Evidence map›Paper›PMID 21822294›Full record

ReviewNature reviews. Microbiology2011

Function, structure and mechanism of bacterial photosensory LOV proteins.

Julien Herrou, Sean Crosson

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
22.1field-weighted citation impact, top 1% 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

126 citing papers in PubMed, 280 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
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  9. Photocleavable Systems for Cell Biology: Conceptual Design across Molecular Modalities.Chembiochem : a European journal of chemical biology · 2025
    Review
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  11. Article
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  16. Review
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66 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

2 authors at 1 institution in 1 country.

Julien HerrouDepartment of Biochemistry and Molecular Biology, The University of Chicago, Illinois 60637, USA.
Sean Crosson
University of Chicago · US

Funding

Intergrated control of Caulobacter cell physiology by visible light and stressR01GM087353 · NIGMS · UNIVERSITY OF CHICAGO · PI CROSSON, SEAN · 2009 to 2018
$2.8M
NIGMS NIH HHS R01 GM087353
6 · The paper itself

Abstract

LOV (light, oxygen or voltage) domains are protein photosensors that are conserved in bacteria, archaea, plants and fungi, and detect blue light via a flavin cofactor. LOV domains are present in both chemotrophic and phototrophic bacterial species, in which they are found amino-terminally of signalling and regulatory domains such as sensor histidine kinases, diguanylate cyclases-phosphodiesterases, DNA-binding domains and regulators of RNA polymerase σ-factors. In this Review, we describe the current state of knowledge about the function of bacterial LOV proteins, the structural basis of LOV domain-mediated signal transduction, and the use of LOV domains as genetically encoded photoswitches in synthetic biology.

Indexed as

BacteriaBacterial ProteinsPhototropismArchaeaArchaeal ProteinsCryptochromesFlavinsFlavoproteinsFungal ProteinsFungiLightPhototropinsPlant ProteinsPlantsSignal TransductionSynthetic BiologyArchaeal ProteinsBacterial ProteinsCryptochromesFlavinsFlavoproteinsFungal ProteinsPhototropinsPlant Proteins

Identifiers

PMID21822294
PMCPMC3286519
OpenAlexW1985256248

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.