Matches in UGent Biblio for { <https://biblio.ugent.be/publication/388877#aggregation> ?p ?o. }
Showing items 1 to 46 of
46
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B416886.
- aggregation creator B416887.
- aggregation creator B416888.
- aggregation creator B416889.
- aggregation creator B416890.
- aggregation creator B416891.
- aggregation creator B416892.
- aggregation creator B416893.
- aggregation creator B416894.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2007".
- aggregation format "application/pdf".
- aggregation hasFormat 388877.bibtex.
- aggregation hasFormat 388877.csv.
- aggregation hasFormat 388877.dc.
- aggregation hasFormat 388877.didl.
- aggregation hasFormat 388877.doc.
- aggregation hasFormat 388877.json.
- aggregation hasFormat 388877.mets.
- aggregation hasFormat 388877.mods.
- aggregation hasFormat 388877.rdf.
- aggregation hasFormat 388877.ris.
- aggregation hasFormat 388877.txt.
- aggregation hasFormat 388877.xls.
- aggregation hasFormat 388877.yaml.
- aggregation isPartOf urn:issn:1535-3893.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Large-scale identification of N-terminal peptides in the halophilic archaea Halobacterium salinarum and Natronomonas pharaonis".
- aggregation abstract "Characterization of protein N-terminal peptides supports the quality assessment of data derived from genomic sequences ( e.g., the correct assignment of start codons) and hints to in vivo N-terminal modifications such as N-terminal acetylation and removal of the initiator methionine. The current work represents the first large-scale identification of N-terminal peptides from prokaryotes, of the two halophilic euryarchaeota Halobacterium salinarum and Natronomonas pharaonis. Two methods were used that specifically allow the characterization of protein N-terminal peptides: combined fractional diagonal chromatography ( COFRADIC) and strong cation exchange chromatography (SCX), both known to enrich for N-terminally blocked peptides. In addition to these specific methods, N-terminal peptide identifications were extracted from our previous genome-wide proteomic data. Combining all data, 606 N-terminal peptides from Hbt. salinarum and 328 from Nmn. pharaonis were reliably identified. These results constitute the largest available dataset holding identified and characterized protein N-termini for prokaryotes (archaea and bacteria). They allowed the validation/improvement of start codon assignments as automatic gene finders tend to misassign start codons for GC-rich genomes. In addition, the dataset allowed unravelling N-terminal protein maturation in archaea, showing that 60% of the proteins undergo methionine cleavage and that-in contrast to current knowledges-N-alpha-acetylation is common in the archaeal domain of life with 13-18% of the proteins being N alpha-acetylated. The protein sets described in this paper are available by FTP and might be used as reference sets to test the performance of new gene finders.".
- aggregation authorList BK736809.
- aggregation endPage "2204".
- aggregation issue "6".
- aggregation startPage "2195".
- aggregation volume "6".
- aggregation aggregates 2057802.
- aggregation isDescribedBy 388877.
- aggregation similarTo pr0700347.
- aggregation similarTo LU-388877.