Results 11 to 20 of about 13,480 (279)
Functional Mammalian Amyloids and Amyloid-Like Proteins
Life, 2020 Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD ...
Maria S. Rubel +6 more
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Nanophotonics of protein amyloids
Nanophotonics, 2014 Technological breakthroughs in the super-resolution optical imaging techniques have enriched our current understanding of a range of biological systems and biomolecular processes at the nanoscopic spatial resolution.
Bhattacharya Mily, Mukhopadhyay Samrat
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Catalytically Active Amyloids as Future Bionanomaterials
Nanomaterials, 2022 Peptides and proteins can aggregate into highly ordered and structured conformations called amyloids. These supramolecular structures generally have convergent features, such as the formation of intermolecular beta sheets, that lead to fibrillary ...
Rodrigo Diaz-Espinoza
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Gene Regulation of Biofilm-Associated Functional Amyloids
Pathogens, 2021 Biofilms are bacterial communities encased in a rigid yet dynamic extracellular matrix. The sociobiology of bacterial communities within a biofilm is astonishing, with environmental factors playing a crucial role in determining the switch from planktonic
Khushal Khambhati +4 more
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Multifunctional Amyloids in the Biology of Gram-Positive Bacteria
Microorganisms, 2020 Since they were discovered, amyloids have proven to be versatile proteins able to participate in a variety of cellular functions across all kingdoms of life.
Ana Álvarez-Mena +3 more
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Cold Spring Harbor Perspectives in Biology, 2019 When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are usually associated with disease including Alzheimer's. However, amyloid has many useful features.
Otzen, Daniel, Riek, Roland
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Amyloidosis-history and development, emphasis on insulin and prion amyloids
Brain DisordersAmyloidosis is associated with misfolding of protein (normal functional and cellular) into intractable aggregates, commonly known as amyloid fibrils.
Sanjay Kisan Metkar +3 more
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Prions and Amyloids - An Overview [PDF]
, 2011 Prions and Amyloids - An ...
Susan W. Liebman (7274912)
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Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids
Molecules, 2023 To date, most research on amyloid aggregation has focused on describing the structure of amyloids and the kinetics of their formation, while the conformational stability of fibrils remains insufficiently explored.
Natalya Katina +6 more
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Biomedical Papers, 2017 Amyloidosis is a heterogeneous group of diseases characterized by the deposition of amyloid. It is caused by extracellular deposition of insoluble fibrils with beta-pleated sheet configuration. The protein misfolding abnormalities result in amyloid fibrils and may manifest as primary, secondary, or familial amyloidosis.
Lucie Karafiatova, Tomas Pika
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