Evidence map›Paper›PMID 29259126›Full record

ArticleThe Journal of biological chemistry2018

Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability.

Daniel Kracher, Martina Andlar, Paul G Furtmüller, Roland Ludwig

Open access · hybridAbstract 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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 105 citations in OpenAlex.

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  14. 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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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

4 authors at 1 institution in 1 country.

Daniel KracherFrom the Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, and daniel.kracher@boku.ac.at.
Martina AndlarFrom the Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, and.
Paul G Furtmüllerthe Division of Biochemistry, Department of Chemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Roland LudwigFrom the Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, and roland.ludwig@boku.ac.at.
BOKU University · AT

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-containing enzymes that oxidatively degrade insoluble plant polysaccharides and soluble oligosaccharides. Upon reductive activation, they cleave the substrate and promote biomass degradation by hydrolytic enzymes. In this study, we employed LPMO9C from

Indexed as

Catalytic DomainCelluloseCopperFungal ProteinsMixed Function OxygenasesNeurospora crassaCelluloseCopperFungal ProteinsMixed Function OxygenasesActive-site coppercarbohydrate-binding proteinlytic polysaccharide monooxygenasemetalloenzymeplant cell wallpolysaccharideprotein stability

Identifiers

PMID29259126
PMCPMC5798298
OpenAlexW2778330153

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.