نتایج جستجو برای: amyloid beta25 35 folding

تعداد نتایج: 244389  

Journal: :FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1996
J King C Haase-Pettingell A S Robinson M Speed A Mitraki

An unexpected aspect of the expression of cloned genes is the frequent failure of newly synthesized polypeptide chains to reach their native state, accumulating instead as insoluble inclusion bodies. Amyloid deposits represent a related state associated with a variety of human diseases. The critical folding intermediates at the juncture of productive folding and the off-pathway aggregation reac...

Journal: :Applied sciences 2021

Amyloid beta (A?) produced by the amyloidogenic pathway induces neurotoxicity, and its accumulation is a well-known cause of Alzheimer’s disease (AD). In this study, protective effect membrane-free stem cell extract (MFSCE) derived from adipose tissue against A?25–35-induced neurotoxicity in neuronal cells was investigated. Treatment with MFSCE increased viability decreased lactate dehydrogenas...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2002
Johannes H Ippel Anders Olofsson Jürgen Schleucher Erik Lundgren Sybren S Wijmenga

Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible Spongiform Encephalopathies. The molecular structure of amyloid is to a large extent unknown, because of lack of high-resolution structural informat...

2010
Paavo K.J. Kinnunen

Several lines of research have concluded lipid membranes to efficiently induce the formation of amyloid-type fibers by a number of proteins. In brief, membranes, particularly when containing acidic, negatively charged lipids, concentrate cationic peptides/proteins onto their surfaces, into a local low pH milieu. The latter together with the anisotropic low dielectricity environment of the lipid...

2002
Buyong Ma Ruth Nussinov

Previously, we have studied the minimal oligomer size of an aggregate amyloid seed and the mechanism of seed growth with a multilayer -sheet model. Under high temperature simulation conditions, our approach can test the stability of possible amyloid forms. Here, we report our study of oligomers of Alzheimer’s amyloid -peptide (A ) fragments 16–22, 16–35, and 10–35 (abbreviated A 16–22, A 16–35,...

2007
Kristen M. Kulinowski Vicki L. Colvin

Amyloid diseases are a broad class that includes familiar ailments such as type 2 diabetes and Alzheimer’s disease as well as more exotic conditions such as Creutzfeldt-Jakob disease and its animal variant, bovine spongiform encephalopathy or “mad cow” disease. Amyloid diseases are thought to be caused by the formation and deposition in the body’s tissues of highly-ordered, thread-like protein ...

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