Sentences with phrase «aggregates of amyloid proteins»

Not exact matches

Co-lead researcher, Australian National University Professor John Carver, said that two unrelated proteins aggregate in UHT milk over a period of months to form clusters called amyloid fibrils, which cause the milk to transform from a liquid into a gel.

While these compounds did not reduce the amount of protein aggregates, they were found to reduce the protein's toxicity and to increase the stability of amyloid fibrils — a finding that lends further evidence to the theory that smaller assemblies of amyloid - beta known as oligomers, and not the fibrils themselves, are the toxic agents responsible for Alzheimer's symptoms.

A protein fragment called amyloid - beta (Aβ) is known to aggregate and create plaque in the brains of Alzheimer's patients.

Previously, researchers have shown that treating cells with neuregulin - 1, for example, dampens levels of amyloid precursor protein, a molecule that generates amyloid beta, which aggregate and form plaques in the brains of Alzheimer's patients.

«These findings suggest that the ability of proteins to aggregate into amyloid fibrils can be considered a more general property of proteins than previously believed,» says Massimo Stefani, a protein chemist at the University of Florence in Italy who co-led the project.

In the brains of patients with Alzheimer's disease (AD), amyloid precursor protein is broken apart, and the resulting fragments — β - amyloid peptides, or Aβ peptides — aggregate to form plaques.

In persons with the disease, the formation of amyloid plaque aggregates, a process known to cause the onset of Alzheimer's disease, prevents the Crtc1 protein from functioning correctly.

The results obtained in the experiments with immunodepletion, administration of pure, synthetic IAPP aggregates prepared in vitro, and aggregates of other disease - associated (Tau implicated in Alzheimer's disease) and nondisease — associated proteins (Mcc, a bacterial amyloid) clearly indicate that the active principle behind the pathologic transmission are the IAPP aggregates themselves.

These results indicated that, under our experimental conditions, other amyloidogenic proteins do not induce significant accumulation of IAPP compared with amyloid aggregates composed of IAPP.

(A) Isolated islets from 3 - wk - old, female, Tg - hIAPP mice were cultured in presence of different concentrations of IAPP aggregates prepared in vitro from synthetic IAPP, as well as controls treated with other amyloidogenic proteins, including the Alzheimer's disease — associated protein Tau (the K18 fragment) and the bacterial amyloid Mcc.

To test the specificity of the effect, we also treated islets with aggregates coming from other disease - associated and functional amyloid proteins.

For that purpose, we used aggregates of the Tau protein, implicated in Alzheimer's disease, as well as the bacterial amyloid protein microcin (Mcc).

Specifically, that aggregates of A-beta peptides, which are formed following cleavage of the Amyloid Precursor Protein (APP), instigate a series of events that leads to neurodegeneration and, eventually, AD.

Total crosslinks, total protein carbonyls, total AGEs, total amyloid, aggregate, adducts, mtDNA oxidative lesions, total lipofuscin, total oxidized redox disulfides, total lipid peroxidation chain propagation by aldehydes and propagators (MDA Malondialdehyde / TBARS, 4 - HNE, Acrolein), total giant senescent mitochondria and a crap load of others.

Proclara has developed a pipeline of drug candidates that use GAIM to target the common amyloid protein conformation, dissociating and preventing the formation of misfolded protein assemblies, and blocking the cell - to - cell transmission of toxic aggregates.

Therapies applying this paradigm to clear β - amyloid protein (Aβ) plaques and soluble aggregates from patients with Alzheimer's disease (AD) is an extremely active field of research, with multiple active and passive Aβ vaccines currently in human clinical trials.

Proclara's approach is based on established knowledge that several toxic misfolded protein aggregates, including Aβ, tau and a-synuclein, share a common amyloid fold and the proprietary discovery of a protein motif that recognizes this common feature.

Four of the mAbs, 2T5C9, 2G9C, T1F11, and TB2H7, demonstrated diagnostic potential in enzyme - linked immunosorbent assays (ELISA) by their low to sub-nanomolar cross-reactivity with recombinant wild - type (WT) and mutant TTR aggregates and lack of binding to native TTR or amyloid fibrils formed by other peptides or proteins.

Unlike canonical prions, most of the proteins lack some conventional prion characteristics, including the formation of large aggregates of similarly folded proteins, called amyloids.

The brains of individuals having Alzheimer's have clumps of amyloid plaques which are made up of aggregates of misfolded proteins.