Evidence map›Paper›PMID 42290085›Full record

ArticleACS infectious diseases2026

Biochemical and Structural Characterization of Two-domain Glycoside Hydrolase PgaB from

Amanda Freitas Cruz, Pedro Ricardo Vieira Hamann, Francisco Eduardo Gontijo Guimaraes, Andrei Nicoli Gebieluca Dabul, Ruth Celestina Condori Mamani, Marcos Pileggi, Mario de Oliveira Neto, Matheus Rodrigues Sauda, Guilherme Targino Valente, Tsutomu Matsui and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS infectious diseases, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

13 authors.

Amanda Freitas CruzInstituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense 400, São Carlos, SP 13566-590, Brazil.
Pedro Ricardo Vieira HamannInstituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense 400, São Carlos, SP 13566-590, Brazil.
Francisco Eduardo Gontijo GuimaraesInstituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense 400, São Carlos, SP 13566-590, Brazil.
Andrei Nicoli Gebieluca DabulSchool of Pharmaceutical Sciences, São Paulo State University, Rodovia Araraquara-Jáu, km 1, Araraquara, SP 14800-903, Brazil.
Ruth Celestina Condori MamaniInstituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense 400, São Carlos, SP 13566-590, Brazil.
Marcos PileggiEnvironmental Microbiology Laboratory, Life Sciences and Health Institute, Structural and Molecular Biology, and Genetics Department, Ponta Grossa State University, Ponta Grossa 84030-900, Brazil.
Mario de Oliveira NetoInstitute of Biosciences, Sao Paulo State University, District of Rubiao Jr., Botucatu, SP 18618-970, Brazil.
Matheus Rodrigues SaudaLaboratory of Applied Biotechnology, São Paulo State University, Botucatu 18618-687, Brazil.
Guilherme Targino ValenteClinical Hospital of Medical School of Botucatu, Botucatu 18618-687, Brazil.
Tsutomu MatsuiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd, Menlo Park, California 94025, United States.
Thomas M WeissStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd, Menlo Park, California 94025, United States.
Evandro A AraújoBrazilian Synchrotron Light Laboratory, Brazilian Center for Research in Energy and Materials, Giuseppe Maximo Scolfaro, 10000, Campinas, SP 13083-970, Brazil.
Igor PolikarpovInstituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense 400, São Carlos, SP 13566-590, Brazil.ORCID 0000-0001-9496-4174

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
PILATUS3 X 1M X-ray detectorS10OD021512 · OD · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 2016 to 2016
$550k
NIGMS NIH HHS P30 GM133894NIH HHS S10 OD021512
6 · The paper itself

Abstract

Antimicrobial resistance (AMR) is a critical global health threat, with projections estimating up to 10 million deaths annually by 2050. One of the strategies for developing bacterial AMR is the formation of microbial biofilms (BFs). Thus, enzymes capable of degrading BF exopolysaccharides represent potential tools for BF disruption. In this work, we characterize β-1,6-

Indexed as

AcetylglucosaminidaseBacterial ProteinsBiofilmsGlycoside HydrolasesSerratia marcescensStaphylococcus aureusAnti-Bacterial AgentsMicrobial Sensitivity TestsAcetylglucosaminidaseAnti-Bacterial AgentsBacterial ProteinsGlycoside Hydrolasesbiofilm degradationPgaBSerratia marcescensStaphylococcus aureus

Identifiers

PMID42290085
PMCPMC13366581

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.