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This topic has appeared in the trending rankings 1 time(s) in the past year. While it does not trend frequently, its appearance suggests a renewed or concentrated surge of public interest.
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Retinylidene_protein entered the ranking for the first time today at position #. This is its highest position ever recorded.
This topic has appeared in the English Wikipedia rankings 1 time. It first appeared on 2026-06-15 and was most recently seen on 2026-06-15.
Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin. While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, rhodopsin in the broad sense refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle.
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