Evidence map›Paper›PMID 42275020›Full record

ReviewRedox report : communications in free radical research2026

Enzymatic and non-enzymatic oxidation of fibrillar collagen.

Felipe Caliani Mathias-Netto, Nathalia Margarida Cantuária, Renato Simões Gaspar

Abstract readReview
In one paragraph

Review in Redox report : communications in free radical research, 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. Review
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.

Felipe Caliani Mathias-NettoDepartment of Pharmacology, Faculty of Medical Sciences, University of Campinas (UNICAMP), Campinas, Brazil.
Nathalia Margarida CantuáriaDepartment of Pharmacology, Faculty of Medical Sciences, University of Campinas (UNICAMP), Campinas, Brazil.
Renato Simões GasparDepartment of Pharmacology, Faculty of Medical Sciences, University of Campinas (UNICAMP), Campinas, Brazil.ORCID 0000-0001-6639-9470

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesCollagen is a long-lived protein present in the extracellular matrix of force-bearing tissues. It has a unique amino acid composition of predominantly glycine, proline and hydroxyproline that repeats throughout its characteristic triple helical structure. In the extracellular space, collagen interact first by a non-enzymatic, entropy-driven process given their high hydrophobicity. Then, enzymes, such as lysyl oxidase (LOX), create covalent bonds (i.e. crosslinks) between triple helices, generating reactive oxygen species (ROS) as a byproduct. Moreover, it was recently discovered that collagen itself generates ROS upon stretching. Therefore, given the close proximity of ROS-generating sources, it seems plausible that collagen undergoes non-enzymatic oxidation.

methodsThis review discusses collagen structure, mechanisms of crosslink formation and collagen oxidation.

resultsDespite abundant data on the mechanisms of LOX-mediated collagen oxidation, there is sparse data on the effects of non-enzymatic oxidation on collagen chemical and biophysical properties, as well as its effects on cells and tissues. DISCUSSION: The premise that collagen oxidation could lead to persistent damage is discussed in light of the immunogenicity and proteolysis induced by such modifications. Overall, data support that oxidative modifications in collagen should be further explored and could pose as a novel underlying mechanism in ageing and chronic diseases.

Indexed as

Fibrillar CollagensAnimalsCollagenHumansOxidation-ReductionProtein-Lysine 6-OxidaseReactive Oxygen SpeciesCollagenFibrillar CollagensProtein-Lysine 6-OxidaseReactive Oxygen SpeciesCollagencrosslinkoxidationoxidative stresspost-translational modificationprotein biophysicsprotein oxidationreactive oxygen species

Identifiers

PMID42275020
PMCPMC13262103

What OpenQuestion holds

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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.