Evidence map›Paper›PMID 30061284›Full record

ReviewAntimicrobial agents and chemotherapy2018

Past and Present Perspectives on β-Lactamases.

Karen Bush

Open access · bronzeAbstract readReview
In one paragraph

Review in Antimicrobial agents and chemotherapy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 410 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
410citing papers in PubMed, 3 pooled it
24.8field-weighted citation impact, top 1% 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

410 citing papers in PubMed, 3 syntheses or guidelines pooled it, 801 citations in OpenAlex.

  1. Pooled it
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  4. Trial
  5. How social is social resistance?Essays in biochemistry · 2026
    Review
  6. Disseminated multidrug-resistant Salmonella enterica serovar Dublin infection associated with plasmid-borne CMY-2 gene in a patient with travel to a farm in Mexico.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Article
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  11. Contributions of intra- and extracellular antibiotic degradation to collective [Formula: see text]-lactam survival.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. bioRxiv : the preprint server for biology · 2026
    Article
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350 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Karen BushDepartment of Biology, Indiana University Bloomington, Bloomington, Indiana, USA karbush@indiana.edu.ORCID 0000-0002-7843-2474
Indiana University Bloomington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactamases, the major resistance determinant for β-lactam antibiotics in Gram-negative bacteria, are ancient enzymes whose origins can be traced back millions of years ago. These well-studied enzymes, currently numbering almost 2,800 unique proteins, initially emerged from environmental sources, most likely to protect a producing bacterium from attack by naturally occurring β-lactams. Their ancestors were presumably penicillin-binding proteins that share sequence homology with β-lactamases possessing an active-site serine. Metallo-β-lactamases also exist, with one or two catalytically functional zinc ions. Although penicillinases in Gram-positive bacteria were reported shortly after penicillin was introduced clinically, transmissible β-lactamases that could hydrolyze recently approved cephalosporins, monobactams, and carbapenems later became important in Gram-negative pathogens. Nomenclature is based on one of two major systems. Originally, functional classifications were used, based on substrate and inhibitor profiles. A later scheme classifies β-lactamases according to amino acid sequences, resulting in class A, B, C, and D enzymes. A more recent nomenclature combines the molecular and biochemical classifications into 17 functional groups that describe most β-lactamases. Some of the most problematic enzymes in the clinical community include extended-spectrum β-lactamases (ESBLs) and the serine and metallo-carbapenemases, all of which are at least partially addressed with new β-lactamase inhibitor combinations. New enzyme variants continue to be described, partly because of the ease of obtaining sequence data from whole-genome sequencing studies. Often, these new enzymes are devoid of any phenotypic descriptions, making it more difficult for clinicians and antibiotic researchers to address new challenges that may be posed by unusual β-lactamases.

Indexed as

Bacterial Proteinsbeta-Lactamasesbeta-LactamsCephalosporinsGram-Negative BacteriaGram-Positive BacteriaPenicillinaseBacterial Proteinsbeta-Lactamasesbeta-LactamscarbapenemaseCephalosporinsPenicillinasecarbapenemasecephalosporinaseESBLMBLpenicillinaseβ-lactamβ-lactamase

Identifiers

PMID30061284
PMCPMC6153792
OpenAlexW2884524290

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.