ArticleScientific reports2017
Computational reconstruction reveals a candidate magnetic biocompass to be likely irrelevant for magnetoreception.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- On the evolutionary trail of MagRs.Zoological research · 2024Article
- Mutational Study of the Tryptophan Tetrad Important for Electron Transfer in European Robin Cryptochrome 4a.ACS omega · 2023Article
- Magnetic field effects on the structure and molecular behavior of pigeon iron-sulfur protein.Protein science : a publication of the Protein Society · 2022Article
- Searching for unity in diversity of animal magnetoreception: From biology to quantum mechanics and back.Innovation (Cambridge (Mass.)) · 2022Review
- Article
- Protein-protein interaction of the putative magnetoreceptor cryptochrome 4 expressed in the avian retina.Scientific reports · 2020Article
- Prechondrogenic ATDC5 Cell Attachment and Differentiation on Graphene Foam; Modulation by Surface Functionalization with Fibronectin.ACS applied materials & interfaces · 2019Article
- Atomistic Insights into Cryptochrome Interprotein Interactions.Biophysical journal · 2018Article
- Molecular Insights into Variable Electron Transfer in Amphibian Cryptochrome.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Birds use the magnetic field of the Earth to navigate during their annual migratory travel. The possible mechanism to explain the biophysics of this compass sense involves electron transfers within the photoreceptive protein cryptochrome. The magnetoreceptive functioning of cryptochromes is supposedly facilitated through an iron rich polymer complex which couples to multiple cryptochromes. The present investigation aims to independently reconstruct this complex and describe its interaction with Drosophila melanogaster cryptochromes. The polymer complex consists of ISCA1 protein monomers with internally bound iron sulphur clusters and simultaneously binds ten cryptochromes. Through molecular dynamics we have analysed the stability of the ISCA1-cryptochrome complex and characterized the interaction at the binding sites between individual cryptochrome and ISCA1. It is found that the cryptochrome binding to the ISCA1 polymer is not uniform and that the binding affinity depends on its placement along the ISCA1 polymer. This finding supports the claim that the individual ISCA1 monomer acts as possible intracellular interaction partner of cryptochrome, but the proposed existence of an elongated ISCA1 polymer with multiple attached cryptochromes appears to be questionable.
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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 OpenQuestion graph.