Evidence map›Paper›PMID 34567832›Full record

ArticleACS catalysis2021

Kinetic Characterization of a Putatively Chitin-Active LPMO Reveals a Preference for Soluble Substrates and Absence of Monooxygenase Activity.

Lukas Rieder, Dejan Petrović, Priit Väljamäe, Vincent G H Eijsink, Morten Sørlie

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Initial characterization of an iron superoxide dismutase from Thermobifida fusca.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
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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

5 authors at 2 institutions in 2 countries.

Lukas RiederFaculty of Chemistry, Biotechnology, and Food Sciences, Norwegian University of Life Sciences (NMBU), Ås N-1432, Norway.ORCID https://orcid.org/0000-0002-3632-2007
Dejan PetrovićFaculty of Chemistry, Biotechnology, and Food Sciences, Norwegian University of Life Sciences (NMBU), Ås N-1432, Norway.
Priit VäljamäeInstitute of Molecular and Cell Biology, University of Tartu, Tartu 50090, Estonia.ORCID https://orcid.org/0000-0002-1035-9493
Vincent G H EijsinkFaculty of Chemistry, Biotechnology, and Food Sciences, Norwegian University of Life Sciences (NMBU), Ås N-1432, Norway.ORCID https://orcid.org/0000-0002-9220-8743
Morten SørlieFaculty of Chemistry, Biotechnology, and Food Sciences, Norwegian University of Life Sciences (NMBU), Ås N-1432, Norway.ORCID https://orcid.org/0000-0001-7259-6710
Norwegian University of Life Sciences · NOUniversity of Tartu · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes known as lytic polysaccharide monooxygenases (LPMOs) are recognized as important contributors to aerobic enzymatic degradation of recalcitrant polysaccharides such as chitin and cellulose. LPMOs are remarkably abundant in nature, with some fungal species possessing more than 50 LPMO genes, and the biological implications of this diversity remain enigmatic. For example, chitin-active LPMOs have been encountered in biological niches where chitin conversion does not seem to take place. We have carried out an in-depth kinetic characterization of a putatively chitin-active LPMO from

Identifiers

PMID34567832
PMCPMC8453653
OpenAlexW3198486125

What OpenQuestion holds

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Registered trials

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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.