Evidence map›Paper›PMID 40994537›Full record

ArticleComputational and structural biotechnology journal2025

Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans.

Rubén Muñoz-Tafalla, Isabel Cea-Rama, Fadia V Cervantes, Jose L Gonzalez-Alfonso, Francisco J Plou, Julio Polaina, Julia Sanz-Aparicio, Manuel Ferrer, Víctor Guallar, David Talens-Perales

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In one paragraph

Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Rubén Muñoz-TafallaDepartment of Life Sciences, Barcelona Supercomputing Center (BSC), Barcelona 08034, Spain.
Isabel Cea-RamaInstitute of Physical Chemistry Blas Cabrera (IQF), CSIC, Madrid 28006, Spain.
Fadia V CervantesInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid 28049, Spain.
Jose L Gonzalez-AlfonsoInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid 28049, Spain.
Francisco J PlouInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid 28049, Spain.
Julio PolainaInstitute of Agrochemistry and Food Technology, Spanish National Research Council (IATA-CSIC), Paterna, Valencia 46980, Spain.
Julia Sanz-AparicioInstitute of Physical Chemistry Blas Cabrera (IQF), CSIC, Madrid 28006, Spain.
Manuel FerrerInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid 28049, Spain.
Víctor GuallarDepartment of Life Sciences, Barcelona Supercomputing Center (BSC), Barcelona 08034, Spain.
David Talens-PeralesInstitute of Agrochemistry and Food Technology, Spanish National Research Council (IATA-CSIC), Paterna, Valencia 46980, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structural complexity of xylan makes its complete degradation challenging. Strategies to improve its hydrolysis often requires enzyme cocktails with multiple specific activities or proteins harboring multiple catalytic domains. Here, we introduce a novel approach through the design of Xyn11

Indexed as

Feruloyl esterasePluriZymeProtein EngineeringXylanXylanase

Identifiers

PMID40994537
PMCPMC12454871

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.