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@ARTICLE{Koudelka:453765,
      author       = {Koudelka, Tomas and Boger, Juliane and Henkel, Alessandra
                      and Schönherr, Robert and Krantz, Stefanie and Fuchs,
                      Sabine and Rodríguez, Estefanía and Redecke, Lars and
                      Tholey, Andreas},
      title        = {{N}‐{T}erminomics for the {I}dentification of {I}n
                      {V}itro {S}ubstrates and {C}leavage {S}ite {S}pecificity of
                      the {SARS}‐{C}o{V}‐2 {M}ain {P}rotease},
      journal      = {Proteomics},
      volume       = {21},
      issn         = {1615-9861},
      address      = {Weinheim},
      publisher    = {Wiley VCH},
      reportid     = {PUBDB-2021-00156},
      pages        = {2000246},
      year         = {2021},
      abstract     = {The genome of coronaviruses, including SARS‐CoV‐2,
                      encodes for two proteases, a papain like (PL$^{pro}$)
                      protease and the so‐called main protease (M$^{pro}$), a
                      chymotrypsin‐like cysteine protease, also named
                      3CL$^{pro}$ or non‐structural protein 5 (nsp5). Mpro is
                      activated by autoproteolysis and is the main protease
                      responsible for cutting the viral polyprotein into
                      functional units. Aside from this, it is described that
                      M$^{pro}$ proteases are also capable of processing host
                      proteins, including those involved in the host innate immune
                      response. To identify substrates of the three main proteases
                      from SARS‐CoV, SARS‐CoV‐2, and hCoV‐NL63
                      coronviruses, an LC‐MS based N‐terminomics in vitro
                      analysis is performed using recombinantly expressed
                      proteases and lung epithelial and endothelial cell lysates
                      as substrate pools. For SARS‐CoV‐2 M$^{pro}$, 445
                      cleavage events from more than 300 proteins are identified,
                      while 151 and 331 M$^{pro}$ derived cleavage events are
                      identified for SARS‐CoV and hCoV‐NL63, respectively.
                      These data enable to better understand the cleavage site
                      specificity of the viral proteases and will help to identify
                      novel substrates in vivo. All data are available via
                      ProteomeXchange with identifier PXD021406.},
      cin          = {FS-PS / DOOR ; HAS-User / U Lübeck},
      ddc          = {540},
      cid          = {I:(DE-H253)FS-PS-20131107 / I:(DE-H253)HAS-User-20120731 /
                      $I:(DE-H253)U_L__beck-20211012$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33111431},
      UT           = {WOS:000589944900001},
      doi          = {10.1002/pmic.202000246},
      url          = {https://bib-pubdb1.desy.de/record/453765},
}