The DOI matches its Crossref record; 269 of the 269 references it cites were found in a registry or an index.
PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light
Open accessAbstract
SUMMARY: PAS domains are newly recognized signaling domains that are widely distributed in proteins from members of the Archaea and Bacteria and from fungi, plants, insects, and vertebrates. They function as input modules in proteins that sense oxygen, redox potential, light, and some other stimuli. Specificity in sensing arises, in part, from different cofactors that may be associated with the PAS fold. Transduction of redox signals may be a common mechanistic theme in many different PAS domains. PAS proteins are always located intracellularly but may monitor the external as well as the internal environment. One way in which prokaryotic PAS proteins sense the environment is by detecting changes in the electron transport system. This serves as an early warning system for any reduction in cellular energy levels. Human PAS proteins include hypoxia-inducible factors and voltage-sensitive ion channels; other PAS proteins are integral components of circadian clocks. Although PAS domains were only recently identified, the signaling functions with which they are associated have long been recognized as fundamental properties of living cells.
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“Besides the high ductility in signal responses developed by the PAS domains (59), these show a high structural conservation of the α and β folds. This includes a five-stranded β -sheet and a long central helix (helical connector) generally linked to a bulge of three small helices.”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [59]
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Denison, M. S., & Nagy, S. R. (2003) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.135828 · Cited by 1,895
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Metadata
- Authors
- Taylor, B. L., & Zhulin, I. B.
- Affiliations
- Loma Linda University (US)
- <!--label omitted: 1-->Department of Microbiology and Molecular Genetics1 and
- ORCID
- Zhulin, Igor B.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 1999-06
- Volume
- 63
- Issue
- 2
- Pages
- 479-506
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- PMC
- PMC98974
- OpenAlex
- W2122023734
- Cited by
- 1,632
- References
- 269
- Citations by year
- 2026: 19 · 2025: 36 · 2024: 31 · 2023: 37 · 2022: 30 · 2021: 51 · 2020: 49 · 2019: 55 · 2018: 44 · 2017: 45 · 2016: 39 · 2015: 55 · 2014: 71 · 2013: 61 · 2012: 63
- FWCI
- 5.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Microbiology and Molecular Biology Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-29481, R01GM029481)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- PAS domain, oxygen sensing, redox signaling, optical sensing, signal transduction, cofactors, electron transport, hypoxia-inducible factor, voltage-gated ion channels, circadian clock
- MeSH terms
- Amino Acid Sequence, Animals, DNA-Binding Proteins, Electron Transport, Eukaryotic Cells, Humans, Light, Molecular Sequence Data, Oxidation-Reduction, Oxygen, Prokaryotic Cells, Potassium Channels, Signal Transduction, Sequence Alignment, Helix-Loop-Helix Motifs, Bacterial Physiological Phenomena
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