| pubmed-article:8994878 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8994878 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:8994878 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:8994878 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8994878 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8994878 | pubmed:dateCreated | 1997-2-5 | lld:pubmed |
| pubmed-article:8994878 | pubmed:abstractText | Muscle contracts by the myosin cross-bridges "rowing' the actin filaments past the myosin filaments. In the past year many structural details of this mechanism have become clear. Structural studies indicate distinct states for myosin S1 in the rigor, ATP or "down' conformation and in the products complex (ADP.Pi) or "up' to state. Crystallographic studies substantiate this classification and yield details of the transformation. The isomerization "up' to "down' is the power stroke of muscle. This consists in the main of large changes of angle of the "lever arm' (at the distal part of the myosin head) which can account for an 11 nm power stroke. | lld:pubmed |
| pubmed-article:8994878 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8994878 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8994878 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8994878 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8994878 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8994878 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8994878 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8994878 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8994878 | pubmed:issn | 0959-440X | lld:pubmed |
| pubmed-article:8994878 | pubmed:author | pubmed-author:HolmesK CKC | lld:pubmed |
| pubmed-article:8994878 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8994878 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:8994878 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8994878 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8994878 | pubmed:pagination | 781-9 | lld:pubmed |
| pubmed-article:8994878 | pubmed:dateRevised | 2005-11-16 | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:meshHeading | pubmed-meshheading:8994878-... | lld:pubmed |
| pubmed-article:8994878 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8994878 | pubmed:articleTitle | Muscle proteins--their actions and interactions. | lld:pubmed |
| pubmed-article:8994878 | pubmed:affiliation | Max Planck Institut für medizinische Forschung, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:8994878 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8994878 | pubmed:publicationType | Review | lld:pubmed |
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