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@ARTICLE{Granzin:21147,
      author       = {Granzin, J. and Huang, Y. and Topbas, C. and Huang, W. and
                      Wu, Z. and Misra, S. and Hazen, S.L. and Blanton, R.E. and
                      Lee, X. and Weiergräber, O. H.},
      title        = {{T}hree-dimensional structure of a schistosome serpin
                      revealing an unusual configuration of the helical subdomain},
      journal      = {Acta crystallographica / D},
      volume       = {68},
      issn         = {0907-4449},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {PreJuSER-21147},
      pages        = {686 - 694},
      year         = {2012},
      note         = {JG and OHW are grateful to Georg Buldt and Dieter Willbold
                      for continuous generous support. XL and SH are supported by
                      NIH grant P01HL076491. Furthermore, excellent assistance by
                      Craig Ogata, the manager of the X4a beamline, and his staff
                      at NSLS is greatly appreciated.},
      abstract     = {Parasitic organisms are constantly challenged by the
                      defence mechanisms of their respective hosts, which often
                      depend on serine protease activities. Consequently, protease
                      inhibitors such as those belonging to the serpin superfamily
                      have emerged as protective elements that support the
                      survival of the parasites. This report describes the crystal
                      structure of ShSPI, a serpin from the trematode Schistosoma
                      haematobium. The protein is exposed on the surface of
                      invading cercaria as well as of adult worms, suggesting its
                      involvement in the parasite-host interaction. While
                      generally conforming to the well established serpin fold,
                      the structure reveals several distinctive features, mostly
                      concerning the helical subdomain of the protein. It is
                      proposed that these peculiarities are related to the unique
                      biological properties of a small serpin subfamily which is
                      conserved among pathogenic schistosomes.},
      keywords     = {Amino Acid Sequence / Animals / Humans / Models, Molecular
                      / Molecular Sequence Data / Protein Structure, Secondary /
                      Protein Structure, Tertiary / Schistosoma haematobium:
                      chemistry / Sequence Alignment / Serpins: chemistry /
                      Structural Homology, Protein / Serpins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemical Research Methods / Biochemistry $\&$ Molecular
                      Biology / Biophysics / Crystallography},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22683791},
      pmc          = {pmc:PMC3370883},
      UT           = {WOS:000305003700009},
      doi          = {10.1107/S0907444912008372},
      url          = {https://juser.fz-juelich.de/record/21147},
}