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Cited by 767

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Structural Basis of a Phototropin Light Switch

Harper, Shannon M., Neil, Lori C., Gardner, Kevin H.·2003·Science

Abstract

Phototropins are light-activated kinases important for plant responses to blue light. Light initiates signaling in these proteins by generating a covalent protein–flavin mononucleotide (FMN) adduct within sensory Per-ARNT-Sim (PAS) domains. We characterized the light-dependent changes of a phototropin PAS domain by solution nuclear magnetic resonance spectroscopy and found that an α helix located outside the canonical domain plays a key role in this activation process. Although this helix associates with the PAS core in the dark, photoinduced changes in the domain structure disrupt this interaction. We propose that this mechanism couples light-dependent bond formation to kinase activation and identifies a signaling pathway conserved among PAS domains.

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Metadata

Authors
Harper, S. M., Neil, L. C., & Gardner, K. H.
Venue
Science
Published
2003-09-12
Volume
301
Issue
5639
Pages
1541-1544
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2003001669
Cited by
767
References
3
FWCI
32.50
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural Basis of a Phototropin Light Switch. https://app.cochat.ai/papers/10.1126/science.1086810
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Harper, S. M., Neil, L. C., & Gardner, K. H. (2003). Structural Basis of a Phototropin Light Switch. Science. https://doi.org/10.1126/science.1086810

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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.