Evidence map›Paper›PMID 29222333›Full record

ArticleThe Journal of biological chemistry2018

Structural determinants of bacterial lytic polysaccharide monooxygenase functionality.

Zarah Forsberg, Bastien Bissaro, Jonathan Gullesen, Bjørn Dalhus, Gustav Vaaje-Kolstad, Vincent G H Eijsink

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 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
11.6field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 106 citations in OpenAlex.

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  14. Immunization with lytic polysaccharide monooxygenase CbpD induces protective immunity againstProceedings of the National Academy of Sciences of the United States of America · 2023
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  19. Characterization of a unique polysaccharide monooxygenase from the plant pathogenProceedings of the National Academy of Sciences of the United States of America · 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

6 authors at 3 institutions in 2 countries.

Zarah ForsbergFrom the Faculty of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway, zarah.forsberg@nmbu.no.
Bastien BissaroFrom the Faculty of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Jonathan GullesenFrom the Faculty of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Bjørn Dalhusthe Department of Medical Biochemistry, Institute for Clinical Medicine, University of Oslo, 0318 Oslo, Norway, and.
Gustav Vaaje-KolstadFrom the Faculty of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Vincent G H EijsinkFrom the Faculty of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences (NMBU), 1432 Ås, Norway.
Norwegian University of Life Sciences · NOLaboratoire d'Ingénierie des Systèmes Biologiques et des Procédés · FROslo University Hospital · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial lytic polysaccharide monooxygenases (LPMO10s) use redox chemistry to cleave glycosidic bonds in the two foremost recalcitrant polysaccharides found in nature, namely cellulose and chitin. Analysis of correlated mutations revealed that the substrate-binding and copper-containing surface of LPMO10s composes a network of co-evolved residues and interactions, whose roles in LPMO functionality are unclear. Here, we mutated a subset of these correlated residues in a newly characterized C1/C4-oxidizing LPMO10 from

Indexed as

Bacterial ProteinsCatalysisHydrogen PeroxideMicromonosporaMixed Function OxygenasesOxidation-ReductionProtein DomainsStructure-Activity RelationshipSubstrate SpecificityBacterial ProteinsHydrogen PeroxideMixed Function Oxygenasescellulosechitinhydrogen peroxideLPMOprotein evolutionregioselectivitysite-directed mutagenesissubstrate specificity

Identifiers

PMID29222333
PMCPMC5787815
OpenAlexW2772940805

What OpenQuestion holds

Textmetadata
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.