| pubmed-article:19505460 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19505460 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:19505460 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:19505460 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:19505460 | lifeskim:mentions | umls-concept:C1417953 | lld:lifeskim |
| pubmed-article:19505460 | lifeskim:mentions | umls-concept:C1156067 | lld:lifeskim |
| pubmed-article:19505460 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:19505460 | pubmed:dateCreated | 2009-7-6 | lld:pubmed |
| pubmed-article:19505460 | pubmed:abstractText | The mitochondrial dynamin-like GTPase Mgm1 exists as a long (l-Mgm1) and a short isoform (s-Mgm1). They both are essential for mitochondrial fusion. Here we show that the isoforms interact in a homotypic and heterotypic manner. Their submitochondrial distribution between inner boundary membrane and cristae was markedly different. Overexpression of l-Mgm1 exerts a dominant negative effect on mitochondrial fusion. A functional GTPase domain is required only in s-Mgm1 but not in l-Mgm1. We propose that l-Mgm1 acts primarily as an anchor in the inner membrane that in concert with the GTPase activity of s-Mgm1 mediates the fusion of inner membranes. | lld:pubmed |
| pubmed-article:19505460 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19505460 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19505460 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19505460 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19505460 | pubmed:issn | 1873-3468 | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:NeupertWalter... | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:VogelFrankF | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:Duvezin-Caube... | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:ReichertAndre... | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:SchäferAnjaA | lld:pubmed |
| pubmed-article:19505460 | pubmed:author | pubmed-author:ZickMichaelM | lld:pubmed |
| pubmed-article:19505460 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19505460 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:19505460 | pubmed:volume | 583 | lld:pubmed |
| pubmed-article:19505460 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19505460 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19505460 | pubmed:pagination | 2237-43 | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:meshHeading | pubmed-meshheading:19505460... | lld:pubmed |
| pubmed-article:19505460 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19505460 | pubmed:articleTitle | Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion. | lld:pubmed |
| pubmed-article:19505460 | pubmed:affiliation | Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, München, Germany. | lld:pubmed |
| pubmed-article:19505460 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19505460 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:854386 | entrezgene:pubmed | pubmed-article:19505460 | lld:entrezgene |
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