pubmed-article:20171176 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20171176 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
pubmed-article:20171176 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:20171176 | lifeskim:mentions | umls-concept:C0023828 | lld:lifeskim |
pubmed-article:20171176 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:20171176 | lifeskim:mentions | umls-concept:C0032521 | lld:lifeskim |
pubmed-article:20171176 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:20171176 | pubmed:dateCreated | 2010-3-22 | lld:pubmed |
pubmed-article:20171176 | pubmed:abstractText | The Arabidopsis dynamin-related protein 1A (AtDRP1A) is involved in endocytosis and cell plate maturation in Arabidopsis. Unlike dynamin, AtDRP1A does not have any recognized membrane binding or protein-protein interaction domains. We report that GTPase active AtDRP1A purified from Escherichia coli as a fusion to maltose binding protein forms homopolymers visible by negative staining electron microscopy. These polymers interact with protein-free liposomes whose lipid composition mimics that of the inner leaflet of the Arabidopsis plasma membrane, suggesting that lipid-binding may play a role in AtDRP1A function. However, AtDRP1A polymers do not appear to assemble and disassemble in a dynamic fashion and do not have the ability to tubulate liposomes in vitro, suggesting that additional factors or modifications are necessary for AtDRP1A's in vivo function. | lld:pubmed |
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pubmed-article:20171176 | pubmed:language | eng | lld:pubmed |
pubmed-article:20171176 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20171176 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:20171176 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20171176 | pubmed:month | Mar | lld:pubmed |
pubmed-article:20171176 | pubmed:issn | 1090-2104 | lld:pubmed |
pubmed-article:20171176 | pubmed:author | pubmed-author:BednarekSebas... | lld:pubmed |
pubmed-article:20171176 | pubmed:author | pubmed-author:BackuesSteven... | lld:pubmed |
pubmed-article:20171176 | pubmed:copyrightInfo | Copyright 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
pubmed-article:20171176 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20171176 | pubmed:day | 19 | lld:pubmed |
pubmed-article:20171176 | pubmed:volume | 393 | lld:pubmed |
pubmed-article:20171176 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20171176 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20171176 | pubmed:pagination | 734-9 | lld:pubmed |
pubmed-article:20171176 | pubmed:dateRevised | 2010-9-30 | lld:pubmed |
pubmed-article:20171176 | pubmed:meshHeading | pubmed-meshheading:20171176... | lld:pubmed |
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pubmed-article:20171176 | pubmed:meshHeading | pubmed-meshheading:20171176... | lld:pubmed |
pubmed-article:20171176 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20171176 | pubmed:articleTitle | Arabidopsis dynamin-related protein 1A polymers bind, but do not tubulate, liposomes. | lld:pubmed |
pubmed-article:20171176 | pubmed:affiliation | Department of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr., Madison, WI 53706, USA. | lld:pubmed |
pubmed-article:20171176 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20171176 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:20171176 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:834213 | entrezgene:pubmed | pubmed-article:20171176 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20171176 | lld:entrezgene |