Evidence map›Paper›PMID 27649488›Full record

ArticlePloS one2016

Streptococcus pneumoniae TIGR4 Flavodoxin: Structural and Biophysical Characterization of a Novel Drug Target.

Ángela Rodríguez-Cárdenas, Adriana L Rojas, María Conde-Giménez, Adrián Velázquez-Campoy, Ramón Hurtado-Guerrero, Javier Sancho

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Flavodoxins as Novel Therapeutic Targets againstInternational journal of molecular sciences · 2020
    Review
  6. Frontiers in genetics · 2020
    Article
  7. Article
  8. 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

6 authors at 4 institutions in 1 country.

Ángela Rodríguez-CárdenasDepartment of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Zaragoza, Spain.
Adriana L RojasStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, Derio, Spain.
María Conde-GiménezDepartment of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Zaragoza, Spain.
Adrián Velázquez-CampoyInstitute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, Joint Unit IQFR-CSIC-BIFI, Joint Unit EEAD-CSIC-BIFI, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D, Zaragoza, Spain.
Ramón Hurtado-GuerreroInstitute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, Joint Unit IQFR-CSIC-BIFI, Joint Unit EEAD-CSIC-BIFI, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D, Zaragoza, Spain.
Javier SanchoDepartment of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Zaragoza, Spain.
Instituto de Investigación Sanitaria Aragón · ESUniversidad de Zaragoza · ESCIC bioGUNE · ESEstación Experimental de Aula Dei · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pneumoniae (Sp) strain TIGR4 is a virulent, encapsulated serotype that causes bacteremia, otitis media, meningitis and pneumonia. Increased bacterial resistance and limited efficacy of the available vaccine to some serotypes complicate the treatment of diseases associated to this microorganism. Flavodoxins are bacterial proteins involved in several important metabolic pathways. The Sp flavodoxin (Spfld) gene was recently reported to be essential for the establishment of meningitis in a rat model, which makes SpFld a potential drug target. To facilitate future pharmacological studies, we have cloned and expressed SpFld in E. coli and we have performed an extensive structural and biochemical characterization of both the apo form and its active complex with the FMN cofactor. SpFld is a short-chain flavodoxin containing 146 residues. Unlike the well-characterized long-chain apoflavodoxins, the Sp apoprotein displays a simple two-state thermal unfolding equilibrium and binds FMN with moderate affinity. The X-ray structures of the apo and holo forms of SpFld differ at the FMN binding site, where substantial rearrangement of residues at the 91-100 loop occurs to permit cofactor binding. This work will set up the basis for future studies aiming at discovering new potential drugs to treat S. pneumoniae diseases through the inhibition of SpFld.

Indexed as

ApoproteinsCloning, MolecularCrystallography, X-RayFlavin MononucleotideFlavodoxinHumansModels, MolecularPneumococcal InfectionsProtein BindingProtein ConformationProtein StabilityProtein UnfoldingStreptococcus pneumoniaeTemperatureapoflavodoxinApoproteinsFlavin MononucleotideFlavodoxin

Identifiers

PMID27649488
PMCPMC5029806
OpenAlexW2522300318

What OpenQuestion holds

Textmetadata
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.