Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/18888Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Christoforidis, S. | en |
| dc.contributor.author | Zerial, M. | en |
| dc.date.accessioned | 2015-11-24T18:55:29Z | - |
| dc.date.available | 2015-11-24T18:55:29Z | - |
| dc.identifier.issn | 1046-2023 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18888 | - |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Brain Chemistry | en |
| dc.subject | Cattle | en |
| dc.subject | Chromatography, Affinity/*methods | en |
| dc.subject | Guanine Nucleotide Exchange Factors/isolation & purification | en |
| dc.subject | Ligands | en |
| dc.subject | Membrane Proteins/isolation & purification | en |
| dc.subject | Nerve Tissue Proteins/*isolation & purification | en |
| dc.subject | Protein Binding | en |
| dc.subject | *Vesicular Transport Proteins | en |
| dc.subject | rab5 GTP-Binding Proteins/*metabolism | en |
| dc.title | Purification and identification of novel Rab effectors using affinity chromatography | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1006/meth.2000.0953 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/10720461 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S1046202300909538/1-s2.0-S1046202300909538-main.pdf?_tid=003a168cb949c705f0caff06d21a6e64&acdnat=1333008960_fb909a4c291c42c72d202db26fd0819c | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 2000 | - |
| heal.abstract | Rab GTPases are central regulatory elements of the intracellular transport machinery of eukaryotic cells. To regulate vesicle docking and fusion as well as organelle dynamics Rab proteins interact with effector molecules in the GTP-bound active state. The identification of Rab effectors is, therefore, of primary importance for the mechanistic understanding of intracellular transport. Here we describe the experimental system we have developed to biochemically purify and identify effectors of the small GTPase Rab5. The method, which is based on an affinity chromatography procedure, results in the large-scale purification of Rab effectors in amounts sufficient for both their identification by microsequencing techniques and their functional characterization. In the case of Rab5, the procedure allows a comprehensive analysis of the downstream effectors and regulators of this GTPase. We expect this strategy to provide fundamental insights into the molecular mechanism of membrane transport but also to be applicable to several other GTPase-dependent biological functions. | en |
| heal.journalName | Methods | 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 | |
|---|---|---|---|---|
| Christoforidis-2000-Purification and ide.pdf | 216.19 kB | Adobe PDF | View/Open Request a copy |
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