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

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Reiner Vogel

Biophysics Section

Institute of Molecular Medicine and Cell Research

Albert-Ludwigs-Universität Freiburg

Hermann-Herder-Strasse 9

Germany

[email]@*.uni-freiburg.de

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Biophysics Section, Institute of Molecular Medicine and Cell Research, Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 9, Germany. 2002 - 2008

References

  1. Functional role of the "ionic lock"--an interhelical hydrogen-bond network in family A heptahelical receptors. Vogel, R., Mahalingam, M., Lüdeke, S., Huber, T., Siebert, F., Sakmar, T.P. J. Mol. Biol. (2008) [Pubmed]
  2. Coupling of protonation switches during rhodopsin activation. Vogel, R., Sakmar, T.P., Sheves, M., Siebert, F. Photochem. Photobiol. (2007) [Pubmed]
  3. Agonists and partial agonists of rhodopsin: retinal polyene methylation affects receptor activation. Vogel, R., Lüdeke, S., Siebert, F., Sakmar, T.P., Hirshfeld, A., Sheves, M. Biochemistry (2006) [Pubmed]
  4. Agonists and partial agonists of rhodopsin: retinals with ring modifications. Vogel, R., Siebert, F., Lüdeke, S., Hirshfeld, A., Sheves, M. Biochemistry (2005) [Pubmed]
  5. Rhodopsin photoproducts in 2D crystals. Vogel, R., Ruprecht, J., Villa, C., Mielke, T., Schertler, G.F., Siebert, F. J. Mol. Biol. (2004) [Pubmed]
  6. Formation of Meta III during the decay of activated rhodopsin proceeds via Meta I and not via Meta II. Vogel, R., Siebert, F., Zhang, X.Y., Fan, G., Sheves, M. Biochemistry (2004) [Pubmed]
  7. Photoreactions of metarhodopsin III. Vogel, R., Lüdeke, S., Radu, I., Siebert, F., Sheves, M. Biochemistry (2004) [Pubmed]
  8. Deactivation of rhodopsin in the transition from the signaling state meta II to meta III involves a thermal isomerization of the retinal chromophore C[double bond]D. Vogel, R., Siebert, F., Mathias, G., Tavan, P., Fan, G., Sheves, M. Biochemistry (2003) [Pubmed]
  9. Conformation and stability of alpha-helical membrane proteins. 1. Influence of salts on conformational equilibria between active and Inactive states of rhodopsin. Vogel, R., Siebert, F. Biochemistry (2002) [Pubmed]
  10. Conformation and stability of alpha-helical membrane proteins. 2. Influence of pH and salts on stability and unfolding of rhodopsin. Vogel, R., Siebert, F. Biochemistry (2002) [Pubmed]
  11. A nonbleachable rhodopsin analogue with a slow photocycle. Vogel, R., Fan, G.B., Ludeke, S., Siebert, F., Sheves, M. J. Biol. Chem. (2002) [Pubmed]
 
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