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Sayfa 1 itibaren 335 Sonuçlar

Marginal zone B-cell lymphoma of minor salivary gland representing tumor-forming amyloidosis of the oral cavity. A case report.

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We report here a case of mucosa-associated lymphoid tissue (MALT)-type lymphoma arising from the minor salivary gland of the oral cavity exhibiting tumor-forming amyloidosis. The patient was a 64-year-old Japanese woman who presented with 4-year history of a left soft palate mass. Despite multiple

Immunohistochemical study of cytokeratins in amyloid deposits associated with squamous cell carcinoma and dysplasia in the oral cavity, pharynx and larynx.

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The frequency of amyloid deposits associated with squamous cell carcinoma (SCC) and dysplasia in the oral cavity, pharynx and larynx was examined. In addition, the origin of amyloid proteins by immunohistochemical staining with a panel of anticytokeratin monoclonal antibodies was investigated.

Hydration, cavities and volume in protein folding, aggregation and amyloid assembly.

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Differential hydration dictates various biological processes, including protein folding, ligand binding, macromolecular assembly, enzyme kinetics and signal transduction. If water is partially or totally removed (experimentally or in silico), the outcome of these processes can be significantly

[An unusual case of generalized amyloidosis with localizations in the oral cavity].

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After a brief examination of the most modern conceptions relating to amyloidosis desease a case of sistemic amyloidosis localized in the oral cavity is presented by the authors. An iconografic series of the lesions affecting the mucous membrane of the lips, checks and tongue is meant to contribute

Bullous amyloidosis of the oral cavity: a rare clinical presentation and review.

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Bullous amyloidosis (BA) is a rare cutaneous manifestation primarily of systemic amyloidosis, a disease in which abnormal proteinaceous material is formed and deposited in response to inflammatory conditions and plasma cell dyscrasias. Hemorrhagic bullae indicative of BA are usually associated with

Amyloidosis of the oral cavity: report of five cases.

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Five cases of amyloidosis involving structures in the oral cavity are reported. Three cases appeared to be secondary systemic amyloidosis, one case was the systemic form associated with multiple myeloma, and one case appeared to represent nodular or localized amyloidosis. All cases appeared in

Amyloidosis concurrently involving the sinonasal cavities and larynx.

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Localized amyloidosis is an uncommon benign disorder. The purpose of this report is to present the case of a 21-year-old man who had localized amyloidosis simultaneously involving the sinonasal cavities and the larynx. The rarer sinonasal lesion demonstrated CT findings of adjacent "fluffy" bone

β-Amyloid peptide (1-40) in the brain reaches the nasal cavity via a non-blood pathway.

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We examined the distribution patterns of human β-amyloid (1-40) peptide labeled with iodine 125 ((125)I-Aβ40) after injections into the cerebral ventricle or tail vein of rats. In rats receiving an intravenous injection, the radioactive concentration of (125)I-Aβ40 in the nasal area was similar to

Amyloid deposition in the oral cavity: a retrospective study and review of the literature.

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OBJECTIVE A retrospective study was conducted to investigate the anatomic location and characteristics of amyloid deposition in the oral cavity. METHODS Seventeen biopsy specimens that were conclusive for a diagnosis of amyloidosis were assessed in terms of their anatomic location and

Reduced left atrial myocardial deformation irrespective of cavity size: a potential cause for atrial arrhythmia in hereditary transthyretin amyloidosis.

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BACKGROUND Cardiac amyloidosis (CA) is a myocardial disease and commonly under-diagnosed condition. In CA patients, atrial fibrillation might occur in the absence of left atrial (LA) enlargement. OBJECTIVE The aim of this study is to assess LA size and function, and its relationship with atrial

Dihydrochalcone molecules destabilize Alzheimer's amyloid-β protofibrils through binding to the protofibril cavity.

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Alzheimer's disease (AD) is associated with the aggregation of amyloid-β (Aβ) peptides into toxic fibrillar aggregates. Finding effective inhibitors of Aβ aggregation is a crucial step for the development of drugs against AD. Recent experiments reported that dihydrochalcone (Dih), a compound

[Amyloidosis diagnosed from changes in the oral cavity mucosa].

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A patient with lesions of the oral mucosa is presented. Biopsy of the lesions showed deposits of amyloid, which lead to further examination of the patient, revealing a generalized amyloidosis.

[Localized Amyloidosis Involving the Nasal Cavity].

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BACKGROUND Amyloidosis is a disease characterized by deposits of abnormal protein known as amyloid in various organs and tissues. It can be classified into systemic or localized forms, the latter of which is less frequent. Deposition of amyloidogenic monoclonal light chains leads to the most common

The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions.

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Elucidating the structure of Aβ(1-40) fibrils is of interest in Alzheimer's disease research because it is required for designing therapeutics that target Aβ(1-40) fibril formation at an early stage of the disease. M35 is a crucial residue because of its potential oxidation and its strong

Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils.

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The misfolding and self-assembly of human islet amyloid polypeptide (hIAPP or amylin) into amyloid fibrils is pathologically linked to type II diabetes. The polymorphic nature of both hIAPP oligomers and fibrils has been implicated for the molecular origin of hIAPP toxicity to islet β-cells, but

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