| pubmed-article:126084 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:126084 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:126084 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
| pubmed-article:126084 | lifeskim:mentions | umls-concept:C0031312 | lld:lifeskim |
| pubmed-article:126084 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:126084 | lifeskim:mentions | umls-concept:C0314672 | lld:lifeskim |
| pubmed-article:126084 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:126084 | pubmed:dateCreated | 1975-12-11 | lld:pubmed |
| pubmed-article:126084 | pubmed:abstractText | The cyclic peptide phalloidin, one of the toxic components of Amanita phalloides prevented the drop of viscosity of F-actin solutions after the addition of 0.6 M KI and inhibited the ATP splitting of F-actin during sonic vibration. The data concerning ATP splitting are consistent with the assumption (a) that only 1 out of every 3 actin units of the filaments needs to be combined with phalloidin in order to suppress the contribution of these 3 actins to the ATPase activity of the filament and (b) that all actin units of the filaments can combine with phalloidin with a very high affinity. -halloidin did not only stabilize the actin-actin bonds in the F-actin structure but it also increased the rate of polymerization of G-actin to F-actin. The ability of F-actin to activate myosin ATPase was not affected by phalloidin. The tropomyosin-troponin complex did not prevent the stabilizing effect of phalloidin on the F-actin structure. | lld:pubmed |
| pubmed-article:126084 | pubmed:language | eng | lld:pubmed |
| pubmed-article:126084 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:126084 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:126084 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:126084 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:126084 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:126084 | pubmed:author | pubmed-author:HasselbachWW | lld:pubmed |
| pubmed-article:126084 | pubmed:author | pubmed-author:WielandTT | lld:pubmed |
| pubmed-article:126084 | pubmed:author | pubmed-author:LöwII | lld:pubmed |
| pubmed-article:126084 | pubmed:author | pubmed-author:DanckerPP | lld:pubmed |
| pubmed-article:126084 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:126084 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:126084 | pubmed:volume | 400 | lld:pubmed |
| pubmed-article:126084 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:126084 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:126084 | pubmed:pagination | 407-14 | lld:pubmed |
| pubmed-article:126084 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:126084 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:126084 | pubmed:articleTitle | Interaction of actin with phalloidin: polymerization and stabilization of F-actin. | lld:pubmed |
| pubmed-article:126084 | pubmed:publicationType | Journal Article | lld:pubmed |
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