Evidence map›Paper›PMID 41958861›Full record

ReviewChemical science2026

Ammonia monooxygenase: a work in progress.

Thomas C Arndt, Alexander L Laughlin, Kyle M Lancaster

Abstract readReview
In one paragraph

Review in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Emerging classes of copper enzymes.Current opinion in chemical biology · 2026
    Review
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

3 authors.

Thomas C ArndtDepartment of Chemistry and Chemical Biology Cornell University, Baker Laboratory 162 Sciences Drive Ithaca NY 14853 USA kml236@cornell.edu.ORCID https://orcid.org/0009-0002-0992-2418
Alexander L LaughlinDepartment of Chemistry and Chemical Biology Cornell University, Baker Laboratory 162 Sciences Drive Ithaca NY 14853 USA kml236@cornell.edu.
Kyle M LancasterDepartment of Chemistry and Chemical Biology Cornell University, Baker Laboratory 162 Sciences Drive Ithaca NY 14853 USA kml236@cornell.edu.ORCID https://orcid.org/0000-0001-7296-128X

Funding

Post-Fixation Nitrogen Cycle MetalloenzymologyR35GM124908 · NIGMS · CORNELL UNIVERSITY · PI Kyle M Lancaster · 2017 to 2026
$3.4M
NIGMS NIH HHS R35 GM124908
6 · The paper itself

Abstract

Ammonia monooxygenase (AMO) is a multimeric, multidomain integral membrane protein belonging to the copper membrane monooxygenase (CuMMO) family. It is responsible for the initiation of nitrification, the process by which certain bacteria and archaea oxidize ammonia (NH

Identifiers

PMID41958861
PMCPMC13058606

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.