Evidence map›Paper›PMID 40568223›Full record

ArticleACS catalysis2025

Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity.

Kelsi R Hall, Synnøve Elisa Rønnekleiv, Alfonso Gautieri, Hedda Lilleås, Rannei Skaali, Lukas Rieder, Andrea Nikoline Englund, Eirin Landsem, Tom Z Emrich-Mills, Iván Ayuso-Fernández and 3 more

Abstract read
In one paragraph

Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. 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

13 authors.

Kelsi R HallFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0001-5611-3010
Synnøve Elisa RønnekleivFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Alfonso GautieriBiomolecular Engineering Lab, Dipartimento di Elettronica, Informazione e Bioingegneria, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133 Milano, Italy.ORCID https://orcid.org/0000-0003-0492-0130
Hedda LilleåsFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Rannei SkaaliFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0009-0005-2281-1327
Lukas RiederFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0002-3632-2007
Andrea Nikoline EnglundFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0001-7123-8743
Eirin LandsemFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Tom Z Emrich-MillsFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0002-4440-626X
Iván Ayuso-FernándezFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Åsmund Kjendseth RøhrFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0002-4956-4865
Morten SørlieFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0001-7259-6710
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.ORCID https://orcid.org/0000-0002-9220-8743

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are important biotechnological tools due to their ability to activate C-H bonds in recalcitrant polysaccharides. To-date, most research has focused on LPMOs from the AA9 and AA10 families, while LPMOs from the AA11 family have not received the same attention since their classification almost a decade ago, despite their wide abundance in fungi. Previous studies have shown that

Indexed as

chitincopperenzyme catalysishole hoppingLPMOperoxygenasesubstrate specificity

Identifiers

PMID40568223
PMCPMC12186267

What OpenQuestion holds

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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.