Evidence map›Paper›PMID 26805042›Full record

ReviewTrends in biochemical sciences2016

The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins.

Ilaria Pettinati, Jürgen Brem, Sook Y Lee, Peter J McHugh, Christopher J Schofield

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
–field-weighted citation impact
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

64 citing papers in PubMed.

  1. Article
  2. Pilot proteomics study for identifying a pollution exposure signature in firefighters.Journal of exposure science & environmental epidemiology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. GlialProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mechanisms and Application of Gas-Based Anticancer Therapies.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

4 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

5 authors.

Ilaria PettinatiDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.
Jürgen BremDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.
Sook Y LeeWeatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK.
Peter J McHughWeatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK.
Christopher J SchofieldDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK. Electronic address: christopher.schofield@chem.ox.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council B18672Cancer Research UKMedical Research Council G1100135Medical Research Council MR/L007665/1
6 · The paper itself

Abstract

The αββα metallo β-lactamase (MBL) fold (MBLf) was first observed in bacterial enzymes that catalyze the hydrolysis of almost all β-lactam antibiotics, but is now known to be widely distributed. The MBL core protein fold is present in human enzymes with diverse biological roles, including cell detoxification pathways and enabling resistance to clinically important anticancer medicines. Human (h)MBLf enzymes can bind metals, including zinc and iron ions, and catalyze a range of chemically interesting reactions, including both redox (e.g., ETHE1) and hydrolytic processes (e.g., Glyoxalase II, SNM1 nucleases, and CPSF73). With a view to promoting basic research on MBLf enzymes and their medicinal targeting, here we summarize current knowledge of the mechanisms and roles of these important molecules.

Indexed as

ArabidopsisBacteriabeta-Lactamasesbeta-LactamsDNA Repair EnzymesExodeoxyribonucleasesGene ExpressionHumansHydrolysisHydroxyacylglutathione HydrolaseMitochondrial ProteinsMuscle ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsProtein BindingProtein Conformation, alpha-Helicalbeta-Lactamasesbeta-LactamsDCLRE1B protein, humanDNA Repair EnzymesETHE1 protein, humanExodeoxyribonucleasesHydroxyacylglutathione HydrolaseMitochondrial ProteinsMuscle ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsPNKD protein, humanThiolester HydrolasesZincDNA repairhydrogen sulphide metabolismmetallo β-lactamase fold proteinnucleaseRNA processingβ-lactam antibiotic and cancer drug resistance

Identifiers

PMID26805042
PMCPMC4819959

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Registered trials

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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.