Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1197590#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B471465.
- aggregation creator B471466.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1197590.bibtex.
- aggregation hasFormat 1197590.csv.
- aggregation hasFormat 1197590.dc.
- aggregation hasFormat 1197590.didl.
- aggregation hasFormat 1197590.doc.
- aggregation hasFormat 1197590.json.
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- aggregation hasFormat 1197590.mods.
- aggregation hasFormat 1197590.rdf.
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- aggregation hasFormat 1197590.txt.
- aggregation hasFormat 1197590.xls.
- aggregation hasFormat 1197590.yaml.
- aggregation isPartOf urn:issn:0032-0889.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Interaction of the tobacco lectin with histone proteins".
- aggregation abstract "The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells. Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant. In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells. Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins. Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was achieved with 1 M N-acetylglucosamine (GlcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc. Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.".
- aggregation authorList BK810278.
- aggregation endPage "1102".
- aggregation issue "3".
- aggregation startPage "1091".
- aggregation volume "155".
- aggregation aggregates 3145683.
- aggregation isDescribedBy 1197590.
- aggregation similarTo pp.110.170134.
- aggregation similarTo LU-1197590.