Matches in UGent Biblio for { <https://biblio.ugent.be/publication/5928645#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B1032920.
- aggregation creator B1032921.
- aggregation creator B1032922.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2015".
- aggregation format "application/pdf".
- aggregation hasFormat 5928645.bibtex.
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- aggregation hasFormat 5928645.didl.
- aggregation hasFormat 5928645.doc.
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- aggregation isPartOf urn:issn:1535-9476.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini".
- aggregation abstract "Cytosolic carboxypeptidases (CCPs) constitute a new subfamily of M14 metallocarboxypeptidases associated to axonal regeneration and neuronal degeneration, among others. CCPs are deglutamylating enzymes, able to catalyze the shortening of polyglutamate side-chains and the gene-encoded C termini of tubulin, telokin, and myosin light chain kinase. The functions of these enzymes are not entirely understood, in part because of the lack of information about C-terminal protein processing in the cell and its functional implications. By means of C-terminal COFRADIC, a positional proteomics approach, we searched for cellular substrates targets of CCP1, the most relevant member of this family. We here identified seven new putative CCP1 protein substrates, including ribosomal proteins, translation factors, and high mobility group proteins. Furthermore, we showed for the first time that CCP1 processes both glutamates as well as C-terminal aspartates. The implication of these C termini in molecular interactions furthermore suggests that CCP1-mediated shortening of acidic protein tails might regulate protein-protein and protein-DNA interactions.".
- aggregation authorList BK1452233.
- aggregation endPage "190".
- aggregation issue "1".
- aggregation startPage "177".
- aggregation volume "14".
- aggregation aggregates 5928654.
- aggregation isDescribedBy 5928645.
- aggregation similarTo mcp.M114.040360.
- aggregation similarTo LU-5928645.