Evidence map›Paper›PMID 29967065›Full record

ArticleThe Journal of biological chemistry2018

The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation.

Gaston Courtade, Zarah Forsberg, Ellinor B Heggset, Vincent G H Eijsink, Finn L Aachmann

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

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  13. 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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  16. 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

5 authors.

Gaston CourtadeFrom NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Sem Sælands vei 6/8, N-7491 Trondheim, Norway.ORCID 0000-0002-1644-3223
Zarah Forsbergthe Faculty of Chemistry, Biotechnology and Food Science, NMBU Norwegian University of Life Sciences, N-1432 Ås, Norway, and.
Ellinor B HeggsetRISE PFI AS, Høgskoleringen 6b, N-7491 Trondheim, Norway.ORCID 0000-0001-8876-8898
Vincent G H Eijsinkthe Faculty of Chemistry, Biotechnology and Food Science, NMBU Norwegian University of Life Sciences, N-1432 Ås, Norway, and.ORCID 0000-0002-9220-8743
Finn L AachmannFrom NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Sem Sælands vei 6/8, N-7491 Trondheim, Norway, finn.l.aachmann@ntnu.no.ORCID 0000-0003-1613-4663

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of polysaccharides such as cellulose and chitin, a feature that makes them key tools in industrial biomass conversion processes. The catalytic domains of a considerable fraction of LPMOs and other carbohydrate-active enzymes (CAZymes) are tethered to carbohydrate-binding modules (CBMs) by flexible linkers. These linkers preclude X-ray crystallographic studies, and the functional implications of these modular assemblies remain partly unknown. Here, we used NMR spectroscopy to characterize structural and dynamic features of full-length modular

Indexed as

Catalytic DomainCelluloseCrystallography, X-RayFungal PolysaccharidesMixed Function OxygenasesModels, MolecularOxidation-ReductionProtein ConformationStreptomyces coelicolorCelluloseFungal PolysaccharidesMixed Function Oxygenasesbiotechnologycarbohydrate-active enzymecarbohydrate-binding modulecellulosecopper monooxygenasehydrolytic enzymeLPMOlytic polysaccharide monooxygenasenanofibrilprotein linker

Identifiers

PMID29967065
PMCPMC6109919

What OpenQuestion holds

Textmetadata
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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.