<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Petruzziello, Filomena</dc:creator>
  <dc:creator>Fouillen, Laetitia</dc:creator>
  <dc:creator>Wadensten, Henrik</dc:creator>
  <dc:creator>Kretz, Robert</dc:creator>
  <dc:creator>Andren, Per E.</dc:creator>
  <dc:creator>Rainer, Gregor</dc:creator>
  <dc:creator>Zhang, Xiaozhe</dc:creator>
  <dc:date>2011-11-09</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Neuropeptidomics is used to characterize endogenous peptides in the brain of tree  shrews (Tupaia belangeri). Tree shrews are small animals similar to rodents in size  but close relatives of primates, and are excellent models for brain research. Currently,  tree shrews have no complete proteome information available on which direct  database search can be allowed for neuropeptide identification. To increase the  capability in the identification of neuropeptides in tree shrews, we developed an  integrated mass spectrometry (MS)-based approach that combines methods including  data-dependent, directed, and targeted liquid chromatography (LC)–Fourier transform  (FT)-tandem MS (MS/MS) analysis, database construction, de novo sequencing,  precursor protein search, and homology analysis. Using this integrated approach, we  identified 107 endogenous peptides that have sequences identical or similar to those  from other mammalian species. High accuracy MS and tandem MS information, with  BLAST analysis and chromatographic characteristics were used to confirm the  sequences of all the identified peptides. Interestingly, further sequence homology  analysis demonstrated that tree shrew peptides have a significantly higher degree of  homology to equivalent sequences in humans than those in mice or rats, consistent  with the close phylogenetic relationship between tree shrews and primates. Our  results provide the first extensive characterization of the peptidome in tree shrews,  which now permits characterization of their function in nervous and endocrine system.  As the approach developed fully used the conservative properties of neuropeptides in  evolution and the advantage of high accuracy MS, it can be portable for identification  of neuropeptides in other species for which the fully sequenced genomes or  proteomes are not available.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/302300</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/302300/files/Journal_of_proteome_research_2012.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1021/pr200709j</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Journal of Proteome Research. - 2012, vol. 11, no. 2, p. 886-896</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">neuropeptide</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">neuropeptidomics</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">high accuracy tandem MS</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">directed and targeted LC−MS/MS analysis</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Tupaia belangeri</dc:subject>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns6="xml" ns6:lang="en">Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
