Evidence map›Paper›PMID 36567772›Full record

ArticleACS catalysis2022

Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase.

Vânia Brissos, Patrícia T Borges, Reyes Núñez-Franco, Maria Fátima Lucas, Carlos Frazão, Emanuele Monza, Laura Masgrau, Tiago N Cordeiro, Lígia O Martins

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
6.1field-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

11 citing papers in PubMed, 32 citations in OpenAlex.

  1. Exploring the role of oxidative defects in polyethylene binding and degradation by a Rhodococcus opacus R7 multicopper oxidase: a computational perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  8. Flexible active-site loops fine-tune substrate specificity of hyperthermophilic metallo-oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  9. Flexible active-site loops fine-tune substrate specificity of hyperthermophilic metallo-oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    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

9 authors at 2 institutions in 2 countries.

Vânia BrissosInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av da República, 2780-157 Oeiras, Portugal.
Patrícia T BorgesInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av da República, 2780-157 Oeiras, Portugal.
Reyes Núñez-FrancoZymvol Biomodeling, Carrer Roc Boronat, 117, 08018 Barcelona, Spain.
Maria Fátima LucasZymvol Biomodeling, Carrer Roc Boronat, 117, 08018 Barcelona, Spain.ORCID https://orcid.org/0000-0001-8672-9940
Carlos FrazãoInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av da República, 2780-157 Oeiras, Portugal.
Emanuele MonzaZymvol Biomodeling, Carrer Roc Boronat, 117, 08018 Barcelona, Spain.
Laura MasgrauZymvol Biomodeling, Carrer Roc Boronat, 117, 08018 Barcelona, Spain.ORCID https://orcid.org/0000-0003-4495-508X
Tiago N CordeiroInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av da República, 2780-157 Oeiras, Portugal.
Lígia O MartinsInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av da República, 2780-157 Oeiras, Portugal.ORCID https://orcid.org/0000-0003-0082-9591
Universidade Nova de Lisboa · PTUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases are in increasing demand as innovative solutions in the biorefinery fields. Here, we combine mutagenesis with structural, kinetic, and

Identifiers

PMID36567772
PMCPMC9775220
OpenAlexW4223918060

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.