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@ARTICLE{Weng:864979,
      author       = {Weng, Samuel SH and Demir, Fatih and Ergin, Enes K. and
                      Dirnberger, Sabrina and Uzozie, Anuli and Tuscher, Domenic
                      and Nierves, Lorenz and Tsui, Janice and Huesgen, Pitter F.
                      and Lange, Philipp F.},
      title        = {{S}ensitive determination of proteolytic proteoforms in
                      limited microscale proteome samples},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {18},
      number       = {11},
      issn         = {1535-9484},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {FZJ-2019-04556},
      pages        = {2335-2347},
      year         = {2019},
      abstract     = {Protein N termini unambiguously identify truncated,
                      alternatively translated or modified proteoforms with
                      distinct functions and reveal perturbations in disease.
                      Selective enrichment of N-terminal peptides is necessary to
                      achieve proteome-wide coverage for unbiased identification
                      of site-specific regulatory proteolytic processing and
                      protease substrates. However, many proteolytic processes are
                      strictly confined in time and space and therefore can only
                      be analyzed in minute samples that provide insufficient
                      starting material for current enrichment protocols. Here we
                      present High-efficiency Undecanal-based N Termini EnRichment
                      (HUNTER), a robust, sensitive and scalable method for the
                      analysis of previously inaccessible microscale samples.
                      HUNTER achieved identification of >1000 N termini from as
                      little as 2 μg raw HeLa cell lysate. Broad applicability is
                      demonstrated by the first N-terminome analysis of sorted
                      human primary immune cells and enriched mitochondrial
                      fractions from pediatric cancer patients, as well as
                      protease substrate identification from individual
                      Arabidopsis thaliana wild type and Vacuolar Processing
                      Enzyme-deficient mutant seedlings. We further implemented
                      the workflow on a liquid handling system and demonstrate the
                      feasibility of clinical degradomics by automated processing
                      of liquid biopsies from pediatric cancer patients.},
      cin          = {ZEA-3},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {582 - Plant Science (POF3-582) / ProPlantStress -
                      Proteolytic processing in plant stress signal transduction
                      and responses to abiotic stress and pathogen attack
                      (639905)},
      pid          = {G:(DE-HGF)POF3-582 / G:(EU-Grant)639905},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31471496},
      UT           = {WOS:000494461000015},
      doi          = {10.1074/mcp.TIR119.001560},
      url          = {https://juser.fz-juelich.de/record/864979},
}