SynthesisInternational journal of molecular sciences2015
Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Synthesis in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
91 citing papers in PubMed, 1 synthesis or guideline pooled it, 184 citations in OpenAlex.
- Drug-resistantClinical microbiology reviews · 2025Pooled it
- Carbapenemase Detection Methods in Clinical Microbiology: Conventional and Automated Approaches.Cureus · 2026Review
- Pre-Target Interception Defines Carbapenem Failure in Carbapenem-Resistant Enterobacterales: A Mechanistic Framework for Spatiotemporal Drug Reprogramming.Pharmaceutics · 2026Review
- Whole-genome sequencing reveals high-risk ESBL and carbapenemase-producing Enterobacterales on maternity ward surfaces in Cameroon.Scientific reports · 2026Article
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026Article
- First report of extended-spectrum beta lactamase (ESBL) and carbapenemase-producing MDR Klebsiella pneumoniae from Fuchka.PloS one · 2026Article
- Mechanisms, Significance, Detection and Emerging Therapies for Carbapenem-Resistant Enterobacterales: A Scoping Review.Journal of tropical medicine · 2026Review
- Molecular analysis of carbapenem-resistantFrontiers in cellular and infection microbiology · 2026Article
- Comparative evaluation of five β-Lactamase inhibitors in combination with β-Lactams against multidrug-resistant Mycobacterium tuberculosis in vitro.BMC infectious diseases · 2025Article
- Biochemical properties and substrate specificity of GOB-38 in Elizabethkingia anophelis.Scientific reports · 2025Article
- Enhancement ofFrontiers in microbiology · 2025Article
- Multidrug resistantCurrent research in microbial sciences · 2025Review
- Structural insights into alterations in the substrate spectrum of serine-β-lactamase OXA-10 fromEmerging microbes & infections · 2024Article
- Genotypic Characterisation of Carbapenem-Resistant Enterobacteriaceae in a Tertiary Care Hospital in South India.Cureus · 2024Article
- Current Strategy for Targeting Metallo-β-Lactamase with Metal-Ion-Binding Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- Hospital and municipal wastewater as a source of carbapenem-resistant Acinetobacter baumannii and Pseudomonas aeruginosa in the environment: a review.Environmental science and pollution research international · 2024Review
- Carbapenem-Resistant NDM and OXA-48-Antibiotics (Basel, Switzerland) · 2024Article
- Article
- Analysis of carbapenem-resistantInternational journal of molecular epidemiology and genetics · 2024Article
- The Dynamics of OXA-23 β-Lactamase fromInternational journal of molecular sciences · 2023Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbapenems (imipenem, meropenem, biapenem, ertapenem, and doripenem) are β-lactam antimicrobial agents. Because carbapenems have the broadest spectra among all β-lactams and are primarily used to treat infections by multi-resistant Gram-negative bacteria, the emergence and spread of carbapenemases became a major public health concern. Carbapenemases are the most versatile family of β-lactamases that are able to hydrolyze carbapenems and many other β-lactams. According to the dependency of divalent cations for enzyme activation, carbapenemases can be divided into metallo-carbapenemases (zinc-dependent class B) and non-metallo-carbapenemases (zinc-independent classes A, C, and D). Many studies have provided various carbapenemase structures. Here we present a comprehensive and systematic review of three-dimensional structures of carbapenemase-carbapenem complexes as well as those of carbapenemases. We update recent studies in understanding the enzymatic mechanism of each class of carbapenemase, and summarize structural insights about regions and residues that are important in acquiring the carbapenemase activity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.