Evidence map›Paper›PMID 39000302›Full record

ArticleInternational journal of molecular sciences2024

Alterations in the Structure, Composition, and Organization of Galactosaminoglycan-Containing Proteoglycans and Collagen Correspond to the Progressive Stages of Dupuytren's Disease.

Luiz Guilherme S Lenzi, João Baptista Gomes Dos Santos, Renan P Cavalheiro, Aline Mendes, Elsa Y Kobayashi, Helena B Nader, Flavio Faloppa

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. 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.

Luiz Guilherme S LenziDepartment of Orthopaedics and Traumatology, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04038-032, SP, Brazil.ORCID 0000-0003-3558-6710
João Baptista Gomes Dos SantosDepartment of Orthopaedics and Traumatology, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04038-032, SP, Brazil.ORCID 0000-0003-0199-6578
Renan P CavalheiroMolecular Biology Program, Instituto de Farmacologia e Biologia Molecular, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04024-002, SP, Brazil.ORCID 0000-0002-3961-4419
Aline MendesMolecular Biology Program, Instituto de Farmacologia e Biologia Molecular, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04024-002, SP, Brazil.ORCID 0000-0001-9255-0429
Elsa Y KobayashiMolecular Biology Program, Instituto de Farmacologia e Biologia Molecular, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04024-002, SP, Brazil.
Helena B NaderMolecular Biology Program, Instituto de Farmacologia e Biologia Molecular, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04024-002, SP, Brazil.ORCID 0000-0002-7569-2166
Flavio FaloppaDepartment of Orthopaedics and Traumatology, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04038-032, SP, Brazil.

Funding

Conselho Nacionnal do Desenvolvimento Científico e Tecnológico, Brazil 421697/2021-0Coordenação de Aperfeicoamento de Pessoal de Nível Superior Proex 0727/2022Financiadora de Estudos e Projetos 04.13.0462.03Fundação de Amparo à Pesquisa do Estado de São Paulo 2015/02345-0
6 · The paper itself

Abstract

Dupuytren's disease (DD) is a prevalent fibroproliferative disorder of the hand, shaped by genetic, epigenetic, and environmental influences. The extracellular matrix (ECM) is a complex assembly of diverse macromolecules. Alterations in the ECM's content, structure and organization can impact both normal physiological functions and pathological conditions. This study explored the content and organization of glycosaminoglycans, proteoglycans, and collagen in the ECM of patients at various stages of DD, assessing their potential as prognostic indicators. This research reveals, for the first time, relevant changes in the complexity of chondroitin/dermatan sulfate structures, specifically an increase of disaccharides containing iduronic acid residues covalently linked to either N-acetylgalactosamine 6-

Indexed as

CollagenDecorinDupuytren ContractureProteoglycansAgedChondroitin SulfatesDermatan SulfateDisease ProgressionExtracellular MatrixFemaleGlycosaminoglycansHumansMaleMiddle AgedPolysaccharidesVersicansChondroitin SulfatesCollagenDecorinDermatan SulfategalactosaminoglycanGlycosaminoglycansPolysaccharidesProteoglycansVersicanschondroitin and dermatan sulfatescollagendecorinextracellular matrixfascia palmarhyaluronic acidproteoglycanssulfated glycosaminoglycansversican

Identifiers

PMID39000302
PMCPMC11241189

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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.