Results 51 to 60 of about 14,195 (294)
Amyloids are non-branching fibrils that are composed of stacked monomers stabilized by intermolecular β-sheets. Some amyloids are associated with incurable diseases, whereas others, functional amyloids, regulate different vital processes.
A.V. Sergeeva +6 more
doaj +1 more source
Pathological self-assembly is a concept that is classically associated with amyloids, such as amyloid-β (Aβ) in Alzheimer's disease and α-synuclein in Parkinson's disease.
Ernest Y. Lee +8 more
doaj +1 more source
Searching for novel functional amyloids in biofilms [PDF]
The identification of novel amyloids is key to understand the many roles of amyloids in biofilm structure and function. Unfortunately, isolation of amyloids is a challenging and not always successful process.
Hove Hansen, Susan +4 more
core +2 more sources
What can AlphaFold do for antimicrobial amyloids?
Amyloids, protein, and peptide assemblies in various organisms are crucial in physiological and pathological processes. Their intricate structures, however, present significant challenges, limiting our understanding of their functions, regulatory ...
Ragonis-Bachar, Peleg +5 more
core +1 more source
Leucine‐rich glioma inactivated 1 (LGI1) is a ganglioside‐binding protein
Neuronal hyperexcitability associated with a decrease/absence of the extracellular protein LGI1 has been suggested to be primarily due to the downregulation of Kv1 channel expression. The molecular mechanisms underlying this decrease have not yet been elucidated.
Kévin Debreux +7 more
wiley +1 more source
A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein
Reversible and irreversible amyloids are two diverging cases of protein (mis)folding associated with the cross-β motif in the protein folding and aggregation energy landscape.
Lukas Frey +13 more
doaj +1 more source
“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine
Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans.
Sherin Abdelrahman +5 more
doaj +1 more source
Smaller is better: nanobodies meet NMR
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley +1 more source
Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage
Despite the current diagnostic and therapeutic approaches to bladder cancer being widely accepted, there have been few significant advancements in this field over the past decades.
Diego Alem +13 more
doaj +1 more source
Functional Amyloids Used by Organisms::A Lesson in Controlling Assembly
Amyloid has been studied primarily in relation to the disease states that it causes in humans, but in recent years, a range of proteins have been identified that self-assemble to a β-sheet rich fold as part of their native function and as such have been ...
SCHEIBEL, T +3 more
core +1 more source

