Evidence map›Paper›PMID 41303578›Full record

ArticleInternational journal of molecular sciences2025

Chemical Modification of

Juan S Pardo-Tamayo, Maria Camila Muñoz-Vega, Oscar L Alférez, Evelyn L Guerrero-Tobar, Chonny Herrera-Acevedo, Ericsson Coy-Barrera, César A Godoy

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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

7 authors.

Juan S Pardo-TamayoLaboratorio de Investigación en Biocatálisis y Biotransformaciones (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Department of Chemistry, Universidad del Valle, Cali 760001, Colombia.ORCID 0000-0002-0345-2489
Maria Camila Muñoz-VegaLaboratorio de Investigación en Biocatálisis y Biotransformaciones (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Department of Chemistry, Universidad del Valle, Cali 760001, Colombia.ORCID 0009-0004-7630-2539
Oscar L AlférezLaboratorio de Investigación en Biocatálisis y Biotransformaciones (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Department of Chemistry, Universidad del Valle, Cali 760001, Colombia.ORCID 0009-0004-3864-4482
Evelyn L Guerrero-TobarLaboratorio de Investigación en Biocatálisis y Biotransformaciones (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Department of Chemistry, Universidad del Valle, Cali 760001, Colombia.
Chonny Herrera-AcevedoDepartment of Chemical Engineering, Universidad ECCI, Bogotá 111311, Colombia.ORCID 0000-0002-6220-9091
Ericsson Coy-BarreraBioorganic Chemistry Laboratory, Facultad de Ciencias Básicas y Aplicadas, Universidad Militar Nueva Granada, Cajicá 250247, Colombia.ORCID 0000-0002-3553-9749
César A GodoyLaboratorio de Investigación en Biocatálisis y Biotransformaciones (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Department of Chemistry, Universidad del Valle, Cali 760001, Colombia.ORCID 0000-0003-4393-9889

Funding

Universidad del Valle CI 71400
6 · The paper itself

Abstract

Chemical modification is a valuable strategy for tuning enzyme functionality by introducing new reactive groups without disrupting the overall fold. Conventional amination using ethylenediamine (EDA) is effective, but the resulting modified proteins show limited reactivity for conjugation at neutral pH, and the modifier itself poses safety concerns due to its volatility and corrosive nature. Dihydrazides, in contrast, offer a safer and more versatile alternative: they operate through the same carboxyl-activation mechanism while enabling systematic investigation of chain-length effects. In this study,

Indexed as

AscomycotaEurotialesFungal ProteinsHydrazinesLaccaseLipaseSordarialesKineticsMolecular Docking SimulationFungal ProteinsHydrazinesLaccaseLipaseaminationdihydrazidesenzyme chemical modificationkinetic parameterslaccaselipasemolecular dynamics

Identifiers

PMID41303578
PMCPMC12652127

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.