Evidence map›Paper›PMID 32024019›Full record

ReviewInternational journal of molecular sciences2020

Laccase Properties, Physiological Functions, and Evolution.

Grzegorz Janusz, Anna Pawlik, Urszula Świderska-Burek, Jolanta Polak, Justyna Sulej, Anna Jarosz-Wilkołazka, Andrzej Paszczyński

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 236 papers.

0numbers the graph read from it
0cells of the map it votes in
236citing papers in PubMed
76.2field-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

236 citing papers in PubMed, 638 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Ecology and Fungicolous Lifestyle ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  8. Evolutionary dynamics of the arthropod molting machinery.Molecular biology and evolution · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Review
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  14. Review
  15. Article
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  19. Review
  20. Article

176 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Grzegorz JanuszDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Anna PawlikDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Urszula Świderska-BurekDepartment of Botany, Mycology and Ecology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Jolanta PolakDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Justyna SulejDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Anna Jarosz-WilkołazkaDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
Andrzej PaszczyńskiProfessor Emeritus, School of Food Science, University of Idaho, Moscow, ID 83844, USA.
Maria Curie-Skłodowska University · PLUniversity of Idaho · US

Funding

Narodowe Centrum Nauki 2014/13/B/NZ9/02106Narodowe Centrum Nauki 2016/21/D/NZ9/02460Narodowe Centrum Nauki 2017/01/X/NZ9/00819Narodowe Centrum Nauki DEC-2013/09/B/NZ9/01829Narodowe Centrum Nauki DEC-2014/15/B/NZ9/01990
6 · The paper itself

Abstract

Discovered in 1883, laccase is one of the first enzymes ever described. Now, after almost 140 years of research, it seems that this copper-containing protein with a number of unique catalytic properties is widely distributed across all kingdoms of life. Laccase belongs to the superfamily of multicopper oxidases (MCOs)-a group of enzymes comprising many proteins with different substrate specificities and diverse biological functions. The presence of cupredoxin-like domains allows all MCOs to reduce oxygen to water without producing harmful byproducts. This review describes structural characteristics and plausible evolution of laccase in different taxonomic groups. The remarkable catalytic abilities and broad substrate specificity of laccases are described in relation to other copper-containing MCOs. Through an exhaustive analysis of laccase roles in different taxa, we find that this enzyme evolved to serve an important, common, and protective function in living systems.

Indexed as

BacteriaEvolution, MolecularFungiHumansLaccasePhylogenyProtein DomainsSubstrate SpecificityLaccaseevolutionfunctionlaccaseligninmelaninmulticopper oxidasepolyphenol oxidase

Identifiers

PMID32024019
PMCPMC7036934
OpenAlexW3004194370

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.