Evidence map›Paper›PMID 28994407›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.

Bjarte Aarmo Lund, Ane Molden Thomassen, Trine Josefine Olsen Carlsen, Hanna Kirsti S Leiros

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 40% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Conserved proline residues prevent dimerization and aggregation in the β-lactamase BlaC.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Article
  7. Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  8. Article
  9. Role of Arginine 214 in the Substrate Specificity of OXA-48.Antimicrobial agents and chemotherapy · 2020
    Article
  10. Article
  11. The Global Ascendency of OXA-48-Type Carbapenemases.Clinical microbiology reviews · 2019
    Review
  12. 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

4 authors at 2 institutions in 2 countries.

Bjarte Aarmo LundDepartment of Chemistry, UiT The Arctic University of Norway, 9037 Tromsø, Norway.
Ane Molden ThomassenDepartment of Chemistry, UiT The Arctic University of Norway, 9037 Tromsø, Norway.
Trine Josefine Olsen CarlsenDepartment of Chemistry, UiT The Arctic University of Norway, 9037 Tromsø, Norway.
Hanna Kirsti S LeirosDepartment of Chemistry, UiT The Arctic University of Norway, 9037 Tromsø, Norway.
Stanford Synchrotron Radiation Lightsource · USUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The first crystal structures of the class D β-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 Å resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 Å resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas aeruginosa and Escherichia coli. Here, enzyme kinetics and thermostability studies are presented, and the new crystal structures are used to explain the observed variations. OXA-245 had the highest melting point (T

Indexed as

Amino Acid Sequencebeta-LactamasesCalorimetry, Differential ScanningCrystallizationEscherichia coli ProteinsHumansProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryX-Ray Diffractionbeta-lactamase OXA-163, E colibeta-lactamase OXA-181, E colibeta-LactamasesEscherichia coli Proteinsantibiotic resistancecarbapenemaseenzyme kineticsOXA-163OXA-181OXA-245thermostabilityX-ray crystal structureβ-lactamase

Identifiers

PMID28994407
PMCPMC5633926
OpenAlexW2761950549

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.