Source:http://linkedlifedata.com/resource/pubmed/id/14731403
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2004-1-20
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| pubmed:abstractText |
Dynamin is a large GTPase implicated in controlling the initial stages of endocytosis. Its mechanism of action remains uncertain, but it is expected to interact cyclically with components of the endocytic machinery. Dynamin binds to a number of different macromolecules, including microtubules, SH3-domain-containing proteins, and acidic phospholipids. We interpret these findings in terms of a cooperative interaction between dynamin and components of coated and non-coated pits.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0962-8924
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
43-7
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| pubmed:year |
1995
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| pubmed:articleTitle |
The regulation of endocytosis: identifying dynamin's binding partners.
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| pubmed:affiliation |
Worcester Foundation for Experimental Biology, 222 Maple Ave, Shrewsbury, MA 01545, USA.
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| pubmed:publicationType |
Journal Article
|