Serious challenges are raised by the way in which technology companies like Facebook and Google harvest and process user data. Companies in the modern data economy mine troves of data with sophisticated algorithms to produce valuable behavioural predictions. These data-driven predictions provide companies with a powerful capacity to influence and manipulate users, and these risks are increasing with the explosive growth of ‘Big Data’ and artificial intelligence machine learning. This article analyses the extent to which these challenges are met by existing regimes such as Australia and New Zealand’s respective privacy acts and the European Union’s General Data Protection Regime. While these laws protect certain privacy interests, I argue that users have a broader set of interests in their data meriting protection. I explore three of these novel interests, including the social dimension of data, control and access to predictions mined from data and the economic value of data. This article shows how existing frameworks fail to recognise or protect these novel interests. In light of this failure, lawmakers urgently need to frame new legal regimes to protect against the worst excesses of the data economy.
The Moeller SMART Team in conjunction with Dr. JiaJie Diao at the University of Cincinnati Medical College and MSOE Center for Biomolecular Modeling used 3‐D modeling and printing technology to study the role of Soluble NSF Attachment Protein Receptor (SNARE) proteins in macroautophagy, a process that recycles damaged organelles, proteins, and microbes in the cell. It begins with the formation and maturation of an autophagosome. The process ends with the fusion of a fully matured autophagosome to a lysosome membrane, which is mediated by SNARE proteins. Vesicular fusion is initiated by the formation of a tetrameric alpha‐helix complex that is formed through the binding of three helical SNARE proteins. One of these SNARE proteins, VAMP8, is located on lysosomes and the other two, syntaxin17 and SNAP‐29, are located on the membrane of autophagosomes. The helices of these proteins coil tightly in the alpha‐helix complex which provides the energy for fusion. To reset the conformation of SNARE proteins, N‐Ethylmaleimide‐Sensitive Factor (NSF) proteins use ATP and water to recycle SNAREs. Alpha‐SNAP, an ATPase, which helps to facilitate this process, returns SNARE to its original high energy state. If fusion is unable to occur in autophagy, the cell accumulates autophagosomes, causing lysosome storage diseases such as Parkinson's and Alzheimer's disease. By 3‐D printing the coiled alpha‐helix complex, our SMART team intends to describe this crucial element of membrane fusion and the disorders associated with macroautophagy.
This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
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