ArticleThe journal of physical chemistry. B2023
Dimerization of European Robin Cryptochrome 4a.
Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Time-Resolved Native Mass Spectrometry Reveals Reversible Light-Driven Oligomerization of Arabidopsis Cryptochrome 1 and Its Antagonism by BIC1.Angewandte Chemie (International ed. in English) · 2026Article
- A Charge-Reversal Point Mutation Completely Depletes Flavin Chromophore from European Robin Cryptochrome 4a Protein.The journal of physical chemistry letters · 2026Article
- Different receptor models show differences in ligand binding strength and location: a computational drug screening for the tick-borne encephalitis virus.Molecular diversity · 2025Article
- Cryptochrome magnetoreception: Time course of photoactivation from non-equilibrium coarse-grained molecular dynamics.Computational and structural biotechnology journal · 2024Article
- RadicalPy: A Tool for Spin Dynamics Simulations.Journal of chemical theory and computation · 2024Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homo-dimer formation is important for the function of many proteins. Although dimeric forms of cryptochromes (Cry) have been found by crystallography and were recently observed in vitro for European robin Cry4a, little is known about the dimerization of avian Crys and the role it could play in the mechanism of magnetic sensing in migratory birds. Here, we present a combined experimental and computational investigation of the dimerization of robin Cry4a resulting from covalent and non-covalent interactions. Experimental studies using native mass spectrometry, mass spectrometric analysis of disulfide bonds, chemical cross-linking, and photometric measurements show that disulfide-linked dimers are routinely formed, that their formation is promoted by exposure to blue light, and that the most likely cysteines are C317 and C412. Computational modeling and molecular dynamics simulations were used to generate and assess a number of possible dimer structures. The relevance of these findings to the proposed role of Cry4a in avian magnetoreception is discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.