Evidence map›Paper›PMID 17709463›Full record

ArticleAntimicrobial agents and chemotherapy2007

TEM-158 (CMT-9), a new member of the CMT-type extended-spectrum beta-lactamases.

Frédéric Robin, Julien Delmas, Amélie Brebion, Damien Dubois, Jean-Michel Constantin, Richard Bonnet

Abstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Characterization of the Novel CMT Enzyme TEM-154.Antimicrobial agents and chemotherapy · 2011
    Article
  4. 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.

Frédéric RobinCHU Clermont-Ferrand, Centre de Biologie, Laboratoire de bactériologiecinique, Faculté de Médecine, 28 place H. Dunant, 63001 Clermont-Ferrand, France. frobin@chu-clermontferrand.fr
Julien Delmas
Amélie Brebion
Damien Dubois
Jean-Michel Constantin
Richard Bonnet

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TEM-158 was found to include the substitutions previously observed for TEM-12 and TEM-35. This enzyme presented hydrolytic activity against ceftazidime and a high level of resistance against clavulanate, which can alter its detection. Its discovery highlights the need for accurate detection methods.

Indexed as

beta-Lactamasesbeta-Lactam Resistancebeta-LactamsCatalysisCeftazidimeClavulanic AcidEscherichia coliEscherichia coli ProteinsIsoenzymesKineticsMicrobial Sensitivity TestsMolecular Sequence DataSequence Analysis, DNAbeta-Lactamasesbeta-lactamase TEM-158, E colibeta-LactamsCeftazidimeClavulanic AcidEscherichia coli ProteinsIsoenzymes

Identifiers

PMID17709463
PMCPMC2151416

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.