| 词汇 | amyloid |
| 释义 | amyloid noun[ U ] medical specializeduk /ˈæm.ɪ.lɔɪd/ us /ˈæm.ɪ.lɔɪd/ a protein that collects in some of the body's tissues and organs, as a feature of some diseases 淀粉状蛋白 Substances & structures in the body abductor accessorius ACL actin adductor funiculus fusiform glomerular glomerulus GnRH navicular neuroendocrine neurohormonal neurohormone nociceptive tendinous tendinum tendo tensor Th You can also find related words, phrases, and synonyms in the topics: Medical treatment: symptoms & diagnosis of medical problems Examples of amyloidamyloid Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Although the b-helix is a plausible structural motif for amyloid fibrils, it has not yet been proven that bona fide b-helices occur in amyloid fibrils. Detailed structural information has been difficult to obtain by conventional techniques because of the inherent non-crystalline and insoluble nature of amyloid fibrils. These models were antiparallel b-helices, presumably because the more common occurrence of parallel b-sheets in amyloid fibrils had not yet been established. Xray analysis suggests that a protofilament in this amyloid is composed of a single pair of -sheets in the normal cross- conformation. This latter reflection, of course, can only occur if the amyloid fibrils, or protofilaments, are composed of two or more -sheets. Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. Thus, there are no absolutely universal molecular structural features in amyloid fibrils, apart from the cross-b motif. The larger number of equatorial reflections reflect the presence of protofilaments in amyloid fibrils. Once formed, amyloid structures are not dependent on the presence of mobile water and are not significantly distorted when mobile water is removed by lyophilization. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. This review will focus on in vitro studies aimed at the characterization of an intermediate on the amyloid pathway as one potential toxic species. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. These examples are from corpora and from sources on the web. Any opinions in the examples do not represent the opinion of the Cambridge Dictionary editors or of Cambridge University Press or its licensors. |
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