Evidence map›Paper›PMID 32067637›Full record

ArticleeLife2020

A widely distributed metalloenzyme class enables gut microbial metabolism of host- and diet-derived catechols.

Vayu Maini Rekdal, Paola Nol Bernadino, Michael U Luescher, Sina Kiamehr, Chip Le, Jordan E Bisanz, Peter J Turnbaugh, Elizabeth N Bess, Emily P Balskus

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Food & function · 2026
    Article
  3. Article
  4. Article
  5. Distinct classes of gut bacterial molybdenum-dependent enzymes produce urolithins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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

9 authors at 3 institutions in 1 country.

Vayu Maini Rekdal *Department of Chemistry and Chemical Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-8699-8902
Paola Nol Bernadino *Department of Chemistry and Molecular Biology, University of California, Irvine, Irvine, United States.
Michael U Luescher *Department of Chemistry and Chemical Biology, Harvard University, Cambridge, United States.
Sina KiamehrDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, United States.
Chip LeDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, United States.
Jordan E BisanzDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-8649-1706
Peter J TurnbaughDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-0888-2875
Elizabeth N BessDepartment of Chemistry and Molecular Biology, University of California, Irvine, Irvine, United States.ORCID 0000-0003-0349-0423
Emily P BalskusDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, United States.ORCID 0000-0001-5985-5714
Harvard University · USUniversity of California, Irvine · USUniversity of California, San Francisco · US

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
NIGMS NIH HHS T32 GM007598NIH HHS 5T32GM007598-38
6 · The paper itself

Abstract

Catechol dehydroxylation is a central chemical transformation in the gut microbial metabolism of plant- and host-derived small molecules. However, the molecular basis for this transformation and its distribution among gut microorganisms are poorly understood. Here, we characterize a molybdenum-dependent enzyme from the human gut bacterium

Indexed as

DietGastrointestinal MicrobiomeCatecholsEnzymesHumansMetalloproteinsCatecholsEnzymesMetalloproteinsbiochemistrycatechol dehydroxylasechemical biologyEggerthella lentaGordonibacter sp.infectious diseasemicrobiologymolybdenum enzyme

Identifiers

PMID32067637
PMCPMC7028382
OpenAlexW3005884664

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.