Evidence map›Paper›PMID 33489432›Full record

ArticleACS catalysis2021

Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase.

Alfons K G Felice, Christian Schuster, Alan Kadek, Frantisek Filandr, Christophe V F P Laurent, Stefan Scheiblbrandner, Lorenz Schwaiger, Franziska Schachinger, Daniel Kracher, Christoph Sygmund and 4 more

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Interface engineering of cellobiose dehydrogenase improves interdomain electron transfer.Protein science : a publication of the Protein Society · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Cellobiose dehydrogenase in biofuel cells.Current opinion in biotechnology · 2022
    Review
  13. Article
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

14 authors at 2 institutions in 2 countries.

Alfons K G FeliceBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Christian SchusterBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Alan KadekBIOCEV-Institute of Microbiology, The Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
Frantisek FilandrBIOCEV-Institute of Microbiology, The Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
Christophe V F P LaurentBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Stefan ScheiblbrandnerBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Lorenz SchwaigerBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Franziska SchachingerBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Daniel KracherBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Christoph SygmundBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Petr ManBIOCEV-Institute of Microbiology, The Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
Petr HaladaBIOCEV-Institute of Microbiology, The Czech Academy of Sciences, Prumyslova 595, 252 50 Vestec, Czech Republic.
Chris OostenbrinkDepartment of Material Sciences and Process Engineering, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Roland LudwigBiocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
BOKU University · ATCzech Academy of Sciences · CZ

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The natural function of cellobiose dehydrogenase (CDH) to donate electrons from its catalytic flavodehydrogenase (DH) domain via its cytochrome (CYT) domain to lytic polysaccharide monooxygenase (LPMO) is an example of a highly efficient extracellular electron transfer chain. To investigate the function of the CYT domain movement in the two occurring electron transfer steps, two CDHs from the ascomycete

Identifiers

PMID33489432
PMCPMC7818652
OpenAlexW3116300474

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.