Matches in UGent Biblio for { <https://biblio.ugent.be/publication/528497#aggregation> ?p ?o. }
Showing items 1 to 46 of
46
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B444892.
- aggregation creator B444893.
- aggregation creator B444894.
- aggregation creator B444895.
- aggregation creator B444896.
- aggregation creator B444897.
- aggregation creator B444898.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2009".
- aggregation format "application/pdf".
- aggregation hasFormat 528497.bibtex.
- aggregation hasFormat 528497.csv.
- aggregation hasFormat 528497.dc.
- aggregation hasFormat 528497.didl.
- aggregation hasFormat 528497.doc.
- aggregation hasFormat 528497.json.
- aggregation hasFormat 528497.mets.
- aggregation hasFormat 528497.mods.
- aggregation hasFormat 528497.rdf.
- aggregation hasFormat 528497.ris.
- aggregation hasFormat 528497.txt.
- aggregation hasFormat 528497.xls.
- aggregation hasFormat 528497.yaml.
- aggregation isPartOf urn:issn:1615-9853.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "A bioanalytical method for the proteome wide display and analysis of protein complexes from whole plant cell lysates".
- aggregation abstract "While protein interaction studies and protein network modeling come to the forefront, the isolation and identification of protein complexes in a cellular context remains a major challenge for plant science. To this end, a nondenaturing extraction procedure was optimized for plant whole cell matrices and the combined use of gel filtration and BN-PAGE for the separation of protein complexes was studied. Hyphenation to denaturing electrophoresis and mass spectrometric analysis allows for the simultaneous identification of multiple (previously unidentified) protein interactions in single samples. The reliability and efficacy of the technique was confirmed (i) by the identification of well-studied plant protein complexes, (ii) by the presence of nonplant interologs for several of the novel complexes (iii) by presenting physical evidence of previously hypothetical plant protein interactions and (iv) by the confirmation of found interactions using co-IP. Furthermore practical issues concerning the use of this 2-D BN/SDS-PAGE display method for the analysis of protein-protein interactions are discussed.".
- aggregation authorList BK776877.
- aggregation endPage "609".
- aggregation issue "3".
- aggregation startPage "598".
- aggregation volume "9".
- aggregation aggregates 3064938.
- aggregation aggregates 3064939.
- aggregation isDescribedBy 528497.
- aggregation similarTo pmic.200800100.
- aggregation similarTo LU-528497.