Evidence map›Paper›PMID 35397203›Full record

ArticleStructure (London, England : 1993)2022

Mechanistic insight into light-dependent recognition of Timeless by Drosophila Cryptochrome.

Changfan Lin, Connor M Schneps, Siddarth Chandrasekaran, Abir Ganguly, Brian R Crane

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. The Timeless (Animals : an open access journal from MDPI · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  12. Article
  13. Review
  14. Review
  15. Room-temperature serial synchrotron crystallography of Drosophila cryptochrome.Acta crystallographica. Section D, Structural biology · 2022
    Article
  16. Article
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

5 authors at 2 institutions in 1 country.

Changfan LinDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Connor M SchnepsDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Siddarth ChandrasekaranDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Abir GangulyInstitute for Quantitative Biomedicine, Rutgers University, Piscataway, NJ 08854, USA.
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA. Electronic address: bc69@cornell.edu.
Cornell University · USQuantitative BioSciences · US

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
Molecular Mechanisms of Signal Transduction Involving Light, Redox and Transmembrane ComplexesR35GM122535 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE · 2017 to 2026
$7.1M
X/Q Band Pulsed ENDOR SpectrometerS10OD021543 · OD · CORNELL UNIVERSITY · PI FREED, JACK H · 2016 to 2016
$1.4M
NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R35 GM122535NIH HHS S10 OD021543
6 · The paper itself

Abstract

Cryptochrome (CRY) entrains the fly circadian clock by binding to Timeless (TIM) in light. Undocking of a helical C-terminal tail (CTT) in response to photoreduction of the CRY flavin cofactor gates TIM recognition. We present a generally applicable select western-blot-free tagged-protein interaction (SWFTI) assay that allowed the quantification of CRY binding to TIM in dark and light. The assay was used to study CRY variants with residue substitutions in the flavin pocket and correlate their TIM affinities with CTT undocking, as measured by pulse-dipolar ESR spectroscopy and evaluated by molecular dynamics simulations. CRY variants with the CTT removed or undocked bound TIM constitutively, whereas those incapable of photoreduction bound TIM weakly. In response to the flavin redox state, two conserved histidine residues contributed to a robust on/off switch by mediating CTT interactions with the flavin pocket and TIM. Our approach provides an expeditious means to quantify the interactions of difficult-to-produce proteins.

Indexed as

CryptochromesDrosophila ProteinsAnimalsDrosophilaDrosophila melanogasterEye ProteinsFlavinsLightCryptochromesDrosophila ProteinsEye ProteinsFlavinsaffinity assaycircadian clockconformational changeelectron-spin resonance spectroscopyflavoproteinphotoreceptionprotein dynamicsprotein-protein interactionswestern blot

Identifiers

PMID35397203
PMCPMC9201872
OpenAlexW4225992484

What OpenQuestion holds

Textmetadata
LicenceTDM
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.