pubmed-article:8460118 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0026597 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0012120 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0024779 | lld:lifeskim |
pubmed-article:8460118 | lifeskim:mentions | umls-concept:C0332246 | lld:lifeskim |
pubmed-article:8460118 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8460118 | pubmed:dateCreated | 1993-4-23 | lld:pubmed |
pubmed-article:8460118 | pubmed:abstractText | Amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin were replaced with histidine residues by site-directed mutagenesis. Mutant actins were expressed in Dictyostelium cells and purified to homogeneity. The sliding movement of mutant actin filaments on heavy meromyosin attached to a glass surface was measured to assess the effect of the mutation on the motility of actin. For two C-terminal mutants, force generated by a single actin filament and myosin was also measured. These measurements indicated that both D24/D25 and E99/E100 are involved in ATP-driven sliding, whereas E360/E361/D363/E364 are not essential for ATP-driven sliding and force generation. | lld:pubmed |
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pubmed-article:8460118 | pubmed:language | eng | lld:pubmed |
pubmed-article:8460118 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8460118 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8460118 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8460118 | pubmed:month | Mar | lld:pubmed |
pubmed-article:8460118 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:KojimaHH | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:SutohKK | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:YanagidaTT | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:IshijimaAA | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:ToyoshimaY... | lld:pubmed |
pubmed-article:8460118 | pubmed:author | pubmed-author:JoharaMM | lld:pubmed |
pubmed-article:8460118 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8460118 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8460118 | pubmed:volume | 90 | lld:pubmed |
pubmed-article:8460118 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8460118 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8460118 | pubmed:pagination | 2127-31 | lld:pubmed |
pubmed-article:8460118 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8460118 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8460118 | pubmed:articleTitle | Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. | lld:pubmed |
pubmed-article:8460118 | pubmed:affiliation | Department of Pure and Applied Sciences, College of Arts and Sciences, University of Tokyo, Japan. | lld:pubmed |
pubmed-article:8460118 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8460118 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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