubmed-author:GraceffaPP | lld:pubmed |
| pubmed-article:11474115 | pubmed:author | pubmed-author:OtterbeinL... | lld:pubmed |
| pubmed-article:11474115 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11474115 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:11474115 | pubmed:volume | 293 | lld:pubmed |
| pubmed-article:11474115 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11474115 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11474115 | pubmed:pagination | 708-11 | lld:pubmed |
| pubmed-article:11474115 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11474115 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11474115 | pubmed:articleTitle | The crystal structure of uncomplexed actin in the ADP state. | lld:pubmed |
| pubmed-article:11474115 | pubmed:affiliation | Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA. | lld:pubmed |
| pubmed-article:11474115 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11474115 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11474115 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11474115 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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