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

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C. Roy D. Lancaster

Max Planck Institute of Biophysics

Max-von-Laue-Str. 3

D-60438 Frankfurt

Germany

[email]@mpibp-frankfurt.mpg.de

Name/email consistency: high

 
 
 
 
 
 
 

Affiliations

  • Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt, Germany. 2007
  • Max-Planck-Institut für Biophysik, Abteilung Molekulare Membranbiologie, Heinrich-Hoffmann Str. 7, D-60528 Frankfurt am Main, Germany. 2000 - 2006
  • Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt am Main, Germany. 2005

References

  1. A comparison of stigmatellin conformations, free and bound to the photosynthetic reaction center and the cytochrome bc1 complex. Lancaster, C.R., Hunte, C., Kelley, J., Trumpower, B.L., Ditchfield, R. J. Mol. Biol. (2007) [Pubmed]
  2. Recent progress on obtaining theoretical and experimental support for the "E-pathway hypothesis" of coupled transmembrane electron and proton transfer in dihaem-containing quinol:fumarate reductase. Lancaster, C.R., Haas, A.H., Madej, M.G., Mileni, M. Biochim. Biophys. Acta (2006) [Pubmed]
  3. Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase. Lancaster, C.R., Sauer, U.S., Gross, R., Haas, A.H., Graf, J., Schwalbe, H., Mäntele, W., Simon, J., Madej, M.G. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. The role of electrostatics in proton-conducting membrane protein complexes. Lancaster, C.R. FEBS Lett. (2003) [Pubmed]
  5. Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase. Lancaster, C.R. FEBS Lett. (2003) [Pubmed]
  6. Succinate:quinone oxidoreductases from epsilon-proteobacteria. Lancaster, C.R., Simon, J. Biochim. Biophys. Acta (2002) [Pubmed]
  7. Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer. Lancaster, C.R. Biochim. Biophys. Acta (2002) [Pubmed]
  8. A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Lancaster, C.R., Gross, R., Simon, J. Eur. J. Biochem. (2001) [Pubmed]
  9. Succinate:quinone oxidoreductases--what can we learn from Wolinella succinogenes quinol:fumarate reductase?. Lancaster, C.R. FEBS Lett. (2001) [Pubmed]
  10. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution. Lancaster, C.R., Bibikova, M.V., Sabatino, P., Oesterhelt, D., Michel, H. J. Biol. Chem. (2000) [Pubmed]
 
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