Evidence map›Paper›PMID 42012095›Full record

ArticleChemistry & biodiversity2026

Biochemical Characterization of a Kunitz-Type Protease Inhibitor From Mimosa regnellii and Its Effects on Melanoma Cell Viability and Angiogenesis.

Luciana Maria Araújo Rabêlo, Pedro Henrique de Oliveira Cardoso, Leonardo Thiago Duarte Barreto Nobre, Paula Ivani Medeiros Dos Santos, Sheyla Varela Lucena, Raphael Paschoal Serquiz, Marcelo Porto Bemquerer, Hugo Alexandre de Oliveira Rocha, Helena Bonciani Nader, Elizeu Antunes Dos Santos and 3 more

Abstract read
In one paragraph

Article in Chemistry & biodiversity, 2026. 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

13 authors.

Luciana Maria Araújo RabêloLaboratório De Química e Função De Proteínas Bioativas, Centro de Biociências, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Pedro Henrique de Oliveira CardosoPrograma de Pós-Graduação em Ciências Ambientais e Sustentabilidade Agropecuária, Universidade Católica Dom Bosco (UCDB), Campo Grande, Brazil.
Leonardo Thiago Duarte Barreto NobreDepartamento De Bioquímica, Universidade Federal de São Paulo (UNIFESP), São Paulo, São Paulo, Brazil.
Paula Ivani Medeiros Dos SantosLaboratório De Química e Função De Proteínas Bioativas, Centro de Biociências, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Sheyla Varela LucenaDiretoria de Recursos Naturais, Programa de Mestrado em Uso Sustentável dos Recursos Naturais, Instituto Federal de Ciências e Tecnologia Do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Raphael Paschoal SerquizLaboratório De Química e Função De Proteínas Bioativas, Centro de Biociências, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Marcelo Porto BemquererEmbrapa Gado de Leite, Juiz de Fora, Minas Gerais, Brazil.
Hugo Alexandre de Oliveira RochaLaboratório De Biotecnologia de Polímeros Naturais-BIOPOL, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Helena Bonciani NaderDepartamento De Bioquímica, Universidade Federal de São Paulo (UNIFESP), São Paulo, São Paulo, Brazil.
Elizeu Antunes Dos SantosLaboratório De Química e Função De Proteínas Bioativas, Centro de Biociências, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Adeliana Silva de OliveiraLaboratório De Química e Função De Proteínas Bioativas, Departamento De Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.
Breno Emanuel Farias FrihlingLaboratório De Purificação de Proteínas e suas Funções Biológicas, Programa de Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, Brazil.
Ludovico MiglioloLaboratório De Química e Função De Proteínas Bioativas, Centro de Biociências, Departamento De Bioquímica, Universidade Federal do Rio Grande Do Norte, Natal, Rio Grande do Norte, Brazil.ORCID https://orcid.org/0000-0002-6606-2189

Funding

CAPESCNPqFUNDECT
6 · The paper itself

Abstract

Cancer is a term used to represent more than 100 diseases, including malignant tumors of different localizations. Among these types, cutaneous melanoma is one of the most common types of skin cancer worldwide. Newer, non-invasive, and more effective forms of treatment are urgently needed. Recently, the cancer membrane has emerged as a novel target for new anticancer drugs. Serine protease inhibitors are researched across all kingdoms; however, the Plantae kingdom is a more sustainable producer of bioactive molecules, including serine protease inhibitors. In this study, a Kunitz trypsin inhibitor (JTI) purified by RP-HPLC from Mimosa regnellii seeds was sequenced, its inhibitory activity quantified, and its inhibition constant determined. It was then tested for its ability to induce cell death via the apoptotic pathway in B16-F10 mouse melanoma cells. To evaluate its pro-apoptotic capacity, the inhibitor's effects on reactive oxygen species release, calcium release, cell morphological changes, and the inhibition of angiogenic and migratory activities of rabbit endothelial cells (RaEC) were also assessed in vitro. Tests for toxicity against normal cells were performed, confirming that JTI acts on melanoma cells with an IC

Indexed as

Antineoplastic Agents, PhytogenicMimosaNeovascularization, PathologicPeptidesSerine Proteinase InhibitorsAnimalsApoptosisCell Line, TumorCell MovementCell ProliferationCell SurvivalDose-Response Relationship, DrugDrug Screening Assays, AntitumorMelanomaMelanoma, ExperimentalMiceAntineoplastic Agents, PhytogenicKunitz-type protease inhibitor, plantPeptidesPlant ProteinsReactive Oxygen SpeciesSerine Proteinase Inhibitorsangiogenesiscell migrationmelanomamitochondrial apoptosisprotease inhibitor

Identifiers

PMID42012095
PMCPMC13098310

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.