Evidence map›Paper›PMID 36071795›Full record

ArticleIUCrJ2022

Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding.

Tobias Tandrup, Sebastian J Muderspach, Sanchari Banerjee, Gianluca Santoni, Johan Ø Ipsen, Cristina Hernández-Rollán, Morten H H Nørholm, Katja S Johansen, Flora Meilleur, Leila Lo Leggio

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Biomolecular NMR assignments · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Electron transfer in polysaccharide monooxygenase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  19. Structural perturbations of substrate binding and oxidation state changes in a lytic polysaccharide monooxygenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    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

10 authors at 4 institutions in 3 countries.

Tobias TandrupDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100-DK, Copenhagen, Denmark.ORCID https://orcid.org/0000-0002-3448-7019
Sebastian J MuderspachDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100-DK, Copenhagen, Denmark.ORCID https://orcid.org/0000-0002-7032-6941
Sanchari BanerjeeDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100-DK, Copenhagen, Denmark.ORCID https://orcid.org/0000-0003-2511-0604
Gianluca SantoniESRF, Structural Biology Group, 71 avenue des Martyrs, 38027 Grenoble cedex, France.ORCID https://orcid.org/0000-0001-6215-998X
Johan Ø IpsenDepartment of Geosciences and Natural Resource Management, University of Copenhagen, 1958-DK, Frederiksberg, Denmark.ORCID https://orcid.org/0000-0001-5509-8496
Cristina Hernández-RollánNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800-DK, Kgs. Lyngby, Denmark.ORCID https://orcid.org/0000-0002-4818-3630
Morten H H NørholmNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800-DK, Kgs. Lyngby, Denmark.ORCID https://orcid.org/0000-0002-7871-5191
Katja S JohansenDepartment of Geosciences and Natural Resource Management, University of Copenhagen, 1958-DK, Frederiksberg, Denmark.ORCID https://orcid.org/0000-0002-7587-5990
Flora MeilleurDepartment of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, Raleigh, NC 27695, USA.ORCID https://orcid.org/0000-0001-9313-8989
Leila Lo LeggioDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100-DK, Copenhagen, Denmark.ORCID https://orcid.org/0000-0002-5135-0882
University of Copenhagen · DKNovo Nordisk Foundation · DKEuropean Science Foundation · FROak Ridge National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal ion from Cu

Indexed as

active-site copperactive-site geometryLentinus similisLPMOlytic polysaccharide monooxygenasessaccharide bindingThermoascus aurantiacusX-ray photoreduction

Identifiers

PMID36071795
PMCPMC9438499
OpenAlexW4291982936

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.