@article{WalzZimmermannSeidl1994,
  author    = {Walz, Bernd and Zimmermann, Bernhard and Seidl, Siegfried},
  title     = {Intracellular Ca2+ concentration and latency of light-induced Ca2+ changes in photoreceptors of the honeybee drone},
  year      = {1994},
  language  = {en}
}
@article{WalzBaumannZimmermannetal.1995,
  author    = {Walz, Bernd and Baumann, Otto and Zimmermann, Bernhard and Ciriacy-Wantrup, E.v.},
  title     = {Caffeine- and ryanodine-sensitive Ca2+-induced Ca2+ release from the endo plasmatic reticulum in honeybee photoreceptors},
  year      = {1995},
  language  = {en}
}
@article{ZimmermannWalz1997,
  author    = {Zimmermann, Bernhard and Walz, Bernd},
  title     = {Serotonin-induced intercellular calcium waves in salivary glands of the blowfley Calliphora erythrocephala},
  year      = {1997},
  language  = {en}
}
@article{Zimmermann1998,
  author    = {Zimmermann, Bernhard},
  title     = {Calcium store depletion activates two distinct calcium entry pathways in secretory cells of the blowfly salivary gland},
  year      = {1998},
  language  = {en}
}
@article{ZimmermannWalz1999,
  author    = {Zimmermann, Bernhard and Walz, Bernd},
  title     = {The mechanism mediating regenerative intercellular Ca2+ waves in the blowfly salivary gland},
  year      = {1999},
  language  = {en}
}
@article{WalzUkhanovZimmermann2000,
  author    = {Walz, Bernd and Ukhanov, Kyrill and Zimmermann, Bernhard},
  title     = {Actions of neomycin on electrical light responses : Ca2+ release and intracellular Ca2+ changes in photoreceptors of the honeybee drone},
  issn      = {0340-7594},
  year      = {2000},
  language  = {en}
}
@article{Zimmermann2000,
  author    = {Zimmermann, Bernhard},
  title     = {Control of insP(3)-induced Ca2+ oscillations in permeabilized blowfly salivary gland cells : contribution of mitochondria},
  issn      = {0022-3751},
  year      = {2000},
  language  = {en}
}
@article{Zimmermann2000,
  author    = {Zimmermann, Bernhard},
  title     = {Subcellular organization of agonist-evoked Ca2+ waves in the blowfly salivary gland},
  year      = {2000},
  language  = {en}
}
@article{ZimmermannDamesWalzetal.2003,
  author    = {Zimmermann, Bernhard and Dames, Petra and Walz, Bernd and Baumann, Otto},
  title     = {Distribution and serotonin-induced activation of vacuolar-type H+-ATPase in the salivary glands of the blowfly Calliphora vicina},
  year      = {2003},
  language  = {en}
}
@article{DamesZimmermannSchmidtetal.2006,
  author    = {Dames, Petra and Zimmermann, Bernhard and Schmidt, Ruth and Rein, Julia and Voss, Martin and Schewe, Bettina and Walz, Bernd and Baumann, Otto},
  title     = {cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands},
  issn      = {0027-8424},
  doi       = {10.1073/pnas.0600011103},
  year      = {2006},
  abstract  = {Reversible assembly of the V0V1 holoenzyme from V-0 and V-1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. in the blowfly (Calliphora vicina) salivary gland, V- ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the CAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity. Fluorescence measurements of pH changes at the luminal surface of isolated glands demonstrate that CAMP, Sp-adenosine-3',5'-cyclic monophosphorothioate, or forskolin, similar to serotonin, cause V-ATPase-dependent luminal acidification. In addition, V-ATPase-dependent ATP hydrolysis increases upon treatment with these agents. Immunofluorescence microscopy and pelleting assays have demonstrated further that V, components become translocated from the cytoplasm to the apical membrane and V-ATPase holoenzymes are assembled at the apical membrane during conditions that increase intracellular cAMP. Because these actions occur without a change in cytosolic Ca2+, our findings suggest that the cAMP pathway mediates the reversible assembly and activation of V-ATPase molecules at the apical membrane upon hormonal stimulus},
  language  = {en}
}