Structural diversity and polymorphism in amyloid fibrils from single organs and single patients with AL amyloidosis [PDF]
Structural DynamicsAmyloidogenic light chain (AL) amyloidosis is a complicated disease that results from aggregation of antibody light chain proteins into amyloid fibrils, that then disrupt organ function.
Parker T Bassett +4 more
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Amyloid Fibrils from Hemoglobin [PDF]
Biomolecules, 2017 Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and ...
Nadishka Jayawardena +7 more
doaj +3 more sources
Thermodynamics of beta-amyloid fibril formation [PDF]
The Journal of Chemical Physics, 2004 Amyloid fibers are aggregates of proteins. They are built out of a peptide called $\beta$--amyloid (A$\beta$) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the Amyloid Precursor ...
F. Simona +4 more
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Cathepsin B prevents cell death by fragmentation and destruction of pathological amyloid fibrils [PDF]
Cell Death DiscoveryAmyloid fibrils cause organ and tissue dysfunction in numerous severe diseases. Despite the prevalence and severity of amyloidoses, there is still no effective and safe anti-amyloid therapy.
Maksim I. Sulatsky +4 more
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Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain
Molecules, 2022 Amyloid fibrils have been an important subject as they are involved in the development of many amyloidoses and neurodegenerative diseases. The formation of amyloid fibrils is typically initiated by nucleation, whereas its exact mechanisms are largely ...
Yuki Yoshikawa +10 more
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Endocytosed 2-Microglobulin Amyloid Fibrils Induce Necrosis and Apoptosis of Rabbit Synovial Fibroblasts by Disrupting Endosomal/Lysosomal Membranes: A Novel Mechanism on the Cytotoxicity of Amyloid Fibrils. [PDF]
PLoS ONE, 2015 Dialysis-related amyloidosis is a major complication in long-term hemodialysis patients. In dialysis-related amyloidosis, β2-microglobulin (β2-m) amyloid fibrils deposit in the osteoarticular tissue, leading to carpal tunnel syndrome and destructive ...
Tadakazu Okoshi +4 more
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AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications, 2021 Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed ...
Akanksha Bansal +8 more
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Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets
Biomolecules, 2023 The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases.
Kanchana Karunarathne +7 more
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Amyloid Fibril Solubility [PDF]
The Journal of Physical Chemistry B, 2015 It is well established that amyloid fibril solubility is protein specific, but how solubility depends on the interactions between the fibril building blocks is not clear. Here we use a simple protein model and perform Monte Carlo simulations to directly measure the solubility of amyloid fibrils as a function of the interaction between the fibril ...
Rizzi, LG, Auer, S
openaire +4 more sources
Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation
AMB Express, 2021 Amyloid fibrils are important scaffold in bacterial biofilms. Streptococcus mutans is an established cariogenic bacteria dwelling within biofilms, and C123 segment of P1 protein is known to form amyloid fibrils in S.
Yuanyuan Chen +4 more
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