Evidence map›Paper›PMID 29602785›Full record

ArticleApplied and environmental microbiology2018

The Pyrroloquinoline-Quinone-Dependent Pyranose Dehydrogenase from Coprinopsis cinerea Drives Lytic Polysaccharide Monooxygenase Action.

Anikó Várnai, Kiwamu Umezawa, Makoto Yoshida, Vincent G H Eijsink

Open access · hybridAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.5field-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

32 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  4. Microbiology spectrum · 2024
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  18. Genome and Secretome Analysis ofMicroorganisms · 2021
    Article
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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 2 institutions in 2 countries.

Anikó Várnai *Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.ORCID 0000-0002-2796-514X
Kiwamu Umezawa *Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Makoto Yoshida *Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo, Japan ymakoto@cc.tuat.ac.jp vincent.eijsink@nmbu.no.
Vincent G H Eijsink *Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway ymakoto@cc.tuat.ac.jp vincent.eijsink@nmbu.no.
Norwegian University of Life Sciences · NOTokyo University of Agriculture and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fungi secrete a set of glycoside hydrolases and oxidoreductases, including lytic polysaccharide monooxygenases (LPMOs), for the degradation of plant polysaccharides. LPMOs catalyze the oxidative cleavage of glycosidic bonds after activation by an external electron donor. So far, only flavin-dependent oxidoreductases (from the auxiliary activity [AA] family AA3) have been shown to activate LPMOs. Here, we present LPMO activation by a pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase (PDH) from

Indexed as

AgaricalesElectron TransportFungal ProteinsMixed Function OxygenasesOxidation-ReductionOxidoreductasesPolysaccharidesPQQ CofactorFungal ProteinsMixed Function OxygenasesOxidoreductasesPolysaccharidesPQQ CofactorAA12AA9carbohydrate-binding moduleelectron transferLPMOlytic polysaccharide monooxygenasePQQ-dependent PDH

Identifiers

PMID29602785
PMCPMC5960967
OpenAlexW2795332788

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.