[1]
|
Blasie, J.K. and Worthington, C.R. (1969) Molecular localization of frog retinal receptor photopigment by electron microscopy and low-angle X-ray diffraction. Journal of Molecular Biology, 39, 407-416.
doi:10.1016/0022-2836(69)90135-1
|
[2]
|
Chabre, M. (1975) X-ray diffraction studies of retinal rods. I. Structure of the disc membrane, effect of illumination. Biochimica et Biophysica Acta, 382, 322-335.
doi:10.1016/0005-2736(75)90274-6
|
[3]
|
Edrington, T.C., Bennett, M. and Albert, A.D. (2008) Calorimetric studies of bovine rod outer segment disk membranes supports a monomeric unit for both rhodopsin and opsin. Biophysical Journal, 95, 2859-2866.
doi:10.1529/biophysj.108.128868
|
[4]
|
Chabre, M., Deterre, P. and Antonny B. (2009) The apparent cooperativity of some GPCRs does not necessarily imply dimerization. Trends in Pharmacological Sciences, 30, 188-197. doi:10.1016/j.tips.2009.01.003
|
[5]
|
Fotiadis, D., Liang Y. and Filipek S., et al. (2003) Atomic force microscopy: Rhodopsin dimers in native disc membranes. Nature, 421, 127-128. doi:10.1038/421127a
|
[6]
|
Fotiadis, D., Liang, Y. and Filipek S., et al. (2003) The G protein-coupled receptor rhodopsin in the native membrane. FEBS Letters, 564, 281-288.
doi:10.1016/S0014-5793(04)00194-2
|
[7]
|
Liang, Y., Fotiadis D. and Liang Y., et al. (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. The Journal of Biological Chemistry, 278, 21655-21662.
doi:10.1074/jbc.M302536200
|
[8]
|
Filipek, S., Krzysko, K.A. and Fotiadis, D., et al. (2004) A concept for G protein activation by G protein-coupled receptor dimers: The transducin/rhodopsin interface. Photochemical & Photobiological Sciences, 3, 628-638.
doi:10.1039/b315661c
|
[9]
|
Jastrzebska, B., Fotiadis, D. and Jang, G.F., et al. (2006) Functional and structural characterization of rhodopsin oligomers. The Journal of Biological Chemistry, 281, 11917-11922. doi:10.1074/jbc.M600422200
|
[10]
|
Morris, M.B., Dastmalchi, S. and Church, W.B. (2009) Rhodopsin: Structure, signal transduction and oligomerisation. The International Journal of Biochemistry & Cell Biology, 41, 721-724. doi: 10.1016/j.biocel.2008.04.025
|
[11]
|
Gurevich, V.V. and Gurevich, E.V. (2008) How and why do GPCRs dimerize? Trends in Pharmacological Sciences, 29, 234-240. doi:10.1016/j.tips.2008.02.004
|
[12]
|
Milligan, G. (2009) G protein-coupled receptor hetero-dimerization: Contribution to pharmacology and function. British Journal of Pharmacology, 158, 5-14.
doi:10.1111/j.1476-5381.2009.00169.x
|
[13]
|
Chamber, M., Deterred, P. and Antonny, B. (2009) The apparent cooperativity of some GPCRs does not necessarily imply dimerization. Trends in Pharmacological Sciences, 30, 188-197.
|
[14]
|
Liu, Z., Zhang, J. and Zhang, A. (2009) Design of multivalent ligand targeting G-protein-coupled receptors. Current Pharmaceutical Design, 15, 682-718.
doi:10.2174/138161209787315639
|
[15]
|
Medina, R., Promo, D. and Bubis, J. (2004) The hydrodynamic properties of dark- and light-activated states of n-dodecyl-beta-D-maltoside solubilized bovine rhodopsin support the dimeric structure of both confomations. The Journal of Biological Chemistry, 279, 39565-39573.
doi:10.1074/jbc.M402446200
|
[16]
|
Shukolyukov, S.A. (2009) Aggregation of frog rhodopsin to oligomers and their dissociation to monomer: Application of BN- and SDS-PAGE. Biochemistry (Moscow), 74, 599-604. doi:10.1134/S0006297909060029
|
[17]
|
Shukolyukov, S.A. (2010) Proof of oligomeric state of frog rhodopsin: Visualization of dimer and oligomers on gels after BN- and HRCN-PAGE using Antibodies to rhodopsin and by retinylopsin fluorescence. Biochemistry (Moscow), 75, 1045-1051.
doi:10.1134/S0006297910080146
|
[18]
|
Neri, M., Vanni, S., Tavernelli, I. and Rothlisberger, U. (2010) Role of aggregation in rhodopsin signal transduction. Biochemistry, 49, 4827-4832.
doi:10.1021/bi100478j
|
[19]
|
Wittig, I., Braun, H.P. and Sch?gger, H. (2006) Blue native PAGE. Nature Protocols, 1, 418-428.
doi:10.1038/nprot.2006.62
|
[20]
|
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685. doi:10.1038/227680a0
|
[21]
|
Sch?gger, H. (2006) Tricine-SDS-PAGE. Nature Protocols, 1, 16-22. doi:10.1038/nprot.2006.4
|
[22]
|
Lowry, O.H., Rosenbrough, N.I., Farr, A.L. and Randall, R.J. (1951). Protein measurement with Folin phenol reagent. The Journal of Biological Chemistry, 193, 265-290.
|
[23]
|
Jastrzebska, B., Maeda, T. and Zhu, L., et al. (2004) Functional characterization of rhodopsin monomers and dimers in detergents. The Journal of Biological Chemistry, 279, 54663-54675. doi:10.1074/jbc.M408691200
|
[24]
|
Dutta, A., Tirupula, K.C. and Alexiev, U., et al. (2010). Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturants. Biochemistry, 49, 6317- 6328. doi:10.1021/bi100338e
|
[25]
|
Dutta, A., Kim, T.Y., Moeller, M. and Wu, J., et al. (2010) Characterization of membrane protein non-native states. 2. The SDS-unfolded states of rhodopsin. Biochemistry, 49, 6329-6340. doi:10.1021/bi100339x
|
[26]
|
Niepmann, M. and Zheng, J. (2006) Discontinuous native protein gel electrophoresis. Electrophoresis, 27, 3949-3951.
doi:10.1002/elps.200600172
|