@incollection{LohseKlotzSchwabeetal.1988,
  author    = {Lohse, M. J. and Klotz, K.-N. and Schwabe, U. and Christalli, G. and Vittori, S. and Grifantini, M.},
  title     = {Pharmacology and Biochemistry of Adenosine Receptors},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86251},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1988},
  abstract  = {Adenosine modulates a variety of physiological functions via membrane-bound receptors. These receptors couple via G proteins to adenylate cyclase and K+channels. The A1 subtype mediates an inhibition of adenylate cyclase and an opening of K+-channels, and the A2 subtype a Stimulation of adenylate cyclase. Both subtypes have been characterized by radioligand binding. This has facilitated the development of agonists and antagonists with more than 1000-fold A1 selectivity. A1-selective photoaffinity labels have been used for the biochemical characterization of A1 receptors and the study of their coupling to adenylate cyclase. Such selective ligands allow the analysis of the involvement of adenosine receptors in physiological functions. Selective interference with adenosine receptors provides new pharmacological tools and eventually new therapeutic approaches to a number of pathophysiological states.},
  subject      = {Adenosinrezeptor},
  language  = {en}
}
@incollection{KlotzKeilZimmeretal.1989,
  author    = {Klotz, Karl-Norbert and Keil, Roger and Zimmer, Franz-Josef and Schwabe, Ulrich},
  title     = {Modulation of (\SH) DPCPX binding to membrane-bound ans solubilized A1 adenosine receptors by guanine nucleotides},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86153},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1989},
  abstract  = {No abstract available},
  subject      = {Adenosinrezeptor},
  language  = {en}
}
@incollection{SpielmannArendKlotzetal.1990,
  author    = {Spielmann, W.-S. and Arend, L. J. and Klotz, Karl-Norbert and Schwabe, U.},
  title     = {Adenosine receptors and singnaling in the kidney},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86114},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1990},
  abstract  = {No abstract available.},
  subject      = {Adenosinrezeptor},
  language  = {en}
}
@incollection{LohseKlotzSchwabe1987,
  author    = {Lohse, Martin J. and Klotz, Karl-Norbert and Schwabe, Ulrich},
  title     = {Functional characterization of A1 adenoosine receptors by photoaffinity labelling},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86097},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1987},
  abstract  = {The ligand-binding subunit ofthe A1 adenosine receptor has been identified in membranes with the photoaffinity Iabel R-2-azido-N6-p-hydroxyphenylisopropyladenosine (R-AHPIA). Covalent labelling ofthe A1 receptor can also be achieved in intact cells. The dissociation of the radioiodinated label (1251-AHPIA) from isolated rat fat cells was incomplete after UV irradiation, leaving about 20°/o of irreversible specific binding. Such covalent labelling of the receptor led to a concentration-dependent reduction of cellular cyclic AMP levels. This persistent effect of covalent labeHing occurred with an IC50 value of 9 nM, as compared to an IC50 value of 0.9 nM for the direct reduction of cyclic AMP Ievels by the ligand. The difference in the IC5o values can be explained by assuming spare receptors. This hypothesis was verified in binding studies using [ 3HJPIA as a radioligand. R-AHPIA inhibited binding of [3H)PIA to intact fat cells with a K1 value of about 20 nM, which is about 20 tim es high er than the corresponding IC50 value of cyclic AMP reduction. These data show that the A1 receptor is activated according to the occupancy theory. The high sensitivity of the activation in intact ceJis is due to a large number of spare receptors.},
  subject      = {Adenosinrezeptor},
  language  = {en}
}
@incollection{LohseKlotzSchwabe1985,
  author    = {Lohse, Martin J. and Klotz, Karl-Norbert and Schwabe, Ulrich},
  title     = {Effects of barbiturates on A1 adenosine receptors of rat brain},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-70100},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1985},
  abstract  = {Barbiturates inhibit binding of radioligands to A 1(Ri) adenosine receptors of rat brain membranes. This inhibition is dose-dependent and stereospecific and occurs in the range of pharmacologically active concentrations. The displacement of radiolabelled A1antagonists by barbiturates is not modified by GTP, indicating that barbiturates might act as antagonists at this receptor. This action of barbiturates does not seem to be related to the binding of barbiturates to plasma membranes, as the latter process has different characteristics. Barbiturates also inhibit the binding of radioligands to solubilized A1receptors, and saturation and kinetic experiments suggest that this is due to a competitive antagonism. These results indicate that barbiturates interact with the recognition site of the A1adenosine receptor.},
  subject      = {Barbiturat},
  language  = {en}
}