Atomic-force microscopy: Rhodopsin dimers in native disc membranes
By D. Fotiadis, Yan Liang, Slawomir Filipek, D. Saperstein, A. Engel, Krzysztof Palczewski. Nature, 2003
780 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e7e875f9c1a1a5539a3d812ed61768b68a2c1224
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In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- Heterotrimeric G protein activation by G-protein-coupled receptors (2008, background): “Rhodopsin also appears to be arranged in paracrystalline rows of dimers in native rod outer-segment membranes as shown by atomic force microscop”
- The activation mechanism of class-C G-protein coupled receptors (2004, result): “As such, the elucidation of the activation mechanism of class-C GPCRs suggests that most, if not all GPCRs function as dimers, an idea supported by several recent studies (Bouvier, 2001; Baneres and Parello, 2003; Fotiadis et al., 2003; Liang et al., 2003).”
- Roles of G‐protein‐coupled receptor dimerization (2004, background): “EMBO reports VOL 5 | NO 1 | 2004 ©2004 EUROPEAN MOLECULAR BIOLOGY ORGANIZATION 32 atomic force microscopy to show that rhodopsin and opsin form constitutive dimers in dark-adapted native retinal membranes (Fotiadis et al, 2003; Liang et al, 2003).”
- High-resolution atomic force microscopy and spectroscopy of native membrane proteins (2011, methodology): “the eye [117], mitochondrial outer membranes hosting”