975 resultados para function space


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'We need to talk (Performace Space)' is a 3 channel audio work with round table and custom cushions, examining the discursive framework of LEVEL as a feminist art collective. It was included in the exhibition 'Sexes', curated by Bec Dean, Jeff Khan and Deborah Kelly, at Performance Space. The audio works feature recontextualised excerpts from a series of dinner party conversations, which focused on the role of women and feminism in the 21st century. Placed in a specially constructed ‘lazy susan’, this audio installation speaks of the experience of sharing information, ideas and experiences ‘around the table’. The fabric patterns on the floor cushions have been designed from banners created in collective workshops with women in Brisbane and Melbourne, Australia, as a way of translating personal statements and political ideas into the everyday.

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Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has been the focus of intense research. Early studies addressed why it is so oxidizing and how it is maintained in its less stable oxidized state. The crystal structure of Escherichia coli DsbA (EcDsbA) revealed that the oxidizing periplasmic enzyme is a distant evolutionary cousin of the reducing cytoplasmic enzyme thioredoxin. Recent significant developments have deepened our understanding of DsbA function, mechanism, and interactions: the structure of the partner membrane protein EcDsbB, including its complex with EcDsbA, proved a landmark in the field. Studies of DsbA machineries from bacteria other than E. coli K-12 have highlighted dramatic differences from the model organism, including a striking divergence in redox parameters and surface features. Several DsbA structures have provided the first clues to its interaction with substrates, and finally, evidence for a central role of DsbA in bacterial virulence has been demonstrated in a range of organisms. Here, we review current knowledge on DsbA, a bacterial periplasmic protein that introduces disulfide bonds into diverse substrate proteins and which may one day be the target of a new class of anti-virulence drugs to treat bacterial infection. Antioxid. Redox Signal. 14, 1729–1760.