Inhibition of β2-Microglobulin Amyloid Fibril Formation by α2-Macroglobulin
نویسندگان
چکیده
منابع مشابه
The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH
RATIONALE Amyloid formation is implicated in a number of human diseases. β(2)-Microglobulin (β(2)m) is the precursor protein in dialysis-related amyloidosis and it has been shown that partial, or more complete, unfolding is key to amyloid fibril formation in this pathology. Here the relationship between conformational flexibility and β(2)m amyloid formation at physiological pH has been investig...
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Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β2-microglobulin (β2m), associated with dialysis-related amyloidosis (DRA), have been shown to cause disruption of anionic lipid bilayers in vitro. However, the eff...
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The deposition of amyloid-like fibrils, composed primarily of the 99-residue protein β2-microglobulin (β2m), is one of the characteristic symptoms of dialysis-related amyloidosis. Fibrils formed in vitro at low pH and low salt concentration share many properties with the disease related fibrils and have been extensively studied by a number of biochemical and biophysical methods. These fibrils c...
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Bakthisaran RAMAN*†, Tadato BAN†, Miyo SAKAI†, Saloni Y. PASTA*, Tangirala RAMAKRISHNA*, Hironobu NAIKI‡, Yuji GOTO†1 and Ch. Mohan RAO*1 *Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India, †Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Agency, Yamadaoka 3-2, Suita, Osaka 565–0871, Japan, and ‡Faculty of Medical Science, ...
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Understanding the structural heterogeneity inherent in the process of amyloid fibril formation is an important goal of protein aggregation studies. Structural heterogeneity in amyloid fibrils formed by a protein manifests itself in fibrils varying in internal structure and external appearance, and may originate from molecular level variations in the internal structure of the cross-β motif. Amyl...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.167965