Mobility is something able-bodied people take for granted. Approximately 132,500 people in the United Kingdom have disabilities which permanently confine them to a wheelchair; 40,000 of these require a powered wheelchair. The opportunity to lead a normal life and be accepted as an equal by the able-bodied population is limited by their reduced mobility. As much freedom of movement as possible is therefore crucial for these people. Powered wheelchair users' mobility depends upon the manoeuvrability of the chair. For optimum manoeuvrability a chair must be capable of moving in any direction. Currently no omni-directional powered wheelchairs are commercially available. This thesis describes the design and deVelopment of a powered base unit for a wheelchair, controlled to instantaneously move in any direction. The novelty is principally represented by the innovative design and configuration of four omni-directional roller wheels* (LUMAN wheels) which, when individually controlled, produce the omni-directional movement of the base unit. Further novelty within the design is a set of bi-directional angled roller couplings that simultaneously disengage the wheels from the motors, via a cable linkage mechanism, and simple control system. Mathematical data models illustrate the theoretical performance of the wheel configuration, and a prototype base unit is tested to prove these hypotheses.

Luman (LZIP/CREB3) is a basic leucine zipper (bZIP) transcription factor that has been linked to the endoplasmic reticulum (ER) stress response. In the event of ER stress, Luman is proteolytically cleaved, or ‘activated’, through regulated intramembrane proteolysis (RIP), resulting in an amino-terminal fragment that translocates to the nucleus to activate transcription of downstream unfolded protein response (UPR)-related genes. The general mode of activation of the key signal transducers of the UPR appears to be an alteration of their oligomeric states. Structural and functional similarities to these proteins suggest that Luman may be activated in a similar manner. In this thesis, we demonstrate through in vitro and in vivo studies that Luman can form homodimers in the cell. Through the use of mutagenesis, we show that Luman dimerization is mediated through the leucine zipper and we provide evidence that Luman dimerization is required for its transcription activation function. However, we found that Luman dimerization is not required for its activation by proteolytic cleavage.