Results 251 to 260 of about 18,838 (278)
Fatty acids alter to the toxicity of islet amyloid polypeptide aggregates in a length and saturation dependent manner. [PDF]
iScienceSitton J +4 more
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Molecular mechanisms of gut microbiota dysbiosis and metabolites in Alzheimer's disease pathogenesis: implications for precision therapeutics. [PDF]
Mol BrainVaziri Y +3 more
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Physics of Protein Aggregation in Normal and Accelerated Brain Aging. [PDF]
BioessaysEspay AJ +9 more
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Cathepsin B prevents cell death by fragmentation and destruction of pathological amyloid fibrils. [PDF]
Cell Death DiscovSulatsky MI +4 more
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Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development. [PDF]
Matrix Biolde Sousa ET +4 more
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Heart, Lung and Circulation, 2020
Amyloid cardiomyopathy is emerging as an important and under-recognised cause of heart failure and cardiac arrhythmias, especially in older adults. This disorder is characterised by extracellular deposition of amyloid fibrils that form due to misfolding of secreted light chains (AL) or transthyretin protein (ATTR). In ATTR, amyloid aggregates typically
Nicole K. Bart +5 more
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Amyloid cardiomyopathy is emerging as an important and under-recognised cause of heart failure and cardiac arrhythmias, especially in older adults. This disorder is characterised by extracellular deposition of amyloid fibrils that form due to misfolding of secreted light chains (AL) or transthyretin protein (ATTR). In ATTR, amyloid aggregates typically
Nicole K. Bart +5 more
openaire +5 more sources
Essays in Biochemistry, 2014
Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures,
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Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures,
openaire +2 more sources
Diseases of the Colon & Rectum, 1982
Amyloidosis not infrequently involves the gastrointestinal tract and may result in a variety of symptoms, including those related to impaired motility, malabsorption, and ulceration due to ischemia. This report describes the case of a 74-year-old man with systemic amyloidosis secondary to multiple myeloma, with striking gross morphologic findings ...
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Amyloidosis not infrequently involves the gastrointestinal tract and may result in a variety of symptoms, including those related to impaired motility, malabsorption, and ulceration due to ischemia. This report describes the case of a 74-year-old man with systemic amyloidosis secondary to multiple myeloma, with striking gross morphologic findings ...
openaire +2 more sources