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Updated: Jul 17, 2026

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Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
Published on: March 7, 2019
[Multifocal localized amyloidosis in a pediatric patient]
N Mesuro Domínguez1, J L Lacosta Nicolás
1Complejo Hospitalario San Millán- San Pedro, Logroño, La Rioja.
Acta Otorrinolaringologica Espanola
|January 19, 2007
Abstract:
Amyloidosis of the upper airway is rare in the pediatric age group. We present a primary amyloidosis in the nasopharynx and nasal cavity in a 14-year-old girl. The symptoms were nasal obstruction and mucoid discharge. The diagnostic was revealed by histologycal analysis obtained from local surgical excision.
Related Concept Videos
Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...