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@ARTICLE{Katsanovskaja:143329,
      author       = {K. Katsanovskaja and T. Driver and R. Pipkorn$^*$ and M.
                      Edelson-Averbukh},
      title        = {{N}egative {I}on {M}ode {C}ollision-{I}nduced
                      {D}issociation for {A}nalysis of {P}rotein {A}rginine
                      {M}ethylation.},
      journal      = {Journal of the American Society for Mass Spectrometry},
      volume       = {30},
      number       = {7},
      issn         = {1879-1123},
      address      = {New York [u.a.]},
      publisher    = {Springer},
      reportid     = {DKFZ-2019-00919},
      pages        = {1229-1241},
      year         = {2019},
      abstract     = {Arginine methylation is a common protein post-translational
                      modification (PTM) that plays a key role in eukaryotic
                      cells. Three distinct types of this modification are found
                      in mammals: asymmetric Nη1Nη1-dimethylarginine (aDMA),
                      symmetric Nη1Nη2-dimethylarginine (sDMA), and an
                      intermediate Nη1-monomethylarginine (MMA). Elucidation of
                      regulatory mechanisms of arginine methylation in living
                      organisms requires precise information on both the type of
                      the modified residues and their location inside the protein
                      amino acid sequences. Despite mass spectrometry (MS) being
                      the method of choice for analysis of multiple protein PTMs,
                      unambiguous characterization of protein arginine methylation
                      may not be always straightforward. Indeed, frequent internal
                      basic residues of Arg methylated tryptic peptides hamper
                      their sequencing under positive ion mode collision-induced
                      dissociation (CID), the standardly used tandem mass
                      spectrometry method, while the relative stability of the
                      aDMA and sDMA side chains under alternative non-ergodic
                      electron-based fragmentation techniques, electron-capture
                      and electron transfer dissociations (ECD and ETD), may
                      impede differentiation between the isobaric residues. Here,
                      for the first time, we demonstrate the potential of the
                      negative ion mode collision-induced dissociation MS for
                      analysis of protein arginine methylation and present data
                      revealing that the negative polarity approach can deliver
                      both an unambiguous identification of the arginine
                      methylation type and extensive information on the modified
                      peptide sequences.},
      cin          = {D015},
      ddc          = {530},
      cid          = {I:(DE-He78)D015-20160331},
      pnm          = {314 - Tumor immunology (POF3-314)},
      pid          = {G:(DE-HGF)POF3-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30915654},
      doi          = {10.1007/s13361-019-02176-9},
      url          = {https://inrepo02.dkfz.de/record/143329},
}