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https://olympias.lib.uoi.gr/jspui/handle/123456789/21898Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Salma, A. | en |
| dc.contributor.author | Tsiapos, A. | en |
| dc.contributor.author | Lazaridis, I. | en |
| dc.date.accessioned | 2015-11-24T19:18:48Z | - |
| dc.date.available | 2015-11-24T19:18:48Z | - |
| dc.identifier.issn | 1742-464X | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/21898 | - |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Antigens, Polyomavirus Transforming/metabolism/*physiology | en |
| dc.subject | COS Cells | en |
| dc.subject | Cell Line | en |
| dc.subject | Cercopithecus aethiops | en |
| dc.subject | HSC70 Heat-Shock Proteins/metabolism/*physiology | en |
| dc.subject | HSP40 Heat-Shock Proteins/*physiology | en |
| dc.subject | Immunoprecipitation | en |
| dc.subject | Mice | en |
| dc.subject | NIH 3T3 Cells | en |
| dc.subject | Protein Binding | en |
| dc.subject | Protein Folding | en |
| dc.title | The viral SV40 T antigen cooperates with dj2 to enhance hsc70 chaperone function | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1111/j.1742-4658.2007.06019.x | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/17760891 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1111/j.1742-4658.2007.06019.x/asset/j.1742-4658.2007.06019.x.pdf?v=1&t=h09fivvq&s=9698c49a750f91151a1acf85b981a2a2546a6ec5 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 2007 | - |
| heal.abstract | Simian virus 40 large T antigen is a J-domain-containing protein with multiple functions. Among its numerous activities, T antigen can bind heat shock cognate 70 (hsc70) but the biological significance of this interaction has not been fully understood. Here, we show that T antigen can act as an hsc70 co-chaperone enhancing the protein-folding ability of the hsc70 chaperone machine. We also show that T antigen exerts its function in collaboration with the mammalian homologue of DnaJ. Moreover, we show that the participation of T antigen in the hsc70 chaperone machine has cell-type-specific characteristics. | en |
| heal.journalName | FEBS J | 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 | |
|---|---|---|---|---|
| Salma-2007-The viral SV40 T ant.pdf | 250.55 kB | Adobe PDF | View/Open Request a copy |
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