Results 241 to 250 of about 75,180 (286)

Perilipin 4 repetitive region forms amyloid fibrils promoted by a genetic expansion found in myopathy patients

Choufani C, Fuggetta N, Moulin C, Sabbagh B, Franckhauser C, Lyonnais S, Arteni A, Rouquier S, Perme T, Pagnotta S, Ruggieri A, Bousset L, Čopič A.   +12 more
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Amyloid fibrils in urine.

The Western journal of medicine, 1978
M E, Titford, B S, Bull
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Amyloid fibril proteins

Mechanisms of Ageing and Development, 2002
Amyloidosis refers to a group of protein folding diseases. Various innocuous and soluble proteins in physiological conditions polymerize to insoluble amyloid fibrils in several serious diseases, including Alzheimer's disease (AD) and prion diseases. In addition, senile amyloidosis is a form of amyloidosis in which the incidence and severity of amyloid ...
Yanming, Xing, Keiichi, Higuchi
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Structures for amyloid fibrils

The FEBS Journal, 2005
Alzheimer's disease and Creutzfeldt–Jakob disease are the best‐known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the ...
O Sumner, Makin, Louise C, Serpell
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Modeling amyloid fibril formation

Biochemistry (Moscow), 2011
No detailed step-by-step model of protein rearrangements during amyloid structure formation has been presented in the literature. The aim of this work was to design a kinetic model for description of the amyloid formation process on the basis of the most recent experimental data.
N V, Dovidchenko, O V, Galzitskaya
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Amyloid fibril protein in familial amyloid polyneuropathy

Neurology, 1981
Amyloid fibril protein was purified from organs of patients with familial amyloid polyneuropathy (Nagano prefecture, Japan). When compared with amyloid fibril protein from primary amyloidosis and secondary amyloidosis, the protein from familial amyloid polyneuropathy was shown to differ in the molecular weight of the subunit.
S, Shoji, A, Okano
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Aprotinin binding to amyloid fibrils

European Journal of Biochemistry, 2000
Different low molecular mass ligands have been used to identify amyloid deposits. Among these markers, the dyes Thioflavin T and Congo Red interact specifically with the β‐sheet structure arranged in a cross‐β conformation, which is characteristic of amyloid. However, the molecular details of this interaction remain unknown.
I, Cardoso, P J, Pereira, A M, Damas, M J, Saraiva   +3 more
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Mechanisms of amyloid fibril formation

Biochemistry (Moscow), 2014
Amyloid and amyloid-like aggregates are elongated unbranched fibrils consisting of β-structures of separate monomers positioned perpendicular to the fibril axis and stacked strictly above each other. In their physicochemical properties, amyloid fibrils are reminiscent of synthetic polymers rather than usual proteins because they are stable to the ...
N V, Dovidchenko, E I, Leonova, O V, Galzitskaya   +2 more
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Hybrid bioinorganic insulin amyloid fibrils

Chemical Communications, 2010
Herein we report a method to functionalize in vitro grown insulin amyloid fibrils with various inorganic materials. The counterion of the positively charged amyloid fibril is exchanged with anions from various salts; subsequent addition of appropriate cations results in functionalization of the amyloid fibril.
Qun, Tang, Niclas, Solin, Jun, Lu, Olle, Inganäs   +3 more
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