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- aggregation classification "A1".
- aggregation creator B220914.
- aggregation creator B220915.
- aggregation creator B220916.
- aggregation creator B220917.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1865252.bibtex.
- aggregation hasFormat 1865252.csv.
- aggregation hasFormat 1865252.dc.
- aggregation hasFormat 1865252.didl.
- aggregation hasFormat 1865252.doc.
- aggregation hasFormat 1865252.json.
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- aggregation hasFormat 1865252.txt.
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- aggregation hasFormat 1865252.yaml.
- aggregation isPartOf urn:issn:1350-9047.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Metacaspases".
- aggregation abstract "Metacaspases are cysteine-dependent proteases found in protozoa, fungi and plants and are distantly related to metazoan caspases. Although metacaspases share structural properties with those of caspases, they lack Asp specificity and cleave their targets after Arg or Lys residues. Studies performed over the past 10 years have demonstrated that metacaspases are multifunctional proteases essential for normal physiology of non-metazoan organisms. This article provides a comprehensive overview of the metacaspase function and molecular regulation during programmed cell death, stress and cell proliferation, as well as an analysis of the first metacaspase-mediated proteolytic pathway. To prevent further misapplication of caspase-specific molecular probes for measuring and inhibiting metacaspase activity, we provide a list of probes suitable for metacaspases.".
- aggregation authorList BK484816.
- aggregation endPage "1288".
- aggregation issue "8".
- aggregation startPage "1279".
- aggregation volume "18".
- aggregation aggregates 3148984.
- aggregation isDescribedBy 1865252.
- aggregation similarTo cdd.2011.66.
- aggregation similarTo LU-1865252.