Sentences with phrase «of fibril»

The reactivity of this monoclonal antibody was not dependent on the V (L) or C (L) isotype of the fibril, but rather seemed to be directed toward a beta - pleated sheet conformational epitope expressed by AL and other amyloid proteins.

Investigations of the fibril specimen by solid - state nuclear magnetic resonance spectroscopy provided additional data to build the model and helped to validate the structure.

Extensive calculations enabled the atomic structure of the fibril to be reconstructed from these measurements.

«If we can manipulate the orientations of fibrils, we can do the same with other linear materials in the future.»

Further immunological examinations show that the investigated form of the fibrils is especially relevant to the illness.

«NMR enabled us to obtain additional information such as which amino acid residues form salt bridges thus enhancing the stability of the fibrils,» explains Prof. Henrike Heise from Heinrich Heine University Düsseldorf and Jülich's Biomolecular NMR Center.

The uptake and degradation of fibrils was analysed by quantitative light - and electron - microscopic immunocytochemistry and immunoreactivity was detectable in 86 + / -3 % cells within 6 h of culture.

This toxicity is mediated by the fibrillar form of the amylin peptide and requires direct contact of the fibrils with the cell surface.

The amyloidolytic response was associated with a pronounced infiltration of the amyloidoma with neutrophils and putatively involved opsonization of fibrils by the antibody, leading to cellular activation and release of proteolytic factors.

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.

«But we were able to find an SOD1 mutation that stabilizes the trimer structure and another mutation that promotes the creation of the larger fibrils at the expense of smaller structures.

But in a study published in the Proceedings of the National Academy of Sciences, scientists at the University of North Carolina at Chapel Hill found evidence that these large SOD1 fibrils protect rather than harm neurons.

«Large aggregates of ALS - causing protein might actually help brain cells: UNC School of Medicine scientists add to evidence that small aggregates of SOD1 protein are the brain - cell killing culprits in ALS, but the formation of larger, more visible, and fibril - like aggregates of the same protein may protect brain cells.»

Left: cells with large, fibril - like aggregates of SOD1 protein.

Chris Dobson, a chemist and structural biologist at the University of Cambridge, U.K., suspected that a much broader range of proteins could form amyloid fibrils in test tubes.

Thus far, each one has proved capable of forming fibrils when heated or immersed in a solution containing acid or a form of alcohol.

This was the first time this technology has been used on amyloid fibrils of the infectious prion, which are a special form of clumped - together proteins that form fibrils.

About 20 proteins share the ability to clump together to form distinctive «amyloid fibrils» that contribute to Alzheimer's, Creutzfeldt - Jakob disease, and a variety of lesser - known disorders.

The 3 - D view of this collagen fibril was created using thermal noise imaging, a technique that's been around since 2001 but technical challenges hindered its development until 2016.

Instead of misfolding the healthy prion protein, PrP, into amyloid fibrils, which have been linked to disease, the team combined the PrP with various blends of lipids — fatty molecules believed to misfold it in the cell.

In all these diseases an important diagnostic feature is the presence of proteinaceous fibrils seen in brain extracts in the electron microscope.

No one knows for certain what the fibrils are — whether they are the agents of the disease, a type of subviral particle, as some researchers suggest, or are a product of the disease.

A number of non-structural screening attempts have been made to identify natural and synthetic compounds that might prevent the aggregation and toxicity of amyloid fibrils.

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.

This A-beta peptide fibril has been rendered in 3 - D by a transmission electron microscope, providing the most detailed look yet at the telltale sign of Alzheimer's disease.

Scientists attribute more than 20 human diseases to the formation of amyloid fibrils.

Such fibrils form plaques, or areas of tissue damage, that researchers can observe with microscopes.

University of Wisconsin - Madison professor Martin Zanni used a sophisticated technique that relies on 2 - D infrared spectroscopy to follow the sequence of events in the chemical reactions leading to fibril formation.

While we still do not know just how Alzheimer's progresses or what role the fibrils play, they are always found in Alzheimer's - ridden brains and are considered diagnostic markers of the disease.

An amyloid fibril is a large structure consisting of misfolded proteins.

«It could be that the fibrils are toxic outside the cells, killing the neurons,» says Nikolaus Grigorieff, head of the Brandeis team that created the image.

In order to demonstrate the versatility of nano - FTIR for nanoscale - resolved protein spectroscopy, the researchers measured infrared spectra of single viruses, ferritin complexes, purple membranes and insulin fibrils.

«They all exhibit variations of their secondary structure — describes Iban Amenabar, who performed the nanospectroscopy experiments -; viruses and ferritin are mainly made of alpha - helical structures, while insulin fibrils are mainly made of beta - sheet structures.»

Simon Poly, the biologist in the team, explains that «in a mixture of insulin fibrils and few viruses, standard FTIR spectroscopy did not reveal the presence of the alpha - helical viruses.

Inhibiting BACE1 will limit the production of Aβ which, in turn, should reduce the production of neurotoxic fibrils and plaques.

More than 40 illnesses known as amyloid diseases — Alzheimer's, Parkinson's and rheumatoid arthritis are a few — are linked to the buildup of proteins after they have transformed from their normally folded, biologically active forms to abnormally folded, grouped deposits called fibrils or plaques.

She says that these findings also have implications for designing treatments for Parkinson's, noting that some drugs currently under development are focused on getting rid of larger fibrils that make up Lewy bodies.

In the current study, Lasmézas and her team looked at cell cultures of neurons that were induced to accumulate fibrils made of misfolded α - synuclein, mimicking Lewy bodies in patients with Parkinson's.

To do so, they engineered a collection of 20 DNA double helices to form a nanotube big enough (15 to 20 nanometers — just over one - billionth of a meter — in diameter) to house the fibrils.

For prevention studies, they injected mouse α - syn synthetic preformed fibrils into wild - type, normal mice, as a control, and then immediately treated the mice with Syn303, one of the MAbs used (or IgG, another type of common antibody, for the control mice).

The platform builds the fibrils by combining the properties of the nanotube with a synthetic peptide fragment that is placed inside the cylinder.

The cell culture experiments showed that MAbs prevented the uptake of misfolded α - syn fibrils by neurons and sharply reduced the recruitment of natural α - syn into new Lewy body aggregates.

The resulting fibril - filled nanotubes can then be organized into two - dimensional structures through a series of DNA - DNA hybridization interactions.

Yet if you look at people who develop the clinical syndrome of dementia, especially later in life, yes, they have amyloid in the brain but they also have other pathologic entities — vascular disease; synucleinopathies [insoluble fibrils of the normally soluble protein, alpha - synuclein]; a tauopathy [which is marked by disease - inducing, insoluble tangles of another protein, tau].

In the past, he said, much research on Alzheimer's and similar disease focused on fibrils, large bundles of misfolded proteins that form in the brain.

We're not worried yet about what happens to the line of cars an hour later — that's the fibril.»

In Alzheimer's disease proteins clump together to long fibrils causing the death of nerve cells.

Fibrils consisting of recMoPrP (89 — 230) were inoculated intracerebrally into transgenic (Tg) mice expressing MoPrP (89 — 231).

But researchers in Italy and the United Kingdom reported in April that many different types of normal proteins — with no known link to diseases — can also fold into shapes indistinguishable from the dreaded amyloid fibrils.

In close collaboration with his TUM colleagues Johannes Buchner, professor of biotechnology and Sevil Weinkauf, professor of electron microscopy, Reif determined that the small heat shock protein uses a specific non-polar beta - sheet structure pile in its center for interactions with the beta - amyloid, allowing it to access the aggregation process in two locations at once: For one it attaches to individual dissolved beta - amyloids, preventing them from forming fibrils.