Understanding the complex mechanisms of β2-microglobulin amyloid assembly
نویسندگان
چکیده
منابع مشابه
Understanding the complex mechanisms of β2-microglobulin amyloid assembly
Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have indicated that non-native proteins are responsible for initiating aggregation in vitro and in vivo. Despite the importance of these species for understanding amyloid disease, the structural and dynamic features of amyloido...
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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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Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is kn...
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OBJECTIVE: To determine β2-microglobulin levels in amniotic fluid during the course of second trimester. STUDY DESIGN: One hundred patient’s amniotic fluid β2-microglobulin levels had been evaluated retrospectively (March-October 2009). The most common amniocentesis indication was advanced maternal age (33.3%). Others were; high risk result for triple test (18.5%), high risk result for double t...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2011
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2011.08186.x