Breaking the Double Impasse: Securing and Supporting Diverse Housing Tenures in the United States

What might be described as a double impasse characterizes debate on U.S. housing tenure with advocates fighting for rental or ownership housing on one side and Third Way or mixed-tenure solutions on the other. Breaking this impasse requires disengaging from conceptions of an idealized form of tenure and instead advocating making virtually all tenures as secure and supported as possible, so that diverse households are able to live in homes that best fit their changing needs over their life cycles. This essay (a) presents data on the variety of tenures in the United States; (b) conveys a new two-dimensional map of tenure according to their degrees of control and potential for wealth-building; and (c) shows how U.S. institutions shape their risks and subsidies. Most U.S. tenures are at least somewhat risky, including those that receive the greatest federal subsidies. A new housing system is needed to secure and support as many tenures as possible

Architectures of control in consumer product design

Copyright @ 2005 Social Services Research GroupThe idea of architectures of control is introduced through examples ranging from urban planning to digital rights management, and the intentions behind their use in consumer products are examined, with reference to case studies of printer cartridges and proposed 'optimum lifetime products.' The reactions of the technical community and consumers themselves are also explored, along with some wider implications for society

A new era for understanding amyloid structures and disease

The aggregation of proteins into amyloid fibrils and their deposition into plaques and intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition of amyloid fibrils, collectively known as amyloidosis, is associated with many pathological conditions that can be associated with ageing, such as Alzheimer disease, Parkinson disease, type II diabetes and dialysis-related amyloidosis. However, elucidation of the atomic structure of amyloid fibrils formed from their intact protein precursors and how fibril formation relates to disease has remained elusive. Recent advances in structural biology techniques, including cryo-electron microscopy and solid-state NMR spectroscopy, have finally broken this impasse. The first near-atomic-resolution structures of amyloid fibrils formed in vitro, seeded from plaque material and analysed directly ex vivo are now available. The results reveal cross-β structures that are far more intricate than anticipated. Here, we describe these structures, highlighting their similarities and differences, and the basis for their toxicity. We discuss how amyloid structure may affect the ability of fibrils to spread to different sites in the cell and between organisms in a prion-like manner, along with their roles in disease. These molecular insights will aid in understanding the development and spread of amyloid diseases and are inspiring new strategies for therapeutic intervention