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@ARTICLE{Yerabham:842941,
      author       = {Yerabham, Antony Sravan Kumar and Müller-Schiffmann,
                      Andreas and Ziehm, Tamar and Stadler, Andreas and Köber,
                      Sabrina and Indurkhya, Xela and Marreiros, Rita and
                      Trossbach, Svenja and Bradshaw, Nicholas and Prikulis,
                      Ingrid and Willbold, Dieter and Weiergräber, Oliver H. and
                      Korth, Carsten},
      title        = {{B}iophysical insights from a single chain camelid antibody
                      directed against the disrupted in schizophrenia 1 protein},
      journal      = {PLoS one},
      volume       = {13},
      number       = {1},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2018-01104},
      pages        = {e0191162 -},
      year         = {2018},
      abstract     = {Accumulating evidence suggests an important role for the
                      Disrupted-in-Schizophrenia 1 (DISC1) protein in
                      neurodevelopment and chronic mental illness. In particular,
                      the C-terminal 300 amino acids of DISC1 have been found to
                      mediate important protein-protein interactions and to harbor
                      functionally important phosphorylation sites and
                      disease-associated polymorphisms. However, long disordered
                      regions and oligomer-forming subdomains have so far impeded
                      structural analysis. VHH domains derived from camelid heavy
                      chain only antibodies are minimal antigen binding modules
                      with appreciable solubility and stability, which makes them
                      well suited for the stabilizing proteins prior to structural
                      investigation. Here, we report on the generation of a VHH
                      domain derived from an immunized Lama glama, displaying high
                      affinity for the human DISC1 C region (aa 691–836), and
                      its characterization by surface plasmon resonance, size
                      exclusion chromatography and immunological techniques. The
                      VHH-DISC1 (C region) complex was also used for structural
                      investigation by small angle X-ray scattering analysis. In
                      combination with molecular modeling, these data support
                      predictions regarding the three-dimensional fold of this
                      DISC1 segment as well as its steric arrangement in complex
                      with our VHH antibody.},
      cin          = {ICS-6 / Neutronenstreuung ; JCNS-1 / ICS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)ICS-1-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29324815},
      UT           = {WOS:000419952400125},
      doi          = {10.1371/journal.pone.0191162},
      url          = {https://juser.fz-juelich.de/record/842941},
}