Evidence map›Paper›PMID 36828841›Full record

ArticleNature communications2023

The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.

Sahar Foroutannejad, Lydia L Good, Changfan Lin, Zachariah I Carter, Mahlet G Tadesse, Aaron L Lucius, Brian R Crane, Rodrigo A Maillard

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Sahar ForoutannejadDepartment of Chemistry, Georgetown University, Washington, DC, USA.ORCID 0000-0002-1846-4300
Lydia L GoodDepartment of Chemistry, Georgetown University, Washington, DC, USA.
Changfan LinDepartment of Chemistry & Chemical Biology, Cornell University, Ithaca, NY, USA.ORCID 0000-0002-8119-9845
Zachariah I CarterDepartment of Chemistry, University of Alabama at Birmingham, Birmingham, AL, USA.
Mahlet G TadesseDepartment of Mathematics and Statistics, Georgetown University, Washington, DC, USA.ORCID 0000-0003-2671-1663
Aaron L LuciusDepartment of Chemistry, University of Alabama at Birmingham, Birmingham, AL, USA.
Brian R CraneDepartment of Chemistry & Chemical Biology, Cornell University, Ithaca, NY, USA.ORCID 0000-0001-8234-9991
Rodrigo A MaillardDepartment of Chemistry, Georgetown University, Washington, DC, USA. rodrigo.maillard@georgetown.edu.ORCID 0000-0001-5078-6775
Georgetown University · USCornell University · USUniversity of Alabama at Birmingham · US

Funding

Molecular Mechanisms of Signal Transduction Involving Light, Redox and Transmembrane ComplexesR35GM122535 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE · 2017 to 2026
$7.1M
Hierarchical Allosteric Regulation Mechanisms in Protein KinasesR15GM135866 · NIGMS · GEORGETOWN UNIVERSITY · PI MAILLARD, RODRIGO ALEJANDRO · 2019 to 2019
$451k
NIGMS NIH HHS R15 GM135866NIGMS NIH HHS R35 GM122535
6 · The paper itself

Abstract

The link between cofactor binding and protein activity is well-established. However, how cofactor interactions modulate folding of large proteins remains unknown. We use optical tweezers, clustering and global fitting to dissect the folding mechanism of Drosophila cryptochrome (dCRY), a 542-residue protein that binds FAD, one of the most chemically and structurally complex cofactors in nature. We show that the first dCRY parts to fold are independent of FAD, but later steps are FAD-driven as the remaining polypeptide folds around the cofactor. FAD binds to largely unfolded intermediates, yet with association kinetics above the diffusion-limit. Interestingly, not all FAD moieties are required for folding: whereas the isoalloxazine ring linked to ribitol and one phosphate is sufficient to drive complete folding, the adenosine ring with phosphates only leads to partial folding. Lastly, we propose a dCRY folding model where regions that undergo conformational transitions during signal transduction are the last to fold.

Indexed as

CryptochromesDrosophilaAnimalsFlavin-Adenine DinucleotideProtein FoldingProteinsCryptochromesFlavin-Adenine DinucleotideProteins

Identifiers

PMID36828841
PMCPMC9958137
OpenAlexW4321784379

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.