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The Journal of Biological Chemistry|June 6, 2009
The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteinsHisao Tsukamoto, David L Farrens, Mitsumasa Koyanagi, et al.
The Journal of Biological Chemistry|January 24, 2006
Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergentMartha E Sommer, W Clay Smith, David L Farrens
The Journal of Biological Chemistry|January 28, 2003
Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2Jay M Janz, Jonathan F Fay, David L Farrens
The Journal of Biological Chemistry|December 14, 2004
Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked eventsMartha E Sommer, W Clay Smith, David L Farrens
Biochemistry|October 5, 2010
Distance mapping in proteins using fluorescence spectroscopy: the tryptophan-induced quenching (TrIQ) methodSteven E Mansoor, Mark A Dewitt, David L Farrens
Journal of Molecular Biology|April 27, 2010
Monomeric rhodopsin is the minimal functional unit required for arrestin bindingHisao Tsukamoto, Abhinav Sinha, Mark DeWitt, et al.
Biophysical Journal|April 18, 2025
Active and inactive pathways in the kinetic mechanism of the G51V retinitis pigmentosa mutant photoreactionIstvan Szundi, Weekie Yao, Eefei Chen, et al.
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