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Atomic-resolution three-dimensional structure of HET-s(218−289) amyloid fibrils by solid-state NMR spectroscopy. |
Authors: Van Melckebeke, H.; Wasmer, C.; Lange, A.; Ab, E.; Loquet, A.; Boeckmann, A.; Meier, B. H. | Date of Publication (YYYY-MM-DD): 2010-09-09 | Title of Journal: Journal of the American Chemical Society | Volume: 132 | Issue / Number: 39 | Start Page: 13765 | End Page: 13775 | Document Type: Article | ID: 521763.0 |
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Amyloid fibrils of the HET-s(218–289) prion form a β-solenoid with a triangular hydrophobic core. |
Authors: Wasmer, C.; Lange, A.; Van Melckebeke, H.; Siemer, A. B.; Riek, R.; Meier, B. H. | Date of Publication (YYYY-MM-DD): 2008-03-14 | Title of Journal: Science | Volume: 319 | Issue / Number: 5869 | Start Page: 1523 | End Page: 1526 | Document Type: Article | ID: 378710.0 |
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