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https://olympias.lib.uoi.gr/jspui/handle/123456789/18941Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Papamarcaki, T. | en |
| dc.contributor.author | Tsolas, O. | en |
| dc.date.accessioned | 2015-11-24T18:55:51Z | - |
| dc.date.available | 2015-11-24T18:55:51Z | - |
| dc.identifier.issn | 0014-5793 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18941 | - |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Animals | en |
| dc.subject | Cattle | en |
| dc.subject | Cell-Free System | en |
| dc.subject | Histones/*metabolism | en |
| dc.subject | Ligands | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Protein Binding | en |
| dc.subject | Protein Precursors/*metabolism | en |
| dc.subject | Subcellular Fractions/metabolism | en |
| dc.subject | Thymosin/*analogs & derivatives/metabolism | en |
| dc.subject | Thymus Gland/metabolism | en |
| dc.title | Prothymosin alpha binds to histone H1 in vitro | 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/8194604 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/0014579394004390/1-s2.0-0014579394004390-main.pdf?_tid=81ec50e683095f19c309446c94a4a27e&acdnat=1337848948_125f4dac88673716d3854eebceaf5b66 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1994 | - |
| heal.abstract | Previous studies have shown that prothymosin alpha (ProT alpha) is a nuclear acidic protein implicated in cell proliferation. To identify proteins that interact with ProT alpha we have used ligand-blotting assays. We report here that purified ProT alpha binds specifically to histone H1 in a dose dependent manner. Polyglutamic acid, an analog of the central acidic domain of ProT alpha, strongly inhibits the above interaction, suggesting that the binding of ProT alpha to histone H1 is mediated through its acidic domain. | en |
| heal.journalName | FEBS Lett | 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 | |
|---|---|---|---|---|
| Papamarcaki-1994-Prothymosin alpha bi.pdf | 1.2 MB | Adobe PDF | View/Open Request a copy |
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