| Author |
Title |
Year |
Publication |
Serial |
Volume  |
Pages |
| Dyson, H.J.; Beattie, J.K. |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
1982 |
The Journal of Biological Chemistry |
3807 |
257 |
2267-2273 |
| Pierce, M.M.; Nall, B.T. |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
2000 |
Journal of Molecular Biology |
3853 |
298 |
955-969 |
| Hirota, S.; Suzuki, M.; Watanabe, Y. |
Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c |
2004 |
Biochemical and Biophysical Research Communications |
3777 |
314 |
452-458 |
| Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. |
Folding units govern the cytochrome c alkaline transition |
2003 |
Journal of Molecular Biology |
3781 |
331 |
37-43 |
| Hasumi, H. |
Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method |
1980 |
Biochimica et Biophysica Acta |
3876 |
626 |
265-276 |
| Saigo, S. |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
1981 |
Biochimica et Biophysica Acta |
3871 |
669 |
13-20 |
| Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. |
Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements |
1989 |
Biochimica et Biophysica Acta |
3803 |
996 |
49-56 |
