Evidence map›Paper›PMID 29909397›Full record

ArticleThe Journal of biological chemistry2018

Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity.

Zishuo Cheng, Pei W Thomas, Lincheng Ju, Alexander Bergstrom, Kelly Mason, Delaney Clayton, Callie Miller, Christopher R Bethel, Jamie VanPelt, David L Tierney and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.3field-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

63 citing papers in PubMed, 100 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. In vitro activity and resistance mechanisms of novel antimicrobial agents against metallo-β-lactamase producers.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
  10. Prevalence of New Delhi Metallo-β-lactamase (blaMolecular biology reports · 2025
    Article
  11. Identification of Potential Inhibitors of Three NDM Variants ofCurrent computer-aided drug design · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Machine Learning Models Identify Inhibitors of New Delhi Metallo-β-lactamase.Journal of chemical information and modeling · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Structural role of K224 in taniborbactam inhibition of NDM-1.Antimicrobial agents and chemotherapy · 2024
    Article

3 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

14 authors at 4 institutions in 2 countries.

Zishuo ChengFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
Pei W Thomasthe Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, and the LaMontagne Center of Infectious Disease, University of Texas, Austin, Texas 78712.
Lincheng Juthe Department of Urology, Shengjing Hospital of China Medical University, Shenyang, Liaoning 110004, China.
Alexander BergstromFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
Kelly MasonFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
Delaney ClaytonFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
Callie MillerFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
Christopher R Bethelthe Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, and.
Jamie VanPeltFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056.
David L TierneyFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, dtierney@miamioh.edu.
Richard C PageFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, pagerc@miamioh.edu.ORCID 0000-0002-3006-3171
Robert A Bonomothe Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, and robert.bonomo@va.gov.
Walter Fastthe Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, and the LaMontagne Center of Infectious Disease, University of Texas, Austin, Texas 78712, walt.fast@austin.utexas.edu.
Michael W CrowderFrom the Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, crowdemw@miamioh.edu.
Miami University · USAustin College · USLouis Stokes Cleveland VA Medical Center · USChina Medical University · CN

Funding

Understanding B-Lactam Resistance in Acinetobacter baumanniiR01AI072219 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ROBERT A. BONOMO, Philip N. Rather · 2007 to 2026
$6.6M
Understanding ceftazidime resistance in SHV B-LactamasesR01AI063517 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A. · 2005 to 2023
$4.9M
A Mechanism-Based Approach to Metallo-beta-Lactamase InhibitionR01AI100560 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A., SPENCER, JAMES · 2012 to 2022
$4.4M
Developing Metallo-Beta-Lactamase InhibitorsR01GM111926 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BONOMO, ROBERT A., COHEN, SETH M · 2015 to 2019
$2.3M
The Continuing Challenge of Carbapenemases in K. pneumoniae: KPC-2 & NDM-1I01BX001974 · VA · LOUIS STOKES CLEVELAND VA MEDICAL CENTER · PI BONOMO, ROBERT A. · 2013 to 2024
–
BLRD VA I01 BX001974NIAID NIH HHS R01 AI063517NIAID NIH HHS R01 AI072219NIAID NIH HHS R01 AI100560NIGMS NIH HHS R01 GM111926
6 · The paper itself

Abstract

Infections by carbapenem-resistant Enterobacteriaceae are difficult to manage owing to broad antibiotic resistance profiles and because of the inability of clinically used β-lactamase inhibitors to counter the activity of metallo-β-lactamases often harbored by these pathogens. Of particular importance is New Delhi metallo-β-lactamase (NDM), which requires a di-nuclear zinc ion cluster for catalytic activity. Here, we compare the structures and functions of clinical NDM variants 1-17. The impact of NDM variants on structure is probed by comparing melting temperature and refolding efficiency and also by spectroscopy (UV-visible,

Indexed as

MutationAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesCrystallography, X-RayEnzyme StabilityHumansMicrobial Sensitivity TestsModels, MolecularProtein ConformationZincAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-lactamase NDM-1beta-LactamasesZincantibiotic resistanceantibioticsCo(II)-substituted enzymeenzyme kineticsenzyme mutationmetalloenzymemetallo-β-lactamaseNDM-1protein evolution

Identifiers

PMID29909397
PMCPMC6093243
OpenAlexW2808099452

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.