Evidence map›Paper›PMID 25229449›Full record

ReviewNature chemical biology2014

Photochemistry of flavoprotein light sensors.

Karen S Conrad, Craig C Manahan, Brian R Crane

Abstract readReview
In one paragraph

Review in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
–field-weighted citation impact
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

100 citing papers in PubMed.

  1. Article
  2. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Photooxidative molecular damage under blue light.Experimental & molecular medicine · 2026
    Review
  6. Article
  7. Hydraulic Activation of the AsLOV2 Photoreceptor.bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Elucidation of a distinct photoreduction pathway in class IIProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Protein design accelerates the development and application of optogenetic tools.Computational and structural biotechnology journal · 2025
    Review
  19. Article
  20. Article

40 more citing papers are in PubMed but not listed here.

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

3 authors.

Karen S ConradDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.ORCID 0000000330482226
Craig C ManahanDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.

Funding

CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
Structure and Function of Circadian Clock Light SensorsR01GM079679 · NIGMS · CORNELL UNIVERSITY · PI CRANE, BRIAN R · 2007 to 2016
$3.1M
Structural and Computational Studies of LOV domain proteins and CryptochromesF32GM099391 · NIGMS · CORNELL UNIVERSITY · PI CONRAD, KAREN S · 2012 to 2013
$101k
NIGMS NIH HHS F32 GM099391NIGMS NIH HHS F32-GM099391NIGMS NIH HHS R01 GM079679NIGMS NIH HHS R01-GM079679NIGMS NIH HHS T32 GM008500NIGMS NIH HHS T32-GM008500
6 · The paper itself

Abstract

Three major classes of flavin photosensors, light oxygen voltage (LOV) domains, blue light sensor using FAD (BLUF) proteins and cryptochromes (CRYs), regulate diverse biological activities in response to blue light. Recent studies of structure, spectroscopy and chemical mechanism have provided unprecedented insight into how each family operates at the molecular level. In general, the photoexcitation of the flavin cofactor leads to changes in redox and protonation states that ultimately remodel protein conformation and molecular interactions. For LOV domains, issues remain regarding early photochemical events, but common themes in conformational propagation have emerged across a diverse family of proteins. For BLUF proteins, photoinduced electron transfer reactions critical to light conversion are defined, but the subsequent rearrangement of hydrogen bonding networks key for signaling remains highly controversial. For CRYs, the relevant photocycles are actively debated, but mechanistic and functional studies are converging. Despite these challenges, our current understanding has enabled the engineering of flavoprotein photosensors for control of signaling processes within cells.

Indexed as

Models, MolecularCryptochromesElectron TransportEscherichia coli ProteinsFlavin-Adenine DinucleotideGene ExpressionHydrogen BondingLightOxidation-ReductionPhosphoric Diester HydrolasesPhotochemical ProcessesProtein EngineeringProtein Structure, SecondaryProtein Structure, TertiarybluF protein, E coliCryptochromesEscherichia coli ProteinsFlavin-Adenine DinucleotidePhosphoric Diester Hydrolases

Identifiers

PMID25229449
PMCPMC4258882

What OpenQuestion holds

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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.