Evidence map›Paper›PMID 40248884›Full record

ArticleProtein science : a publication of the Protein Society2025

The structural basis for the broad aldehyde specificity of the aminoaldehyde dehydrogenase PauC from the human pathogen Pseudomonas aeruginosa.

Yudy V Cardona-Cardona, Lilian González-Segura, Rogelio Rodríguez-Sotres, Javier Andrés Juárez-Díaz, Carlos Mújica-Jiménez, Ignacio Regla, Manuel López-Ortiz, Rosario A Muñoz-Clares

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

8 authors.

Yudy V Cardona-CardonaDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Lilian González-SeguraDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Rogelio Rodríguez-SotresDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Javier Andrés Juárez-DíazDepartamento de Biología Celular, Facultad de Ciencias, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Carlos Mújica-JiménezDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Ignacio ReglaFES Zaragoza, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Manuel López-OrtizFES Zaragoza, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.
Rosario A Muñoz-ClaresDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad de México, Mexico.ORCID 0000-0002-0115-3565

Funding

Consejo Nacional de Ciencia y Tecnología (CONACYT) 252123Consejo Nacional de Ciencia y Tecnología (CONACYT) 283524UNAM-PAPIIT IN220317
6 · The paper itself

Abstract

Despite significant differences in size and formal charge, the aldehyde dehydrogenase PaPauC (PA5312) from Pseudomonas aeruginosa PAO1 efficiently catalyzes the NAD

Indexed as

AldehydesBacterial ProteinsPseudomonas aeruginosaCatalytic DomainCrystallography, X-RayHumansMolecular Docking SimulationMutagenesis, Site-DirectedSubstrate SpecificityAldehydesBacterial Proteinsamino aldehydes and indole‐3‐acetaldehyde oxidationmolecular dockingP. aeruginosa pathogenicitysite‐directed mutagenesisstructure–function relationshipsX‐ray protein structure

Identifiers

PMID40248884
PMCPMC12006823

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.