Results 11 to 20 of about 36,527 (232)
Molecular Mechanisms of Amylin Turnover, Misfolding and Toxicity in the Pancreas
Amyloidosis is a common pathological event in which proteins self-assemble into misfolded soluble and insoluble molecular forms, oligomers and fibrils that are often toxic to cells.
Diti Chatterjee Bhowmick +3 more
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Systemic aging fuels heart failure: Molecular mechanisms and therapeutic avenues
Systemic aging influences various physiological processes and contributes to structural and functional decline in cardiac tissue. These alterations include an increased incidence of left ventricular hypertrophy, a decline in left ventricular diastolic ...
Zhuyubing Fang +7 more
semanticscholar +2 more sources
Serum amyloid A and protein AA: Molecular mechanisms of a transmissible amyloidosis [PDF]
Systemic AA‐amyloidosis is a complication of chronic inflammatory diseases and the fibril protein AA derives from the acute phase reactant serum AA. AA‐amyloidosis can be induced in mice by an inflammatory challenge. The lag phase before amyloid develops can be dramatically shortened by administration of a small amount of amyloid fibrils.
Westermark, Gunilla T., Westermark, Per
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Exploring the Molecular Pathology of Iatrogenic Amyloidosis
Iatrogenic amyloidosis results from medical therapeutic interventions, leading to the misfolding and aggregation of proteins into amyloid fibrils or to their direct deposition in different tissues.
Bernardo Bonilauri
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Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43
FUS and TDP-43, two RNA-binding proteins from the heterogeneous nuclear ribonucleoprotein family, have gained significant attention in the field of neurodegenerative diseases due to their association with amyotrophic lateral sclerosis (ALS) and frontotemporal degeneration (FTD).
Jianxing Song
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Hereditary transthyretin (ATTRv) amyloidosis is a severe, progressive, and heterogeneous multisystemic condition due to mutations in the TTR gene. Although multiple aspects of its molecular pathophysiological mechanisms have been elucidated over the ...
Marco Luigetti +10 more
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Current and New Perspectives on the Molecular and Cellular Mechanisms of Amyloid Formation and Toxicity in Light Chain Amyloidosis [PDF]
Light chain (AL) amyloidosis is a protein misfolding disease characterized by the abnormal proliferation of monoclonal plasma cells that secrete free immunoglobulin light chains (LC) into circulation. These LCs misfold and aggregate as amyloid fibrils in vital organs.
DiCostanzo, Ara Celi +1 more
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Herein, immunoglobulin light chains (LCs) native state was studied in the context of the pathology known as light chain amyloidosis (AL). This pathology is characterized by LCs overexpression, which leads to toxicity and aggregation into amyloid fibrils in target organs, with heart being the most affected one.
S. Ricagno, Oberti Luca
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Protein aggregation drives proteinopathies ranging from ALS to systemic amyloidosis, yet the multiscale determinants bridging sequence, structure, and kinetics remain elusive.
Wei Xuan Wilson Loo +7 more
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Background Alzheimer’s disease (AD) is characterized by progressive amyloid beta (Aβ) deposition in the brain, with eventual widespread neurodegeneration.
Stefan Wendt +18 more
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