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https://olympias.lib.uoi.gr/jspui/handle/123456789/20511Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Georgatos, S. D. | en |
| dc.contributor.author | Blobel, G. | en |
| dc.date.accessioned | 2015-11-24T19:08:15Z | - |
| dc.date.available | 2015-11-24T19:08:15Z | - |
| dc.identifier.issn | 0021-9525 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/20511 | - |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Binding Sites | en |
| dc.subject | Chromatography, Affinity | en |
| dc.subject | Cytoskeleton/*metabolism/*ultrastructure | en |
| dc.subject | Immunologic Techniques | en |
| dc.subject | Intermediate Filaments/*metabolism/ultrastructure | en |
| dc.subject | Lamin Type A | en |
| dc.subject | Lamin Type B | en |
| dc.subject | Lamins | en |
| dc.subject | Nephelometry and Turbidimetry | en |
| dc.subject | Nuclear Envelope/*metabolism/ultrastructure | en |
| dc.subject | Nucleoproteins/immunology/*physiology | en |
| dc.subject | Protein Binding | en |
| dc.subject | Rats | en |
| dc.subject | Turkeys | en |
| dc.subject | Vimentin/*metabolism | en |
| dc.title | Lamin B constitutes an intermediate filament attachment site at the nuclear envelope | 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/3301863 | - |
| heal.identifier.secondary | http://jcb.rupress.org/content/105/1/117.full.pdf | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1987 | - |
| heal.abstract | We found that urea extraction of turkey erythrocyte nuclear envelopes abolished their ability to bind exogenous 125I-vimentin, while, at the same time, it removed the nuclear lamins from the membranes. After purification of the lamins from such urea extracts, a specific binding between isolated vimentin and lamin B, or a lamin A + B hetero-oligomer, was detected by affinity chromatography. Similar analysis revealed that the 6.6-kD vimentin tail piece was involved in this interaction. By other approaches (quantitative immunoprecipitation, rate zonal sedimentation, turbidometric assays) a substoichiometric lamin B-vimentin binding was determined under in vitro conditions. It was also observed that anti-lamin B antibodies but not other sera (anti-lamin A, anti-ankyrin, preimmune) were able to block 70% of the binding of 125I-vimentin to native, vimentin-depleted, nuclear envelopes. These data, which were confirmed by using rat liver nuclear lamins, indicate that intermediate filaments may be anchored directly to the nuclear lamina, providing a continuous network connecting the plasma membrane skeleton with the karyoskeleton of eukaryotic cells. | 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-1987-Lamin B constitutes.pdf | 1.43 MB | Adobe PDF | View/Open |
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