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Vision Research|November 13, 2003
Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanismsJay M Janz, David L FarrensThe Journal of Biological Chemistry|April 9, 2004
Rhodopsin activation exposes a key hydrophobic binding site for the transducin alpha-subunit C terminusJay M Janz, David L FarrensThe Journal of Biological Chemistry|October 12, 2004
Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysisJay M Janz, David L FarrensThe 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 FarrensProceedings of the National Academy of Sciences of the United States of America|October 6, 2016
Decay of an active GPCR: Conformational dynamics govern agonist rebinding and persistence of an active, yet empty, receptor stateChristopher T Schafer, Jonathan F Fay, Jay M Janz, et al.Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology|October 23, 2010
What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein bindingDavid L FarrensThe Journal of Biological Chemistry|August 14, 2013
A constitutively activating mutation alters the dynamics and energetics of a key conformational change in a ligand-free G protein-coupled receptorHisao Tsukamoto, David L FarrensBiochimica Et Biophysica Acta|November 5, 2013
Fluorescence spectroscopy of rhodopsins: insights and approachesUlrike Alexiev, David L FarrensVision Research|October 31, 2006
Arrestin can act as a regulator of rhodopsin photochemistryMartha E Sommer, David L FarrensThe Journal of Biological Chemistry|December 14, 2023
A rapid, tag-free way to purify functional GPCRsAnthony D Shumate, David L FarrensPageof 6