pubmed-article:8395172 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8395172 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
pubmed-article:8395172 | lifeskim:mentions | umls-concept:C0206454 | lld:lifeskim |
pubmed-article:8395172 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8395172 | pubmed:dateCreated | 1993-9-21 | lld:pubmed |
pubmed-article:8395172 | pubmed:abstractText | Binding of a growth factor (GF) to its specific receptor on the cell surface causes the initiation of a signal transduction cascade which eventually results in mitosis. GF:receptor complexes are removed from the cell surface via receptor-mediated endocytosis, a process which involves clathrin-coated pits. After internalization into the endosomal compartment, a significant pool of GFs and GF receptors escape recycling to the cell surface and are sorted to the degradation pathway. The ligand-induced internalization and lysosomal degradation of GF receptors result in the dramatic loss of surface receptors, a phenomenon termed receptor down-regulation. In this review, we discuss relevant biochemical, morphological and kinetic studies of the mechanism of GF endocytosis, and the possible role of this process in mitogenic signaling by growth factor receptors. | lld:pubmed |
pubmed-article:8395172 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8395172 | pubmed:language | eng | lld:pubmed |
pubmed-article:8395172 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8395172 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8395172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8395172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8395172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8395172 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8395172 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8395172 | pubmed:issn | 0265-9247 | lld:pubmed |
pubmed-article:8395172 | pubmed:author | pubmed-author:WatersC MCM | lld:pubmed |
pubmed-article:8395172 | pubmed:author | pubmed-author:SorkinAA | lld:pubmed |
pubmed-article:8395172 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8395172 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:8395172 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8395172 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8395172 | pubmed:pagination | 375-82 | lld:pubmed |
pubmed-article:8395172 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:8395172 | pubmed:meshHeading | pubmed-meshheading:8395172-... | lld:pubmed |
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pubmed-article:8395172 | pubmed:meshHeading | pubmed-meshheading:8395172-... | lld:pubmed |
pubmed-article:8395172 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8395172 | pubmed:articleTitle | Endocytosis of growth factor receptors. | lld:pubmed |
pubmed-article:8395172 | pubmed:affiliation | Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146. | lld:pubmed |
pubmed-article:8395172 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8395172 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8395172 | pubmed:publicationType | Review | lld:pubmed |
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