Evidence map›Paper›PMID 23183431›Full record

ArticleAntimicrobial agents and chemotherapy2013

R164H and V240H replacements by site-directed mutagenesis of TEM-149 extended-spectrum β-lactamase: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants.

Mariagrazia Perilli, Giuseppe Celenza, Paola Sandra Mercuri, Moreno Galleni, Cristina Pellegrini, Bernardetta Segatore, Gianfranco Amicosante

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 61% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 2 countries.

Mariagrazia PerilliDipartimento di Scienze Cliniche Applicate e Biotecnologiche, Università degli Studi dell'Aquila, L'Aquila, Italy. perilli@univaq.it
Giuseppe Celenza
Paola Sandra Mercuri
Moreno Galleni
Cristina Pellegrini
Bernardetta Segatore
Gianfranco Amicosante
University of L'Aquila · ITUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two laboratory mutant forms, TEM-149(H240) and TEM-149(H164-H240), of the TEM-149 extended-spectrum β-lactamase enzyme were constructed by site-directed mutagenesis. TEM-149(H240) and TEM-149(H164-H240) were similar in kinetic behavior, except with respect to benzylpenicillin and ceftazidime. Molecular modeling of the two mutant enzymes demonstrated the role of histidine at position 240 in the reduction of the affinity of the enzyme for ceftazidime.

Indexed as

Amino Acid SubstitutionAnti-Bacterial Agentsbeta-LactamasesBiocatalysisCeftazidimeDrug Resistance, Multiple, BacterialEnterobacter aerogenesEscherichia coliKineticsMicrobial Sensitivity TestsMutagenesis, Site-DirectedPenicillin GSerratia marcescensAnti-Bacterial Agentsbeta-LactamasesCeftazidimePenicillin G

Identifiers

PMID23183431
PMCPMC3553744
OpenAlexW1970596914

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.