Evidence map›Paper›PMID 26960341›Full record

ReviewCurrent drug targets2016

Structural and Functional Aspects of Class A Carbapenemases.

Thierry Naas, Laurent Dortet, Bogdan I Iorga

Open access · bronzeAbstract readReview
In one paragraph

Review in Current drug targets, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

92 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Natural Protective Mechanisms ofPathogens (Basel, Switzerland) · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Comparative genomic study of blaScientific reports · 2025
    Article
  9. Clinical carbapenem-resistantMicrobiology spectrum · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Evolution ofJournal of Korean medical science · 2024
    Article
  17. Article
  18. Article
  19. Carbapenem-ResistantMedicina (Kaunas, Lithuania) · 2024
    Review
  20. Review

32 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

3 authors at 1 institution in 1 country.

Thierry NaasService de Bactériologie- Hygiène, Hôpital de Bicêtre, APHP, EA7361, Faculté de Médecine Paris- Sud, LabEx LERMIT, Le Kremlin-Bicêtre, France. thierry.naas@bct.aphp.fr.
Laurent Dortet
Bogdan I Iorga
Institut de Chimie des Substances Naturelles · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fight against infectious diseases is probably one of the greatest public health challenges faced by our society, especially with the emergence of carbapenem-resistant gram-negatives that are in some cases pan-drug resistant. Currently,β-lactamase-mediated resistance does not spare even the newest and most powerful β-lactams (carbapenems), whose activity is challenged by carbapenemases. The worldwide dissemination of carbapenemases in gram-negative organisms threatens to take medicine back into the pre-antibiotic era since the mortality associated with infections caused by these "superbugs" is very high, due to limited treatment options. Clinically-relevant carbapenemases belong either to metallo-β- lactamases (MBLs) of Ambler class B or to serine-β-lactamases (SBLs) of Ambler class A and D enzymes. Class A carbapenemases may be chromosomally-encoded (SME, NmcA, SFC-1, BIC-1, PenA, FPH-1, SHV-38), plasmid-encoded (KPC, GES, FRI-1) or both (IMI). The plasmid-encoded enzymes are often associated with mobile elements responsible for their mobilization. These enzymes, even though weakly related in terms of sequence identities, share structural features and a common mechanism of action. They variably hydrolyse penicillins, cephalosporins, monobactams, carbapenems, and are inhibited by clavulanate and tazobactam. Three-dimensional structures of class A carbapenemases, in the apo form or in complex with substrates/inhibitors, together with site-directed mutagenesis studies, provide essential input for identifying the structural factors and subtle conformational changes that influence the hydrolytic profile and inhibition of these enzymes. Overall, these data represent the building blocks for understanding the structure-function relationships that define the phenotypes of class A carbapenemases and can guide the design of new molecules of therapeutic interest.

Indexed as

Anti-Bacterial Agentsbeta-LactamasesChromosomes, BacterialCommunicable DiseasesCrystallography, X-RayDrug Resistance, BacterialGram-Negative BacteriaHumansHydrolysisModels, MolecularPhylogenyPlasmidsProtein ConformationStructure-Activity RelationshipAnti-Bacterial Agentsbeta-Lactamases

Identifiers

PMID26960341
PMCPMC5405625
OpenAlexW2293828825

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.