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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1985-11-1
|
pubmed:abstractText |
Actin filaments can assemble at the barbed end and disassemble simultaneously at the pointed end. Prerequisites for this treadmilling reaction are the structural polarity of actin filaments and tight coupling of the actin assembly reaction and the adenosine triphosphate hydrolysis occurring during actin polymerization. In this article, investigations on the actin treadmill are reviewed.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0714-7511
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
63
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
414-21
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3899328-Actins,
pubmed-meshheading:3899328-Adenosine Triphosphate,
pubmed-meshheading:3899328-Animals,
pubmed-meshheading:3899328-Hydrolysis,
pubmed-meshheading:3899328-Macromolecular Substances,
pubmed-meshheading:3899328-Models, Biological,
pubmed-meshheading:3899328-Protein Binding
|
pubmed:year |
1985
|
pubmed:articleTitle |
The actin treadmill.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|