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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Gerd Gäde

Zoology Department

University of Cape Town

Rondebosch

South Africa

[email]@botzoo.uct.ac.za

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Zoology Department, University of Cape Town, Rondebosch, South Africa. 1997 - 2006

References

  1. Unique translational modification of an invertebrate neuropeptide: a phosphorylated member of the adipokinetic hormone peptide family. Gäde, G., Simek, P., Clark, K.D., Auerswald, L. Biochem. J. (2006) [Pubmed]
  2. Flight fuel and neuropeptidergic control of fuel mobilisation in the twig wilter, Holopterna alata (Hemiptera, Coreidae). Gäde, G., Auerswald, L., Marco, H.G. J. Insect Physiol. (2006) [Pubmed]
  3. The adipokinetic hormones of Odonata: a phylogenetic approach. Gäde, G., Marco, H.G. J. Insect Physiol. (2005) [Pubmed]
  4. Regulation of intermediary metabolism and water balance of insects by neuropeptides. Gäde, G. Annu. Rev. Entomol. (2004) [Pubmed]
  5. Mode of action of neuropeptides from the adipokinetic hormone family. Gäde, G., Auerswald, L. Gen. Comp. Endocrinol. (2003) [Pubmed]
  6. Red pigment-concentrating hormone is not limited to crustaceans. Gäde, G., Auerswald, L., Simek, P., Marco, H.G., Kodrík, D. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  7. Insect peptide hormones: a selective review of their physiology and potential application for pest control. Gäde, G., Goldsworthy, G.J. Pest Manag. Sci. (2003) [Pubmed]
  8. Beetles' choice--proline for energy output: control by AKHs. Gäde, G., Auerswald, L. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2002) [Pubmed]
  9. Potencies of naturally-occurring AKH/RPCH peptides in Locusta migratoria in the acetate uptake assay in vitro and comparison with their potencies in the lipid mobilisation assay in vivo. Gäde, G., Lee, M.J., Goldsworthy, G.J., Kellner, R. Acta. Biol. Hung. (2000) [Pubmed]
  10. Distinct sequences of AKH/RPCH family members in beetle (Scarabaeus-species) corpus cardiacum contain three aromatic amino acid residues. Gäde, G. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
 
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