Results 181 to 190 of about 69,622 (226)

Charged membrane interfaces reshape the nucleation landscape of RIPK3 amyloid variants. [PDF]

Eur Biophys J
Escobedo-González FC, Gelardo A, Titaux-Delgado GA, Mompeán M.   +3 more
europepmc   +1 more source

A machine learning protocol for predicting structural distributions of amyloid-forming proteins from 2D IR spectra. [PDF]

Proc Natl Acad Sci U S A
Ye S, Wang B, Li Z, Zhu L, Yin Sun C, Mukamel S, Jiang J.   +6 more
europepmc   +1 more source

Amyloid Beta in Alzheimer's Disease: Mechanisms, Biomarker Potential, and Therapeutic Targets. [PDF]

CNS Neurosci Ther
Ahmadi S, Khaledi S, Ahmadi K, Hassanzadeh K.   +3 more
europepmc   +1 more source

Primary (AL) Amyloidosis Following COVID-19 Infection: A Case Report. [PDF]

Clin Case Rep
Gholami N, Tahsini Tekantapeh S, Khalaji A, Nejati B, Ravaei G.   +4 more
europepmc   +1 more source

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Porelike Morphologies in Amyloidogenic Proteins

2021
Intrinsically disordered proteins (IDPs) have been linked to a variety of human diseases. The roles that IDPs play in physiological functions and disease pathology are frequently an enigma. Their disordered nature and structural complexity presents significant experimental and computational challenges, and makes IDPs difficult to study and characterize
Matthew J. Voelker, Brigita Urbanc
openaire   +1 more source

Interactions of Amyloidogenic Proteins

NeuroMolecular Medicine, 2003
The various protein deposits of brain amyloidosis share common ultrastructural, biophysical, and histological properties. These amyloidogenic deposits can be composed of distinct proteins, which are conceptually associated with different neurodegenerative diseases.
Benoit I, Giasson, Virginia M-Y, Lee, John Q, Trojanowski   +2 more
openaire   +2 more sources

Novel approaches for studying amyloidogenic peptides/proteins

Current Opinion in Pharmacology, 2013
A growing number of important human diseases are associated with the aggregation and deposition of incorrectly folded proteins in the form of highly structured amyloid fibrils. The aggregation process involves the formation of intermediate oligomeric assemblies with toxic properties.
Marten, Beeg, Luisa, Diomede, Matteo, Stravalaci, Mario, Salmona, Marco, Gobbi   +4 more
openaire   +2 more sources

Amyloidogenic metal-binding proteins: new investigative pathways

Biochemical Society Transactions, 2008
Neurodegenerative diseases remain perplexing and problematic for modern research. Those associated with amyloidogenic proteins have often been lumped together simply because those proteins aggregate. However, research has identified a more logical reason to group some of these diseases together. The associated proteins not only aggregate, but also bind
Paul, Davies, Sarah N, Fontaine, Dima, Moualla, Xiaoyan, Wang, Josephine A, Wright, David R, Brown   +5 more
openaire   +2 more sources