Evidence map›Paper›PMID 36504118›Full record

ReviewEssays in biochemistry2023

On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs).

Zarah Forsberg, Gaston Courtade

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

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  8. Immobilization ofACS omega · 2025
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  16. The disordered C-terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  18. Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024
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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

2 authors at 2 institutions in 1 country.

Zarah ForsbergFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, 1432 Ås, Norway.ORCID 0000-0002-8236-7986
Gaston CourtadeDepartment of Biotechnology and Food Science, NTNU-Norwegian University of Science and Technology, 7491 Trondheim, Norway.ORCID 0000-0002-1644-3223
Norwegian University of Life Sciences · NONorwegian University of Science and Technology · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) have revolutionized our understanding of how enzymes degrade insoluble polysaccharides. Compared with the substantial knowledge developed on the structure and mode of action of the catalytic LPMO domains, the (multi)modularity of LPMOs has received less attention. The presence of other domains, in particular carbohydrate-binding modules (CBMs), tethered to LPMOs has profound implications for the catalytic performance of the full-length enzymes. In the last few years, studies on LPMO modularity have led to advancements in elucidating how CBMs, other domains, and linker regions influence LPMO structure and function. This mini review summarizes recent literature, with particular focus on comparative truncation studies, to provide an overview of the diversity in LPMO modularity and the functional implications of this diversity.

Indexed as

Mixed Function OxygenasesPolysaccharidesMixed Function OxygenasesPolysaccharidescarbohydrate binding modulesenzymologylytic polysaccharide monooxygenase (LPMO)metalloenzymesprotein-carbohydrate interactions

Identifiers

PMID36504118
PMCPMC10154629
OpenAlexW4311205840

What OpenQuestion holds

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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.