Evidence map›Paper›PMID 30262667›Full record

ArticleThe Journal of biological chemistry2018

Plasticity in oligomerization, operator architecture, and DNA binding in the mode of action of a bacterial B

Jesús Fernández-Zapata, Ricardo Pérez-Castaño, Juan Aranda, Francesco Colizzi, María Carmen Polanco, Modesto Orozco, S Padmanabhan, Montserrat Elías-Arnanz

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Redox driven BNature communications · 2023
    Article
  3. Coenzyme BEnvironmental microbiology · 2022
    Article
  4. Review
  5. Review
  6. Article
  7. 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

8 authors at 2 institutions in 1 country.

Jesús Fernández-ZapataFrom the Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, 28006 Madrid.
Ricardo Pérez-CastañoDepartamento de Genética y Microbiología, Área de Genética (Unidad Asociada al Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas), Facultad de Biología, Universidad de Murcia, Murcia 30100.
Juan ArandaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona; Joint BSC-IRB Research Program in Computational Biology, Baldiri Reixac 10-12, 08028 Barcelona.
Francesco ColizziInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona; Joint BSC-IRB Research Program in Computational Biology, Baldiri Reixac 10-12, 08028 Barcelona.
María Carmen PolancoDepartamento de Genética y Microbiología, Área de Genética (Unidad Asociada al Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas), Facultad de Biología, Universidad de Murcia, Murcia 30100.
Modesto OrozcoInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona; Joint BSC-IRB Research Program in Computational Biology, Baldiri Reixac 10-12, 08028 Barcelona; Department of Biochemistry and Biomedicine, University of Barcelona, 08028 Barcelona, Spain.
S PadmanabhanFrom the Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, 28006 Madrid. Electronic address: padhu@iqfr.csic.es.
Montserrat Elías-ArnanzDepartamento de Genética y Microbiología, Área de Genética (Unidad Asociada al Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas), Facultad de Biología, Universidad de Murcia, Murcia 30100. Electronic address: melias@um.es.
Consejo Superior de Investigaciones Científicas · ESInstitute for Research in Biomedicine · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Newly discovered bacterial photoreceptors called CarH sense light by using 5'-deoxyadenosylcobalamin (AdoCbl). They repress their own expression and that of genes for carotenoid synthesis by binding in the dark to operator DNA as AdoCbl-bound tetramers, whose light-induced disassembly relieves repression. High-resolution structures of

Indexed as

Amino Acid MotifsAmino Acid SequenceBacillus megateriumBacterial ProteinsBinding SitesCobamidesDNA, BacterialGene Expression Regulation, BacterialOperator Regions, GeneticPhotoreceptors, MicrobialPromoter Regions, GeneticProtein BindingProtein DomainsProtein MultimerizationRepressor ProteinsUltraviolet RaysBacterial ProteinscobamamideCobamidesDNA, BacterialPhotoreceptors, MicrobialRepressor Proteinsadenosylcobalamin (AdoCbl)Bacillus megateriumbacterial signal transductionbacterial transcriptionCarHlight sensoroxidative stressphotoreceptorphotoregulationprotein-DNA interactionSpx

Identifiers

PMID30262667
PMCPMC6240859
OpenAlexW2893511634

What OpenQuestion holds

Textmetadata
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.