Evidence map›Paper›PMID 38187819›Full record

ArticleNature catalysis2023

Product analog binding identifies the copper active site of particulate methane monooxygenase.

Frank J Tucci, Richard J Jodts, Brian M Hoffman, Amy C Rosenzweig

Open access · greenAbstract read
In one paragraph

Article in Nature catalysis, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  13. Review
  14. Structures of methane and ammonia monooxygenases in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Nanodiscs for the study of membrane proteins.Current opinion in structural biology · 2024
    Review
  19. Article
  20. Extending the Range of Distances Accessible byJournal of the American Chemical Society · 2024
    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

4 authors at 1 institution in 1 country.

Frank J TucciDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL, USA.
Richard J JodtsDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL, USA.
Brian M HoffmanDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL, USA.
Amy C RosenzweigDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL, USA.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
Metalloenzymes and metal homeostasisR35GM118035 · NIGMS · NORTHWESTERN UNIVERSITY · PI AMY C. ROSENZWEIG · 2016 to 2026
$7.1M
Coboglobins-Cobalt-Substituted Hemoglobins and MyoglobinR01GM111097 · NIGMS · NORTHWESTERN UNIVERSITY · PI HOFFMAN, BRIAN M · 2014 to 2025
$6.7M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Chemistry of Life Processes Predoctoral Training ProgramT32GM105538 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2013 to 2022
$2.7M
Investigating the role of the membrane in particulate methane monooxygenase (pMMO) structure and functionF31ES034283 · NIEHS · NORTHWESTERN UNIVERSITY · PI TUCCI, FRANK · 2022 to 2024
$122k
NCI NIH HHS P30 CA060553NIEHS NIH HHS F31 ES034283NIGMS NIH HHS R01 GM111097NIGMS NIH HHS R35 GM118035NIGMS NIH HHS T32 GM008382NIGMS NIH HHS T32 GM105538NIGMS NIH HHS U24 GM129539
6 · The paper itself

Abstract

Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu

Identifiers

PMID38187819
PMCPMC10766429
OpenAlexW4388409563

What OpenQuestion holds

Textmetadata
LicenceTDM
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.