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@ARTICLE{RajaiahPrabhu:417259,
      author       = {Rajaiah Prabhu, Prince and Moorthy, Sakthi Devi and
                      Madhumathi, Jayaprakasam and Pradhan, Satya Narayan and
                      Perbandt, Markus and Betzel, Christian and Kaliraj, Perumal},
      title        = {{W}ucherria bancrofti glutathione {S}-{T}ransferase:
                      {I}nsights into the 2.3 Å resolution {X}-ray structure
                      and function, a therapeutic target for human lymphatic
                      filariasis},
      journal      = {Biochemical and biophysical research communications},
      volume       = {505},
      number       = {4},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PUBDB-2018-05492},
      pages        = {979 - 984},
      year         = {2018},
      note         = {© Elsevier Inc.},
      abstract     = {The notoriety of parasitic nematode survival is directly
                      related to chronic pathogenicity, which is evident in human
                      lymphatic filariasis. It is a disease of poverty which
                      causes severe disability affecting more than 120 million
                      people worldwide. These nematodes down-regulate host immune
                      system through a myriad of strategies that includes
                      secretion of antioxidant and detoxification enzymes like
                      glutathione-S-transferases (GSTs). Earlier studies have
                      shown Wuchereria bancrofti GST to be a potential therapeutic
                      target. Parasite GSTs catalyse the conjugation of
                      glutathione to xenobiotic and other endogenous electrophiles
                      and are essential for their long-term survival in lymph
                      tissues. Hence, the crystal structure of WbGST along with
                      its cofactor GSH at 2.3 Å resolution was determined.
                      Structural comparisons against host GST reveal distinct
                      differences in the substrate binding sites. The parasite
                      xenobiotic binding site is more substrate/solvent
                      accessible. The structure also suggests the presence of
                      putative non-catalytic binding sites that may permit
                      sequestration of endogenous and exogenous ligands. The
                      structure of WbGST also provides a case for the role of the
                      π-cation interaction in stabilizing catalytic Tyr compared
                      to stabilization interactions described for other GSTs.
                      Hence, the obtained information regarding crucial
                      differences in the active sites will support future design
                      of parasite specific inhibitors. Further, the study also
                      evaluates the inhibition of WbGST and its variants by
                      antifilarial diethylcarbamazine through kinetic assays.},
      cin          = {DOOR / UNI/CUI / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731 /
                      $I:(DE-H253)UNI_CUI-20121230$ /
                      I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000450019400004},
      pubmed       = {pmid:30297111},
      doi          = {10.1016/j.bbrc.2018.09.077},
      url          = {https://bib-pubdb1.desy.de/record/417259},
}