نتایج جستجو برای: amyloid fibrils

تعداد نتایج: 41968  

ژورنال: یافته 2020

Background: Recently, there has been growing efforts to elucidate the molecular mechanism of amyloid formation and investigating effective compounds for inhibiting of amyloid structures. Investigation of the fibrillation process through its induction and inhibition using specific compounds such as aromatic derivatives provide useful information for stabilizing the protein structure. In the pres...

Journal: :international journal of advanced biological and biomedical research 2013
hamid reza guodarzi mohammad agha mohammadi mohsen mousavi1

amyloid-β (aβ) self-assembly into cross-β amyloidfibrils is implicated in a causative role in alzheimer’s disease pathology.uncertainties persist regarding the mechanisms of amyloid self assembly and the role of metastable prefibrillar aggregates. aβ fibrilsfeature a sheet-turn-sheet motif in the constituent β-strands; as such, turn nucleation has been proposed as a rate-limiting step in the se...

Journal: :modares journal of medical sciences: pathobiology 2009
majid sadeghizadeh

objective: to study the mechanisms involved in amyloid formation processes, we made a mammalian cell culture model of amylin aggregation and characterized its properties. materials and methods: amyloid fibrils were extracted from cho cells and binding affinity to thioflavin t and congo red was investigated. then the apple-green birefringence of extracted fibrils was detected under polarized li...

Journal: :The Journal of biological chemistry 2011
Daisaku Ozawa Yuichi Kaji Hisashi Yagi Kazumasa Sakurai Toru Kawakami Hironobu Naiki Yuji Goto

Mutations in keratoepithelin are associated with blinding ocular diseases, including lattice corneal dystrophy type 1 and granular corneal dystrophy type 2. These diseases are characterized by deposits of amyloid fibrils and/or granular non-amyloid aggregates in the cornea. Removing the deposits in the cornea is important for treatment. Previously, we reported the destruction of amyloid fibrils...

Journal: :journal of reports in pharmaceutical sciences 0
reza khodarahmi zahra hossein-pour kamran mansouri seyyed abolghasem ghadami

the aberrant assembly of proteins into fibrillar aggregates is accused to be the primary cause of pathogenesis of neurodegenerative diseases. but the structural determinants of protein fibrils that are responsible for cell dysfunction are not yet clear. in the current study, cell culture, spectroscopic techniques as well as theoretical and structural investigations were used to determine the ab...

Journal: :Prion 2008

Journal: :Protein science : a publication of the Protein Society 2012
Lukasz Skora Markus Zweckstetter

Amyloid fibrils are the pathological hallmark of a large variety of neurodegenerative disorders. The structural characterization of amyloid fibrils, however, is challenging due to their non-crystalline, heterogeneous, and often dynamic nature. Thus, the structure of amyloid fibrils of many proteins is still unknown. We here show that the structure calculation program CS-Rosetta can be used to o...

2015
Tadakazu Okoshi Itaru Yamaguchi Daisaku Ozawa Kazuhiro Hasegawa Hironobu Naiki Reza Khodarahmi

Dialysis-related amyloidosis is a major complication in long-term hemodialysis patients. In dialysis-related amyloidosis, β2-microglobulin (β2-m) amyloid fibrils deposit in the osteoarticular tissue, leading to carpal tunnel syndrome and destructive arthropathy with cystic bone lesions, but the mechanism by which these amyloid fibrils destruct bone and joint tissue is not fully understood. In t...

2014
Erin R. Greiner Jeffery W. Kelly Fernando L. Palhano

Amyloid fibrils are associated with many maladies, including Alzheimer's disease (AD). The isolation of amyloids from natural materials is very challenging because the extreme structural stability of amyloid fibrils makes it difficult to apply conventional protein science protocols to their purification. A protocol to isolate and detect amyloids is desired for the diagnosis of amyloid diseases ...

Journal: :Annals of the rheumatic diseases 1989
J H Magnus G Husby S O Kolset

Previous studies have strongly suggested an association between glycosaminoglycans and tissue deposits of amyloid. The present study was aimed at studying this association in purified preparations of hepatic amyloid fibrils obtained from human AA type secondary amyloidosis. Glycosaminoglycans were isolated by gradient ion exchange chromatography of purified amyloid fibrils treated with pronase....

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