pubmed-article:8539621 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8539621 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
pubmed-article:8539621 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:8539621 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
pubmed-article:8539621 | lifeskim:mentions | umls-concept:C1545588 | lld:lifeskim |
pubmed-article:8539621 | lifeskim:mentions | umls-concept:C0311417 | lld:lifeskim |
pubmed-article:8539621 | pubmed:issue | 5246 | lld:pubmed |
pubmed-article:8539621 | pubmed:dateCreated | 1996-2-8 | lld:pubmed |
pubmed-article:8539621 | pubmed:abstractText | Conventional myosin functions universally as a generator of motive force in eukaryotic cells. Analysis of mutants of the microorganism Dictyostelium discoideum revealed that myosin also provides resistance against high external osmolarities. An osmo-induced increase of intracellular guanosine 3',5'-monophosphate was shown to mediate phosphorylation of three threonine residues on the myosin tail, which caused a relocalization of myosin required to resist osmotic stress. This redistribution of myosin allowed cells to adopt a spherical shape and may provide physical strength to withstand extensive cell shrinkage in high osmolarities. | lld:pubmed |
pubmed-article:8539621 | pubmed:language | eng | lld:pubmed |
pubmed-article:8539621 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8539621 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8539621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8539621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8539621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8539621 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8539621 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8539621 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:8539621 | pubmed:author | pubmed-author:GerischGG | lld:pubmed |
pubmed-article:8539621 | pubmed:author | pubmed-author:KuwayamaHH | lld:pubmed |
pubmed-article:8539621 | pubmed:author | pubmed-author:EckeMM | lld:pubmed |
pubmed-article:8539621 | pubmed:author | pubmed-author:Van... | lld:pubmed |
pubmed-article:8539621 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8539621 | pubmed:day | 12 | lld:pubmed |
pubmed-article:8539621 | pubmed:volume | 271 | lld:pubmed |
pubmed-article:8539621 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8539621 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8539621 | pubmed:pagination | 207-9 | lld:pubmed |
pubmed-article:8539621 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:8539621 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8539621 | pubmed:articleTitle | Protection against osmotic stress by cGMP-mediated myosin phosphorylation. | lld:pubmed |
pubmed-article:8539621 | pubmed:affiliation | Department of Biochemistry, University of Groningen, Netherlands. | lld:pubmed |
pubmed-article:8539621 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8539621 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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