The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Retinylidene Proteins: Structures and Functions from Archaea to Humans
Abstract
▪ Abstract Retinylidene proteins, containing seven membrane-embedded α-helices that form an internal pocket in which the chromophore retinal is bound, are ubiquitous in photoreceptor cells in eyes throughout the animal kingdom. They are also present in a diverse range of other organisms and locations, such as archaeal prokaryotes, unicellular eukaryotic microbes, the dermal tissue of frogs, the pineal glands of lizards and birds, the hypothalamus of toads, and the human brain. Their functions include light-driven ion transport and phototaxis signaling in microorganisms, and retinal isomerization and various types of photosignal transduction in higher animals. The aims of this review are to examine this group of photoactive proteins as a whole, to summarize our current understanding of structure/function relationships in the best-studied examples, and to report recent new developments.
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Cites
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
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Melanopsin: An opsin in melanophores, brain, and eye
Provencio, I., Jiang, G., De Grip, W. J., Hayes, W. P., & Rollag, M. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.340 · Cited by 975
Membrane phospholipids as an energy source in the operation of the visual cycle
Rando, R. R. (1991) · Biochemistry · doi:10.1021/bi00217a001 · Cited by 86
Cited by
Structure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications
Govorunova, E. G., Sineshchekov, O. A., Li, H., & Spudich, J. L. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-101910-144233 · Cited by 363
Self-citationXanthorhodopsin: A Proton Pump with a Light-Harvesting Carotenoid Antenna
Balashov, S. P., Imasheva, E. S., Boichenko, V. A., Antón, J., Wang, J. M., & Lanyi, J. K. (2005) · Science · doi:10.1126/science.1118046 · Cited by 344
A photoactive carotenoid protein acting as light intensity sensor
Wilson, A., Punginelli, C., Gall, A., Bonetti, C., Alexandre, M., Routaboul, J.-M., Kerfeld, C. A., van Grondelle, R., Robert, B., Kennis, J. T. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804636105 · Cited by 342
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Metadata
- Authors
- Spudich, J. L., Yang, C.-S., Jung, K.-H., & Spudich, E. N.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2000-11
- Volume
- 16
- Issue
- 1
- Pages
- 365-392
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2110415094
- Cited by
- 675
- References
- 4
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- Spudich, J. L., Yang, C.-S., Jung, K.-H., & Spudich, E. N. (2000). Retinylidene Proteins: Structures and Functions from Archaea to Humans. Annual Review of Cell and Developmental Biology. https://doi.org/10.1146/annurev.cellbio.16.1.365
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.