Retinylidene proteins: structures and functions from archaea to humans.

By J. Spudich, Chii‐Shen Yang, K. Jung, E. Spudich. Annual Review of Cell and Developmental Biology, 2000

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Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. (2001, background): “swimming away from high-energy wavelengths of solar radiation (Spudich et al. 2000), and the depth of cells in the water column is regulated by buoyant gas vesicles in response to oxygen and nutrient levels (DasSarma and Arora 1997).”
Machine learning to design integral membrane channelrhodopsins for efficient eukaryotic expression and plasma membrane localization (2017, background): “This scaffold is conserved in both microbial rhodopsins (light-driven ion pumps, channels, and light sensors–type I rhodopsins) and animal rhodopsins (light-sensing G-protein coupled receptors–type II rhodopsins) [8].”
Gene duplication and the origins of morphological complexity in pancrustacean eyes, a genomic approach (2010, background): “clades (R- and C-opsins), and their associated pathway proteins, tend to be segregated between rhabdomeric and ciliary photoreceptor cell types [27-30].”
Community structure of marine bacterioplankton: patterns, networks, and relationships to function (2008, neutral): “Rhodopsin-like pigments are 7-helix trans-membrane apoproteins (opsins), capable of binding all-trans-retinal (vitamin A aldehyde) inside the membrane-embedded helices (opsin proteins bound to retinal are called rhodopsins) (Spudich et al. 2000).”