Erika E. Büllesbach
Department of Biochemistry and Molecular Biology
Medical University of South Carolina
Charleston
SC 29425
USA
Name/email consistency: high
- Replacement of disulfides by amide bonds in the relaxin-like factor (RLF/INSL3) reveals a role for the A11-B10 link in transmembrane signaling. Büllesbach, E.E., Schwabe, C. Biochemistry (2012)
- Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor. Büllesbach, E.E., Hass, M.A., Jensen, M.R., Hansen, D.F., Kristensen, S.M., Schwabe, C., Led, J.J. Biochemistry (2008)
- LGR8 signal activation by the relaxin-like factor. Büllesbach, E.E., Schwabe, C. J. Biol. Chem. (2005)
- Synthetic cross-links arrest the C-terminal region of the relaxin-like factor in an active conformation. Büllesbach, E.E., Schwabe, C. Biochemistry (2004)
- The primary structure and the disulfide links of the bovine relaxin-like factor (RLF). Büllesbach, E.E., Schwabe, C. Biochemistry (2002)
- Synthesis and conformational analysis of the insulin-like 4 gene product. Büllesbach, E.E., Schwabe, C. J. Pept. Res. (2001)
- Bombyxin exhibits an insulin-like response to modification in the N-terminal region of the A chain. Büllesbach, E.E. J. Pept. Res. (1999)
