Evidence map›Paper›PMID 32723819›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Mechanistic basis of substrate-O

Gaston Courtade, Luisa Ciano, Alessandro Paradisi, Peter J Lindley, Zarah Forsberg, Morten Sørlie, Reinhard Wimmer, Gideon J Davies, Vincent G H Eijsink, Paul H Walton and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.7field-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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Histidine oxidation in lytic polysaccharide monooxygenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  13. Review
  14. Article
  15. 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
  16. Article
  17. Chitin-Active Lytic Polysaccharide Monooxygenases Are Rare inApplied and environmental microbiology · 2022
    Article
  18. Article
  19. Article
  20. 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

11 authors at 5 institutions in 3 countries.

Gaston CourtadeNorwegian Biopolymer Laboratory (NOBIPOL), Department of Biotechnology and Food Science, Norwegian University of Science and Technology, N-7491 Trondheim, Norway.ORCID 0000-0002-1644-3223
Luisa CianoDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom.
Alessandro ParadisiDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom.
Peter J LindleyDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom.ORCID 0000-0001-9647-7177
Zarah ForsbergFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, N-1432 Ås, Norway.
Morten SørlieFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, N-1432 Ås, Norway.ORCID 0000-0001-7259-6710
Reinhard WimmerDepartment of Chemistry and Bioscience, Aalborg University, 9220 Aalborg Ø, Denmark.ORCID 0000-0001-6942-5056
Gideon J DaviesDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom.ORCID 0000-0002-7343-776X
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, N-1432 Ås, Norway.ORCID 0000-0002-9220-8743
Paul H WaltonDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom; paul.walton@york.ac.uk finn.l.aachmann@ntnu.no.ORCID 0000-0002-1152-1480
Finn L AachmannNorwegian Biopolymer Laboratory (NOBIPOL), Department of Biotechnology and Food Science, Norwegian University of Science and Technology, N-7491 Trondheim, Norway; paul.walton@york.ac.uk finn.l.aachmann@ntnu.no.ORCID 0000-0003-1613-4663
University of York · GBNorwegian University of Life Sciences · NONorwegian University of Science and Technology · NOAalborg University · DKUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L001926/1
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important enzymes, we have performed an integrated NMR/electron paramagnetic resonance (EPR) study into the detailed aspects of an AA10 LPMO-substrate interaction. Using NMR spectroscopy, we have elucidated the solution-phase structure of

Indexed as

Bacillus licheniformisBacterial ProteinsCatalytic DomainChitinCopperElectron Spin Resonance SpectroscopyMagnetic Resonance ImagingMixed Function OxygenasesOxygenSubstrate SpecificityBacterial ProteinsChitinCopperMixed Function OxygenasesOxygenchitincopperEPRlytic polysaccharide monooxygenaseNMR

Identifiers

PMID32723819
PMCPMC7431007
OpenAlexW3046034062

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.