| pubmed-article:12049672 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12049672 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:12049672 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12049672 | lifeskim:mentions | umls-concept:C1423702 | lld:lifeskim |
| pubmed-article:12049672 | lifeskim:mentions | umls-concept:C0056080 | lld:lifeskim |
| pubmed-article:12049672 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12049672 | pubmed:dateCreated | 2002-6-6 | lld:pubmed |
| pubmed-article:12049672 | pubmed:abstractText | The ADF/cofilins are a family of actin-binding proteins expressed in all eukaryotic cells so far examined. Members of this family remodel the actin cytoskeleton, for example during cytokinesis, when the actin-rich contractile ring shrinks as it contracts through the interaction of ADF/cofilins with both monomeric and filamentous actin. The depolymerizing activity is twofold: ADF/cofilins sever actin filaments and also increase the rate at which monomers leave the filament's pointed end. The three-dimensional structure of ADF/cofilins is similar to a fold in members of the gelsolin family of actin-binding proteins in which this fold is typically repeated three or six times; although both families bind polyphosphoinositide lipids and actin in a pH-dependent manner, they share no obvious sequence similarity. Plants and animals have multiple ADF/cofilin genes, belonging in vertebrates to two types, ADF and cofilins. Other eukaryotes (such as yeast, Acanthamoeba and slime moulds) have a single ADF/cofilin gene. Phylogenetic analysis of the ADF/cofilins reveals that, with few exceptions, their relationships reflect conventional views of the relationships between the major groups of organisms. | lld:pubmed |
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| pubmed-article:12049672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12049672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12049672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12049672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12049672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12049672 | pubmed:issn | 1465-6914 | lld:pubmed |
| pubmed-article:12049672 | pubmed:author | pubmed-author:HusseyPatrick... | lld:pubmed |
| pubmed-article:12049672 | pubmed:author | pubmed-author:MaciverSuther... | lld:pubmed |
| pubmed-article:12049672 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:12049672 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:12049672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12049672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12049672 | pubmed:pagination | reviews3007 | lld:pubmed |
| pubmed-article:12049672 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
