| pubmed-article:2904698 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2904698 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2904698 | lifeskim:mentions | umls-concept:C0021868 | lld:lifeskim |
| pubmed-article:2904698 | lifeskim:mentions | umls-concept:C1513112 | lld:lifeskim |
| pubmed-article:2904698 | lifeskim:mentions | umls-concept:C0008905 | lld:lifeskim |
| pubmed-article:2904698 | pubmed:issue | 4884 | lld:pubmed |
| pubmed-article:2904698 | pubmed:dateCreated | 1989-1-19 | lld:pubmed |
| pubmed-article:2904698 | pubmed:abstractText | Clathrin polymerization at the cytoplasmic side of the plasma membrane forms coated pits and vesicles that mediate uptake of cell surface receptors. Clathrin-coated vesicles have also been implicated in protein export but definition of their precise role has been controversial. Recent advances in characterization of the clathrin subunits and additional coated vesicle components have identified molecular interactions involved in clathrin polymerization and coated vesicle formation, and have provided new approaches to investigating its function. These studies suggest that clathrin's role, in both inward and outward membrane traffic, is to facilitate receptor transport by a concentration and sorting process that initiates targeting to specific intracellular compartments. | lld:pubmed |
| pubmed-article:2904698 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904698 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2904698 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904698 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2904698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904698 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2904698 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2904698 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2904698 | pubmed:author | pubmed-author:BrodskyF MFM | lld:pubmed |
| pubmed-article:2904698 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2904698 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:2904698 | pubmed:volume | 242 | lld:pubmed |
| pubmed-article:2904698 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2904698 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2904698 | pubmed:pagination | 1396-402 | lld:pubmed |
| pubmed-article:2904698 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2904698 | pubmed:meshHeading | pubmed-meshheading:2904698-... | lld:pubmed |
| pubmed-article:2904698 | pubmed:meshHeading | pubmed-meshheading:2904698-... | lld:pubmed |
| pubmed-article:2904698 | pubmed:meshHeading | pubmed-meshheading:2904698-... | lld:pubmed |
| pubmed-article:2904698 | pubmed:meshHeading | pubmed-meshheading:2904698-... | lld:pubmed |
| pubmed-article:2904698 | pubmed:meshHeading | pubmed-meshheading:2904698-... | lld:pubmed |
| pubmed-article:2904698 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2904698 | pubmed:articleTitle | Living with clathrin: its role in intracellular membrane traffic. | lld:pubmed |
| pubmed-article:2904698 | pubmed:affiliation | Department of Pharmacy, School of Pharmacy, University of California, San Francisco 94143. | lld:pubmed |
| pubmed-article:2904698 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2904698 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2904698 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2904698 | pubmed:publicationType | Review | lld:pubmed |
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