| pubmed-article:2141027 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C0027103 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C0000879 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C1420192 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C1323418 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C1880180 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2141027 | lifeskim:mentions | umls-concept:C0444930 | lld:lifeskim |
| pubmed-article:2141027 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:2141027 | pubmed:dateCreated | 1990-7-16 | lld:pubmed |
| pubmed-article:2141027 | pubmed:abstractText | Myosin II from Acanthamoeba castellanii is a conventional myosin composed of two heavy chains and two pairs of light chains. The amino-terminal approximately 90 kDa of each heavy chain form a globular head that contains the ATPase site and an ATP-sensitive actin-binding site. The carboxyl-terminal approximately 80 kDa of both heavy chains interact to form a coiled coil, helical rod (through which the molecules self-associate into bipolar filaments) ending in a short nonhelical tailpiece. Phosphorylation of 3 serine residues at the tip of the tail (at positions 11, 16, and 21 from the carboxyl terminus) inactivates the actin-activated Mg2(+)-ATPase activity of myosin II filaments. Previous work had indicated that the activity of each myosin II molecule in a filament reflects the global state of phosphorylation of the filament rather than the phosphorylation state of the molecule itself. We have now purified the approximately 28-kDa carboxyl-terminal region of the heavy chain lacking the last two phosphorylation sites, and we have shown that this peptide copolymerizes with and regulates the actin-activated Mg2(+)-ATPase activities of native dephosphorylated and phosphorylated myosin II. It can be concluded from these studies that the biologically relevant enzymatic activity of myosin II is regulated by a phosphorylation-dependent conformational change in the myosin filaments. | lld:pubmed |
| pubmed-article:2141027 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2141027 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2141027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2141027 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2141027 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2141027 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:AttriA KAK | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:KornE DED | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:AtkinsonM AMA | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:BowersBB | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:GangulyCC | lld:pubmed |
| pubmed-article:2141027 | pubmed:author | pubmed-author:Sathyamoorthy... | lld:pubmed |
| pubmed-article:2141027 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2141027 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2141027 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2141027 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2141027 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2141027 | pubmed:pagination | 9993-8 | lld:pubmed |
| pubmed-article:2141027 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:meshHeading | pubmed-meshheading:2141027-... | lld:pubmed |
| pubmed-article:2141027 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2141027 | pubmed:articleTitle | Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain. | lld:pubmed |
| pubmed-article:2141027 | pubmed:affiliation | Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2141027 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2141027 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2141027 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2141027 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2141027 | lld:pubmed |
