| pubmed-article:2849826 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C0036208 | lld:lifeskim |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C0521387 | lld:lifeskim |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C0301624 | lld:lifeskim |
| pubmed-article:2849826 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2849826 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2849826 | pubmed:dateCreated | 1989-2-3 | lld:pubmed |
| pubmed-article:2849826 | pubmed:abstractText | It is established that Ca2+ transport from the predominantly inverted vesicles of pig myometrium sarcolemma depends on the value of the membrane potential which is created on vesicles by the K+-valinomycin system. It is shown that variations in the membrane potential from -60 to +30 mV cause acceleration of the calcium transport from the vesicles, the maximal transport being observed at delta psi from 0 up to +30 mV. The endogenic and exogenic cAMP-dependent phosphorylation of plasma membrane proteins inhibits the passive transport of calcium at all the membrane potential values studied. A degree of potential-dependent Ca2+ transport inhibition correlates with the value of cAMP-dependent phosphorylation of sarcolemma proteins. | lld:pubmed |
| pubmed-article:2849826 | pubmed:language | rus | lld:pubmed |
| pubmed-article:2849826 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2849826 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2849826 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2849826 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2849826 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2849826 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2849826 | pubmed:issn | 0201-8470 | lld:pubmed |
| pubmed-article:2849826 | pubmed:author | pubmed-author:Kurski?M DMD | lld:pubmed |
| pubmed-article:2849826 | pubmed:author | pubmed-author:KondratiukT... | lld:pubmed |
| pubmed-article:2849826 | pubmed:author | pubmed-author:BabichL GLG | lld:pubmed |
| pubmed-article:2849826 | pubmed:author | pubmed-author:BychenokS FSF | lld:pubmed |
| pubmed-article:2849826 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2849826 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:2849826 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2849826 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2849826 | pubmed:pagination | 30-4 | lld:pubmed |
| pubmed-article:2849826 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:meshHeading | pubmed-meshheading:2849826-... | lld:pubmed |
| pubmed-article:2849826 | pubmed:articleTitle | [cAMP-dependent phosphorylation inhibits potential-dependent passive transport of Ca2+ in myometrial sarcolemma vesicles]. | lld:pubmed |
| pubmed-article:2849826 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2849826 | pubmed:publicationType | English Abstract | lld:pubmed |
