The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins.
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Activation of Transducin by Bistable Pigment Parapinopsin in the Pineal Organ of Lower VertebratesRetinal Attachment Instability Is Diversified among Mammalian Melanopsins.Distance mapping in proteins using fluorescence spectroscopy: the tryptophan-induced quenching (TrIQ) method.Real-time conformational changes in LacY.Covalent bond between ligand and receptor required for efficient activation in rhodopsin.Expression of UV-sensitive parapinopsin in the iguana parietal eyes and its implication in UV-sensitivity in vertebrate pineal-related organsConvergent transmission of RNAi guide-target mismatch information across Argonaute internal allosteric network.Chimeric proton-pumping rhodopsins containing the cytoplasmic loop of bovine rhodopsinStructural dynamics and energetics underlying allosteric inactivation of the cannabinoid receptor CB1.A key agonist-induced conformational change in the cannabinoid receptor CB1 is blocked by the allosteric ligand Org 27569.A constitutively activating mutation alters the dynamics and energetics of a key conformational change in a ligand-free G protein-coupled receptorDecay of an active GPCR: Conformational dynamics govern agonist rebinding and persistence of an active, yet empty, receptor state.Fluorescence spectroscopy of rhodopsins: insights and approaches.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein binding.A pivot between helices V and VI near the retinal-binding site is necessary for activation in rhodopsins.Chimeric microbial rhodopsins containing the third cytoplasmic loop of bovine rhodopsin.Activation induces structural changes in the liganded angiotensin II type 1 receptor.Distance mapping in proteins using fluorescence spectroscopy: tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner.Evolutionary steps involving counterion displacement in a tunicate opsin.Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish.Conformational activation of visual rhodopsin in native disc membranes
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P2860
The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 04 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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The magnitude of the light-ind ...... bility to activate G proteins.
@en
The magnitude of the light-ind ...... bility to activate G proteins.
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type
label
The magnitude of the light-ind ...... bility to activate G proteins.
@en
The magnitude of the light-ind ...... bility to activate G proteins.
@nl
prefLabel
The magnitude of the light-ind ...... bility to activate G proteins.
@en
The magnitude of the light-ind ...... bility to activate G proteins.
@nl
P2093
P2860
P356
P1476
The magnitude of the light-ind ...... bility to activate G proteins.
@en
P2093
Akihisa Terakita
David L Farrens
Hisao Tsukamoto
Mitsumasa Koyanagi
P2860
P304
20676-20683
P356
10.1074/JBC.M109.016212
P407
P577
2009-06-04T00:00:00Z