The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Fluoroaluminates activate transducin‐GDP by mimicking the γ‐phosphate of GTP in its binding site
Open accessAbstract
Fluoride activation of the cGMP cascade of vision requires the presence of aluminum, and is shown to be mediated by the binding of one AlF‐4 to the GDP/GTP‐binding subunit of transducin. The presence of GDP in the site is required: AlF 4 − is ineffective when the site is empty or when GDPßS is substituted for GDP. This sensitivity to the sulfur of GDPßS suggests that AlF 4 − is in contact with the GDP. Striking structural similarities between AlF 4 − and PO 4 −1 lead us to propose that AlF 4 − mimics the role of the γ‐phosphate of GTP.
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Cites
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The structural chemistry of phosphorus
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Trigger and Amplification Mechanisms in Visual Phototransduction
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Fluoride stimulation of adenylate cyclase is dependent on the guanine nucleotide regulatory protein.
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Cited by
Flow-mediated endothelial mechanotransduction
Davies, P. F. (1995) · Physiological Reviews · doi:10.1152/physrev.1995.75.3.519 · Cited by 2,802
Evidence for a Regulated Interaction between Heterotrimeric G Proteins and Caveolin
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Molecular mechanism of visual transduction
CHABRE, M., & DETERRE, P. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14549.x · Cited by 310
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Metadata
- Authors
- Bigay, J., Deterre, P., Pfister, C., & Chabre, M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1985-10-28
- Volume
- 191
- Issue
- 2
- Pages
- 181-185
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2107465400
- Cited by
- 417
- References
- 14
- FWCI
- 9.77
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Bigay, J., Deterre, P., Pfister, C., & Chabre, M. (1985). Fluoroaluminates activate transducin‐GDP by mimicking the γ‐phosphate of GTP in its binding site. FEBS Letters. https://doi.org/10.1016/0014-5793(85)80004-1
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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.