Evidence map›Paper›PMID 32661601›Full record

ReviewWorld journal of microbiology & biotechnology2020

The crucial role of bacterial laccases in the bioremediation of petroleum hydrocarbons.

Yan Zhang, Dong-Fa Lin, Jun Hao, Zhi-Hao Zhao, Ying-Jiu Zhang

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 6% 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

5 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Fungal Laccases: The Forefront of Enzymes for Sustainability.Journal of fungi (Basel, Switzerland) · 2021
    Review
  5. 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

5 authors at 1 institution in 2 countries.

Yan ZhangKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130012, People's Republic of China.
Dong-Fa LinKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130012, People's Republic of China.
Jun HaoKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130012, People's Republic of China.
Zhi-Hao ZhaoKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130012, People's Republic of China.
Ying-Jiu ZhangKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130012, People's Republic of China. yingjiu@jlu.edu.cn.ORCID http://orcid.org/0000-0002-8047-9204
Jilin University · CN

Funding

Department of Science and Technology of Jilin Province 20140101020JC
6 · The paper itself

Abstract

Laccases (EC 1.10.3.2) are a class of metallo-oxidases found in a variety of fungi, plants, and bacteria as well as in certain insects. They can oxidize a wide variety of organic compounds and can be widely applied in many fields, especially in the field of biodegradation and detoxification of environmental pollutants. The practical efficacy of laccases depends on their ability to capture the target substance as well as their catalytic activity, which is related to their catalytic center, substrate selectivity, and substrate tolerance. Over the past few decades, many laccases have been identified in plants and fungi. Concurrently, bacterial laccases have received increasing attention because of their high thermostability and high tolerance to organic compounds. The aim of this review is to summarize the role of bacterial laccases in the bioremediation of petroleum hydrocarbons and to outline the correlation between the molecular structure of the mononuclear T1 Cu center of bacterial laccases and their substrate preference.

Indexed as

Biodegradation, EnvironmentalAmino Acid SequenceBacteriaBacterial ProteinsLaccasePetroleumPhenolsPolycyclic Aromatic HydrocarbonsProtein ConformationBacterial ProteinsLaccasePetroleumPhenolsPolycyclic Aromatic HydrocarbonsBacterial laccaseBioremediationHydrocarbonPetroleumSubstrate preference

Identifiers

PMID32661601
OpenAlexW3042799963

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.