| dc.contributor.author | Barritt, JD | en_US |
| dc.contributor.author | Viles, JH | en_US |
| dc.date.accessioned | 2016-02-02T12:30:06Z | |
| dc.date.issued | 2015-11-13 | en_US |
| dc.date.submitted | 2015-12-10T15:31:37.607Z | |
| dc.identifier.issn | 0021-9258 | en_US |
| dc.identifier.uri | http://qmro.qmul.ac.uk/xmlui/handle/123456789/11005 | |
| dc.format.extent | 27791 - 27802 | en_US |
| dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | en_US |
| dc.rights | This research was originally published in Journal of Biological Chemistry. Barritt, Joseph D., and John H. Viles. "Truncated Amyloid-β (11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly." Journal of Biological Chemistry 290.46 (2015): 27791-27802. © The American Society for Biochemistry and Molecular Biology | |
| dc.title | Truncated Amyloid-beta((11-40/42)) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly | en_US |
| dc.type | Article | |
| dc.identifier.doi | 10.1074/jbc.M115.684084 | en_US |
| pubs.author-url | http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000365757500030&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=612ae0d773dcbdba3046f6df545e9f6a | en_US |
| pubs.issue | 46 | en_US |
| pubs.notes | No embargo | en_US |
| pubs.notes | This is the accepted daft with figs as a pdf Now published in JBC | en_US |
| pubs.publication-status | Published | en_US |
| pubs.volume | 290 | en_US |
| qmul.funder | Fundamental membrane interactions of copper generated oligomers, profibrils and amyloid fibres::Biotechnology and Biological Sciences Research Council | en_US |
