Results 11 to 20 of about 547,277 (291)
Structural Studies of Cystatin B Amyloid Fibre and Oligomer [PDF]
, 2013 Amyloid fibres are characteristic of over 25 degenerative human diseases including Alzheimer’s and Parkinson’s disease. Amyloid fibres are insoluble, highly stable, ordered cross-β sheet structures, which form as a result of conformational change and ...
Davis, Peter J.
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Alzheimer's Disease Beyond Amyloid: Lessons From Atherosclerosis. [PDF]
Ann Clin Transl NeurolAnnals of Clinical and Translational Neurology, EarlyView.
Ciaccio M, Agnello L.
europepmc +2 more sources
Applied Biochemistry and Biotechnology, 2012 The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease.
Pulawski W +3 more
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AmyloGraph: a comprehensive database of amyloid–amyloid interactions
Nucleic Acids Research, 2022 Abstract Information about the impact of interactions between amyloid proteins on their fibrillization propensity is scattered among many experimental articles and presented in unstructured form. We manually curated information located in almost 200 publications (selected out of 562 initially considered), obtaining details of 883 ...
Michal Burdukiewicz +14 more
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Zinc metalloproteinases and amyloid Beta-Peptide metabolism : the positive side of proteolysis in Alzheimer's disease [PDF]
, 2011 Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (Aβ-)peptides in the brain causing progressive neuronal death.
Gough, Mallory +5 more
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Cerebrospinal Fluid Over Plasma Links Analytes to Cognitive Decline in Older Adults at Risk for Alzheimer's Disease. [PDF]
Ann Clin Transl NeurolABSTRACT Objective To identify inflammatory analytes in cerebrospinal fluid (CSF) and plasma associated with cognitive decline in cognitively normal (CN) older adults at risk for Alzheimer's disease (AD). Methods In a longitudinal study of 118 CN older adults (65–80 years, 54% APOE ε4, 26% preclinical AD), 1331 CSF and 1501 plasma analytes were ...
Pillai JA +13 more
europepmc +2 more sources
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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Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters [PDF]
, 2010 Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is therefore
Xue, Wei-Feng +3 more
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Microbial amyloids in neurodegenerative amyloid diseases
The FEBS Journal, 2023 Human‐disease associated amyloidogenic proteins are not unique in their ability to form amyloid fibrillar structures. Numerous microbes produce amyloidogenic proteins that have distinct functions for their physiology in their amyloid form, rather than solely detrimental. Emerging data indicate associations between various microbial organisms, including
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The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer. [PDF]
Mol OncolMutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Abad L, Tosatto SCE, Leonardi E.
europepmc +2 more sources