نتایج جستجو برای: β amyloid aggregation

تعداد نتایج: 265469  

Journal: :Food Chemistry 2021

Fish is one of the eight major foods causing type-I food allergy, and prevalence its allergy increasing in part due to changes consumption habits. One main drivers for these has been processing developments transforming fish muscle into seafood products. Most allergic patients react Ca2+-binding protein β-parvalbumin (β-PV) abundant muscle. Here we have analyzed effect content allergenic proper...

Journal: :Science and Technology of Advanced Materials 2008

Journal: :The American Journal of Pathology 2017

2014
Seifollah Bahramikia

Amyloid aggregation of polypeptides is related to a growing number of pathologic states known as amyloid disorders. In recent years, blocking or reversing amyloid aggregation via the use of small compounds are considered as two useful approaches in hampering the development of these diseases. In this research, we have compared the ability of several manganese-salen derivatives, as synthetic com...

Journal: :Molecular Biology 2021

Abstract Alzheimer’s disease (AD) is a neurodegenerative that inevitably results in dementia and death. Currently, there are no pathogenetically grounded methods for the prevention treatment of AD, all current regimens symptomatic unable to significantly delay development dementia. The accumulation β-amyloid peptide (Aβ), which spontaneous, aggregation-prone, neurotoxic product processing signa...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Cong Liu Minglei Zhao Lin Jiang Pin-Nan Cheng Jiyong Park Michael R Sawaya Anna Pensalfini Dawei Gou Arnold J Berk Charles G Glabe James Nowick David Eisenberg

Although aberrant protein aggregation has been conclusively linked to dozens of devastating amyloid diseases, scientists remain puzzled about the molecular features that render amyloid fibrils or small oligomers toxic. Here, we report a previously unobserved type of amyloid fibril that tests as cytotoxic: one in which the strands of the contributing β-sheets are out of register. In all amyloid ...

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