Titlebook: Lipids in Protein Misfolding; Olga Gursky Book 2015 The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer N

amphibian

Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights,ts that are likely to initiate β-aggregation. Mapping such segments on the available atomic structures of apolipoproteins helps explain why some of them readily form amyloid while others do not. Our analysis shows that nearly all amyloidogenic segments: (i) are largely hydrophobic, (ii) are located

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Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth-servers that combine several independent approaches, and by the method PASTA2. Thus, correct prediction of amyloidogenic segments remains a difficult task. Additional data and new algorithms that are becoming available are expected to improve the accuracy of the prediction methods, particularly if

insurgent

Role of Syndecans in Lipid Metabolism and Human Diseases,ptor with its agonist, leading to an increased appetite. Finally, syndecan-4 initiates the capture of modified low-density lipoproteins by macrophages and thereby promotes the atheroma formation. We hypothesize that syndecan modifications such as desulfation of glycosaminoglycan chains may contribut

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男學院

supported ionic liquid catalysis. His results have significantly contributed to the present level of understanding in the field and accordingly he is author and coauthor of ten publications on the topic in hig978-3-319-03345-7978-3-319-00380-1Series ISSN 2190-5053 Series E-ISSN 2190-5061

reflection