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Current Opinion in Structural Biology|June 11, 2017
Structural mechanism of arrestin activationPatrick Scheerer, Martha E SommerMethods in Enzymology|April 11, 2015
Structure-based biophysical analysis of the interaction of rhodopsin with G protein and arrestinMartha E Sommer, Matthias Elgeti, Peter W Hildebrand, et al.Nature|April 23, 2013
Crystal structure of pre-activated arrestin p44Yong Ju Kim, Klaus Peter Hofmann, Oliver P Ernst, et al.Vision Research|October 31, 2006
Arrestin can act as a regulator of rhodopsin photochemistryMartha E Sommer, David L FarrensNature Communications|September 11, 2014
Crystal structure of a common GPCR-binding interface for G protein and arrestinMichal Szczepek, Florent Beyrière, Klaus Peter Hofmann, et al.Biochemistry|July 20, 2011
Alkylated hydroxylamine derivatives eliminate peripheral retinylidene Schiff bases but cannot enter the retinal binding pocket of light-activated rhodopsinRonny Piechnick, Martin Heck, Martha E SommerMethods in Molecular Biology (Clifton, N.J.)|February 21, 2015
Quantification of arrestin-rhodopsin binding stoichiometryCiara C M Lally, Martha E SommerPhotochemistry and Photobiology|May 14, 2017
Phytochromes from Agrobacterium fabrumTilman Lamparter, Norbert Krauß, Patrick ScheererNature Communications|August 9, 2012
Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsinMartha E Sommer, Klaus Peter Hofmann, Martin HeckThe Journal of Biological Chemistry|December 21, 2010
Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptorsMartha E Sommer, Klaus Peter Hofmann, Martin HeckPageof 15