Evidence map›Paper›PMID 41588624›Full record

ArticleJournal of chemical information and modeling2026

Mechanism of Hyaluronic Acid Hydrolysis Catalyzed by Snake Venom Hyaluronidase.

Juliana Castro-Amorim, Maria J Ramos, Pedro A Fernandes

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 2026. 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

3 authors.

Juliana Castro-AmorimLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0002-7689-4448
Maria J RamosLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0002-7554-8324
Pedro A FernandesLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0003-2748-4722

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hyaluronidases are widely distributed in nature being ubiquitous in snake species (svHyal). They catalyze the hydrolysis of β-1,4-glycosidic bonds in hyaluronic acid, a critical constituent of the extracellular matrix. This facilitates the spread of venom toxins into the bloodstream, exacerbating tissue damage and systemic toxicity─a rationale for their common designation as "spreading factors". While svHyals are not directly toxic, they substantially contribute to the morbidity and mortality associated with snakebite envenomation, the world's most lethal neglected tropical disease. Despite their important role in tissue penetration, the atomic-level reaction mechanism of these enzymes remains poorly understood. To bridge this knowledge gap, we studied the chemical mechanism of the Hyal-1 enzyme isolated from the Puff Adder viper (

Indexed as

BiocatalysisHyaluronic AcidHyaluronoglucosaminidaseSnake VenomsAnimalsCatalytic DomainHydrolysisMolecular Dynamics SimulationHyaluronic AcidHyaluronoglucosaminidaseSnake Venoms

Identifiers

PMID41588624
PMCPMC13080975

What OpenQuestion holds

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LicenceCC BY
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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.