Evidence map›Paper›PMID 29269938›Full record

ArticleNature communications2017

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis.

Han Feng, Xuehui Liu, Sheng Wang, Joy Fleming, Da-Cheng Wang, Wei Liu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 113 citations in OpenAlex.

  1. The genomic landscape of Klebsiella pneumoniae in Russia.World journal of microbiology & biotechnology · 2026
    Article
  2. Functional dynamics of water in New Delhi metallo-β-lactamase catalysis.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
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  5. Review
  6. Article
  7. Review
  8. Article
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  12. Approachable Synthetic Methodologies for Second-GenerationPharmaceuticals (Basel, Switzerland) · 2024
    Review
  13. Review
  14. Article
  15. Structural role of K224 in taniborbactam inhibition of NDM-1.Antimicrobial agents and chemotherapy · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Genetic and enzymatic characterization of two novel blaEuropean journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2023
    Article
  20. 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 at 4 institutions in 1 country.

Han FengNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Xuehui LiuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.ORCID http://orcid.org/0000-0001-8987-6145
Sheng WangKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, China.
Joy FlemingKey Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Da-Cheng WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. dcwang@ibp.ac.cn.
Wei LiuInstitute of Immunology, The Third Military Medical University, Chongqing, 400038, China. wei.liu.2005@gmail.com.
Chinese Academy of Sciences · CNArmy Medical University · CNFoshan University · CNHuazhong University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New Delhi metallo-β-lactamases (NDMs), the recent additions to metallo-β-lactamases (MBLs), pose a serious public health threat due to its highly efficient hydrolysis of β-lactam antibiotics and rapid worldwide dissemination. The MBL-hydrolyzing mechanism for carbapenems is less studied than that of penicillins and cephalosporins. Here, we report crystal structures of NDM-1 in complex with hydrolyzed imipenem and meropenem, at resolutions of 1.80-2.32 Å, together with NMR spectra monitoring meropenem hydrolysis. Three enzyme-intermediate/product derivatives, EI

Indexed as

beta-LactamasesCarbapenemsCephalosporinsCrystallizationCrystallography, X-RayEscherichia coliHydrolysisImipenemMagnetic Resonance SpectroscopyMeropenemModels, MolecularPenicillinsThienamycinsbeta-lactamase NDM-1beta-LactamasesCarbapenemsCephalosporinsImipenemMeropenemPenicillinsThienamycins

Identifiers

PMID29269938
PMCPMC5740130
OpenAlexW2775373670

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.