The University of South Australia (UniSA)

Australia

In 2016, the University of South Australia (UniSA) celebrates its 25th birthday. We are a young university, continuing to set the pace for world-class research and solutions for a changing world. As Australia’s University of Enterprise, the spirit of enterprise runs through everything we do.

Our research is inspired by challenges and opportunities, partnered with end-users and communities, and underpinned by excellence. We work collaboratively with our partners right from the conception of a research idea, allowing our research directions to be shaped by their opportunities and challenges.

UniSA’s strong commitment to cutting-edge research and engagement with industry has been well recognised, with 97 per cent of our research rated at or above world-class standard (Excellence for Research in Australia 2015). This is an impressive result for a young university, and we are proud of our achievements.

Our research culture is vibrant, outward facing and responsive. We pride ourselves on our capacity to create interdisciplinary teams that can tackle significant real-world challenges, and our researchers strive to make a difference outside the world of academe.

We are globally connected and engaged, helping solve the problems of industry and the professions. Our teaching is industry-informed, our research inventive and adventurous, and focused on creating impact. Through our research, we create knowledge that is central to global economic and social prosperity.

1 February 2017 - 31 January 2018

Region: Global
Subject/journal group: All

The table to the right includes counts of all research outputs for The University of South Australia (UniSA) published between 1 February 2017 - 31 January 2018 which are tracked by the Nature Index.

Hover over the donut graph to view the WFC output for each subject. Below, the same research outputs are grouped by subject. Click on the subject to drill-down into a list of articles organized by journal, and then by title.

Note: Articles may be assigned to more than one subject area.

AC	FC	WFC
30	2.89	2.89

Outputs by subject (WFC)

Subject	AC	FC	WFC
Chemistry	11	2.09	2.09
Physical Sciences	10	0.47	0.47
Life Sciences	14	0.83	0.83
Earth & Environmental Sciences	1	0.10	0.10

Highlight of the month

Bound by salt

© KATERYNA KON/SCIENCE PHOTO LIBRARY/Getty

A new study reveals how members of the 14-3-3 protein family chaperone their target proteins, including those linked with Alzheimer’s and Parkinson’s, such as tau proteins.

14-3-3 proteins become pairs to form dimers which are thought to be stabilized by salt bridges between sites in the two proteins. To understand the importance of these salt bridges, a team including researchers at the University of South Australia engineered a 14-3-3 protein in which the salt bridge-forming sites had been mutated.

The mutated proteins could not make salt bridges, but still formed dimers. These dimers, however, were more dynamic and thus less resilient to changes in temperature or concentration of 14-3-3 proteins. Further analysis revealed that the interface between the subunits of the dimer was more exposed in the mutated proteins, explaining the reduced dimer stability. Exposure of the interface in the mutated proteins also made them more effective at blocking the aggregation of signalling proteins.

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