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@ARTICLE{Pissarek:276645,
      author       = {Pissarek, Margit},
      title        = {{P}otential {PET} {L}igands for {I}maging of {C}erebral
                      {VPAC} and {PAC} {R}eceptors: {A}re {N}on-{P}eptide {S}mall
                      {M}olecules {S}uperior to {P}eptide {C}ompounds?},
      journal      = {World Journal of Neuroscience},
      volume       = {05},
      number       = {05},
      issn         = {2162-2019},
      address      = {Irvine, CA},
      publisher    = {Scientific Research Publ.},
      reportid     = {FZJ-2015-06973},
      pages        = {364 - 384},
      year         = {2015},
      abstract     = {Pituitary adenylate cyclase activating polypeptide (PACAP)
                      and vasoactive intestinal peptide (VIP) have been known for
                      decades to mediate neuroendocrine and vasodilative actions
                      via G-protein-coupled receptors of Class B. These are
                      targets of imaging probes for positron emission tomography
                      (PET) or single photon emission tomography (SPECT) in tumor
                      diagnostics and tumor grading. However, they play only a
                      subordinate role in the development of tracers for brain
                      imaging. Difficulties in development of non-peptide ligands
                      typical for cerebral receptors of PACAP and VIP are shared
                      by all members of Class B receptor family. Essential
                      landmarks have been confirmed for understanding of
                      structural details of Class B receptor molecular signalling
                      during the last five years. High relevance in the
                      explanation of problems in ligand development for these
                      receptors is admitted to the large N-terminal ectodomain
                      markedly different from Class A receptor binding sites and
                      poorly suitable as orthosteric binding sites for the most
                      small-molecule compounds. The present study is focused on
                      the recently available receptor ligands for PAC1, VPAC1 and
                      VPAC2 receptors as well as potential small-molecule lead
                      structures suitable for use in PET or SPECT. Recently,
                      biaryl, cyanothiophene and pentanamide structures with
                      affinities in nM-range have been proposed as non-peptide
                      ligands at VPAC1 and VPAC2 receptors. However, most of these
                      ligands have been classified as non-competitive related to
                      the orthosteric binding site of endogenous peptide ligands
                      of VPAC receptors. For PAC1 receptors have been identified
                      hydrazide compounds for which an inhibitory and potentially
                      competitive mechanism of receptor binding has been
                      postulated based on molecular docking studies.},
      cin          = {INM-5},
      ddc          = {610},
      cid          = {I:(DE-Juel1)INM-5-20090406},
      pnm          = {315 - Imaging and radiooncology (POF3-315)},
      pid          = {G:(DE-HGF)POF3-315},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.4236/wjns.2015.55036},
      url          = {https://juser.fz-juelich.de/record/276645},
}