Matches in UGent Biblio for { <https://biblio.ugent.be/publication/4179242#aggregation> ?p ?o. }
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- aggregation classification "A1".
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- aggregation date "2013".
- aggregation format "application/pdf".
- aggregation hasFormat 4179242.bibtex.
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- aggregation isPartOf urn:issn:1040-4651.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "The Arabidopsis METACASPASE9 degradome".
- aggregation abstract "Metacaspases are distant relatives of the metazoan caspases, found in plants, fungi, and protists. However, in contrast with caspases, information about the physiological substrates of metacaspases is still scarce. By means of N-terminal combined fractional diagonal chromatography, the physiological substrates of METACASPASE9 (MC9; AT5G04200) were identified in young seedlings of Arabidopsis thaliana on the proteome-wide level, providing additional insight into MC9 cleavage specificity and revealing a previously unknown preference for acidic residues at the substrate prime site position P1'. The functionalities of the identified MC9 substrates hinted at metacaspase functions other than those related to cell death. These results allowed us to resolve the substrate specificity of MC9 in more detail and indicated that the activity of phosphoenolpyruvate carboxykinase 1 (AT4G37870), a key enzyme in gluconeogenesis, is enhanced upon MC9-dependent proteolysis.".
- aggregation authorList BK569647.
- aggregation endPage "2847".
- aggregation issue "8".
- aggregation startPage "2831".
- aggregation volume "25".
- aggregation aggregates 4179267.
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- aggregation similarTo tpc.113.115287.
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