Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/18256Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Georgatos, S. D. | en |
| dc.contributor.author | Weaver, D. C. | en |
| dc.contributor.author | Marchesi, V. T. | en |
| dc.date.accessioned | 2015-11-24T18:51:25Z | - |
| dc.date.available | 2015-11-24T18:51:25Z | - |
| dc.identifier.issn | 0021-9525 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18256 | - |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Ankyrins | en |
| dc.subject | Cattle | en |
| dc.subject | Chymotrypsin/metabolism | en |
| dc.subject | Cytoskeleton/drug effects/*metabolism | en |
| dc.subject | Humans | en |
| dc.subject | Macromolecular Substances | en |
| dc.subject | Membrane Proteins/pharmacology | en |
| dc.subject | Microscopy, Electron | en |
| dc.subject | Molecular Weight | en |
| dc.subject | Peptide Fragments/*metabolism | en |
| dc.subject | Thiocyanates/pharmacology | en |
| dc.subject | Vimentin/antagonists & inhibitors/*metabolism | en |
| dc.title | Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/3158665 | - |
| heal.identifier.secondary | http://jcb.rupress.org/content/100/6/1962.full.pdf | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1985 | - |
| heal.abstract | Fragments of vimentin, generated by chemical or enzymatic cleavages, were analyzed for their capacity to bind to human inverted erythrocyte membrane vesicles. Only peptides comprising the amino-terminal head domain of vimentin molecules were competent in associating with the membranes. In vitro studies also demonstrated that isolated ankyrin (the major vimentin acceptor site on the membrane) binds to an oligomeric species of vimentin and prevents the formation of characteristic 10-nm filaments. These data, taken together with the observation that the NH2-terminal end of vimentin is implicated in the polymerization process (Traub, P., and C. Vorgias, J. Cell Sci., 1983, 63:43-67), imply that intermediate filaments may contact the membrane in an end-on fashion, using the exposed head domains of their terminal subunits. | en |
| heal.journalName | J Cell Biol | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Georgatos-1985-Site specificity in.pdf | 688.97 kB | Adobe PDF | View/Open |
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