pubmed-article:470613 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C0242697 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C0035028 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C1704970 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C0026022 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:470613 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
pubmed-article:470613 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:470613 | pubmed:dateCreated | 1979-10-26 | lld:pubmed |
pubmed-article:470613 | pubmed:abstractText | By means of polarized ultraviolet fluorescence microscopy the conformational changes of F-actin occuring in glycerinated muscle fibers of rabbit and barnacle (Balanus rostratus Hock.) under the influence of adenosine triphosphate in the presence of ethylene glycol bis(beta-amino-ethyl ether)-N,N'-tetraacetic acid were discovered. These changes seem to be located near the surface of the globules thus hampering the penetration of univalent iones and neutral molecules into the F-actin macromolecule. It is suggested that similar changes of F-actin take place in thin myofilaments of living muscle fiber during the contraction-relaxation process. | lld:pubmed |
pubmed-article:470613 | pubmed:language | eng | lld:pubmed |
pubmed-article:470613 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:470613 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:470613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:470613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:470613 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:470613 | pubmed:month | May | lld:pubmed |
pubmed-article:470613 | pubmed:issn | 0044-376X | lld:pubmed |
pubmed-article:470613 | pubmed:author | pubmed-author:Chernogriadsk... | lld:pubmed |
pubmed-article:470613 | pubmed:author | pubmed-author:BorovikovY... | lld:pubmed |
pubmed-article:470613 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:470613 | pubmed:volume | 81 | lld:pubmed |
pubmed-article:470613 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:470613 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:470613 | pubmed:pagination | 383-92 | lld:pubmed |
pubmed-article:470613 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
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pubmed-article:470613 | pubmed:meshHeading | pubmed-meshheading:470613-M... | lld:pubmed |
pubmed-article:470613 | pubmed:year | 1979 | lld:pubmed |
pubmed-article:470613 | pubmed:articleTitle | Studies on conformational changes in F-actin of glycerinated muscle fibers during relaxation by means of polarized ultraviolet fluorescence microscopy. | lld:pubmed |
pubmed-article:470613 | pubmed:publicationType | Journal Article | lld:pubmed |
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