The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Structure and Signaling Mechanism of Per-ARNT-Sim Domains
Open accessAbstract
Summary Per-ARNT-Sim (PAS) domains serve as widely-distributed, versatile, sensor and interaction modules in signal transduction proteins. PAS sensors detect a wide range of chemical and physical stimuli and regulate the activity of functionally diverse effector domains. In contrast to this chemical, physical and functional diversity, the structure of the core of PAS domains is broadly conserved and comprises a five-stranded antiparallel β-sheet and several α-helices. Signals originate within the conserved core and generate structural and dynamic changes predominantly within the β-sheet, from which they propagate via amphipathic α-helical and coiled-coil linkers at the N- or C-termini of the core to the covalently-attached effector domain. Effector domains are typically dimeric; their activity appears to be largely regulated by signal-dependent changes in quaternary structure and dynamics. The signaling mechanisms of PAS and other signaling domains share common features, and these commonalities can be exploited to enable structure-based design of artificial photo- and chemosensors.
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Structure and function of plant photoreceptors
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Self-citationStructure and Regulation of Soluble Guanylate Cyclase
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Metadata
- Authors
- Möglich, A., Ayers, R. A., & Moffat, K.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 17
- Issue
- 10
- Pages
- 1282-1294
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2160405880
- Cited by
- 531
- References
- 74
- FWCI
- 11.76
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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