Results 301 to 310 of about 288,605 (343)

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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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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Nucleation and Growth of Amyloid Fibrils

The Journal of Physical Chemistry B, 2023
The formation of amyloid fibrils is a complex phenomenon that remains poorly understood at the atomic scale. Herein, we perform extended unbiased all-atom simulations in explicit solvent of a short amphipathic peptide to shed light on the three mechanisms accounting for fibril formation, namely, nucleation via primary and secondary mechanisms, and ...
Sharareh Jalali, Ruoyao Zhang, Mikko P. Haataja, Cristiano L. Dias   +3 more
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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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Review: History of the Amyloid Fibril

Journal of Structural Biology, 2000
Rudolph Virchow, in 1854, introduced and popularized the term amyloid to denote a macroscopic tissue abnormality that exhibited a positive iodine staining reaction. Subsequent light microscopic studies with polarizing optics demonstrated the inherent birefringence of amyloid deposits, a property that increased intensely after staining with Congo red ...
J D, Sipe, A S, Cohen
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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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The Purification of Amyloid Fibril Proteins

Preparative Biochemistry, 1972
Abstract Amyloid fibril concentrates have been fractionated and shown to have homogeneous fragments of the variable region of immunoglobulin proteins as their major protein constituent. Amyloid fibril protein purification was performed on ten amyloid preparations by sequential gel filtration on Sepharose 4 B and Sephadex G-100 columns equilibrated with
G G, Glenner, M, Harada, C, Isersky
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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 Oligomers, Protofibrils and Fibrils

2019
Amyloid diseases are of major concern all over the world due to a number of factors including: (i) aging population, (ii) increasing life span and (iii) lack of effective pharmacotherapy options. The past decade has seen intense research in discovering disease-modifying multi-targeting small molecules as therapeutic options.
Mohammad Khursheed, Siddiqi, Nabeela, Majid, Sadia, Malik, Parvez, Alam, Rizwan Hasan, Khan   +4 more
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