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- W2594823992 endingPage "549" @default.
- W2594823992 startingPage "549" @default.
- W2594823992 abstract "Here we discuss studies of the structure, folding, oligomerization and amyloid fibril formation of several proline mutants of human stefin B, which is a protein inhibitor of lysosomal cysteine cathepsins and a member of the cystatin family. The structurally important prolines in stefin B are responsible for the slow folding phases and facilitate domain swapping (Pro 74) and loop swapping (Pro 79). Moreover, our findings are compared to β2-microglobulin, a protein involved in dialysis-related amyloidosis. The assessment of the contribution of proline residues to the process of amyloid fibril formation may shed new light on the critical molecular events involved in conformational disorders." @default.
- W2594823992 created "2017-03-16" @default.
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- W2594823992 creator A5060301823 @default.
- W2594823992 creator A5064969865 @default.
- W2594823992 creator A5079634789 @default.
- W2594823992 date "2017-03-07" @default.
- W2594823992 modified "2023-10-17" @default.
- W2594823992 title "Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation" @default.
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