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1.
Am J Ophthalmol Case Rep ; 35: 102075, 2024 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-38841151

RESUMO

Purpose: This case report aims to present a rare instance of conjunctival melanoma in a 5-year-old patient and contribute to the limited body of knowledge on pediatric conjunctival melanoma. The purpose is to understand the characteristics, diagnosis, and management of this uncommon malignancy in young individuals. Observations: The case describes a 5-year-old female with a progressively growing pigmented conjunctival lesion. The lesion was observed to be located on the temporal conjunctiva of the right eye and displayed distinctive features, including feeder vessels. Imaging revealed specific dimensions of the lesion and ruled out deeper invasions. Histopathological examination revealed architectural and cytologic atypia, positive immunohistochemical staining for HMB-45, and a Ki67 proliferation index of 20 %, confirming the diagnosis of conjunctival melanoma. Conclusions: Conjunctival melanoma, an uncommon malignancy even more so in pediatric patients, typically presents with pigmented growths and feeder vessels. This case underscores the need for thorough diagnosis and early intervention, as conjunctival melanoma can lead to devastating outcomes. The rarity of such cases limits our understanding of their etiology and progression. This case contributes to the literature on pediatric conjunctival melanoma and reinforces the importance of vigilance in detecting and managing ocular pigmented lesions in children.

3.
Artigo em Espanhol | LILACS | ID: lil-660038

RESUMO

Antecedentes: En las proteínas no se logra siempre su cristalización, de buen tamaño y de buena calidad para someterla a difracción de rayos X. De tal manera que se abre un campo para el desarrollo de estudios teóricos moleculares y proteínicos, que permiten la representación de las moléculas en tres dimensiones, proporcionando una información espacial para estudiar la interacción entre ligandos y receptores macromoleculares. Materialesy Métodos: Estudio In silico, a partir del análisis de secuencias primarias de seis diferentes proteínas LuxS cristalizadas de diversas bacterias, se seleccionó la proteína 1J6X del Helicobacter pylori, por su similaridad con la secuencia de la proteína LuxS en Porphyromonas gingivalis (P. gingivalis) cepa W83, para producir un modelo por homología de esta proteína, utilizando los programas Sybyl y MOE. Se realizó un acoplamiento con el ligando natural para evaluar la reproducibilidad del modelo en un ambiente biológico. Resultados: Se desarrolló el modelado de la proteína LuxS de P. gingivalis cepa W83, que permite el acercamiento a una estructura que se propone, por la interacción entre la proteína y su ligando natural. El modelo generado con recursos computacionales logró una correcta estructura molecular que aceptó la realización de diversos cálculos. El acoplamiento demostró una cavidad donde se logran diversas posiciones del ligando con buenos resultados. Conclusiones: Se obtuvo un modelo 3D para la proteína LuxS en la P. gingivalis cepa W83 validado por diferentes métodos computacionales con una adecuada reproducibilidad biológica por medio del acoplamiento molecular.


Background: Crystallization is not always achieved for all proteins in a good size and a good quality for X-ray diffraction. So that condition opens a field for the development of theoretical molecular and protein studies allowing the representation of the molecules in 3D, providing spatial information to study the interaction between ligands and macromolecular receptors. Materials and Methods: In silico study from primary sequence analysis of six different proteins LuxS crystallized of several bacteria. 1J6X protein of Helicobacter pylori was selected for its similarity with the LuxS protein sequence in Porphyromonas gingivalis (P. gingivalis) strain W83 to produce a homology model of this protein, using the Sybyl and MOE software. A docking was performed to assess the reproducibility of the model in a biological environment. Results: The LuxS protein modelling of P. gingivalis strain W83 was developed, which allows the approach to a proposed structure for the interaction between the protein and its natural ligand. The model generated with computational resources achieved the correct position and biological behavior by means of developed calculations. The docking showed a cavity in which the ligand adopted several positions with good results. Conclusions: A LuxS protein model was obtained, validated by different methods. This generated a 3D model for LuxS protein in P. gingivalis strain W83 with biological reproducibility by means of molecular docking.


Assuntos
Proteínas de Bactérias , Conformação Molecular , Porphyromonas gingivalis , Homologia Estrutural de Proteína , Liases de Carbono-Enxofre
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