15 research outputs found
Optimization and design of a cable driven upper arm exoskeleton
This paper presents the design of a wearable upper arm exoskeleton that can be used to assist and train arm movements of stroke survivors or subjects with weak musculature. In the last ten years, a number of upper-arm training devices have emerged. However, due to their size and weight, their use is restricted to clinics and research laboratories. Our proposed wearable exoskeleton builds upon our extensive research experience in wire driven manipulators and design of rehabilitative systems. The exoskeleton consists of three main parts: (i) an inverted U-shaped cuff that rests on the shoulder, (ii) a cuff on the upper arm, and (iii) a cuff on the forearm. Six motors, mounted on the shoulder cuff, drive the cuffs on the upper arm and forearm, using cables. In order to assess the performance of this exoskeleton, prior to use on humans, a laboratory test-bed has been developed where this exoskeleton is mounted on a model skeleton, instrumented with sensors to measure joint angles and transmitted forces to the shoulder. This paper describes design details of the exoskeleton and addresses the key issue of parameter optimization to achieve useful workspace based on kinematic and kinetic models.</jats:p
Differential effects of phenobarbital, pentobarbital and diphenylhydantoin on motor cortical and reticular thresholds in the rhesus monkey
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/46378/1/213_2004_Article_BF00404118.pd
Influence of Autoclave Molding Modes and Stack Structure on Porosity of Composite Materials
Effect of Low Temperature on Fatigue Crack Formation and Microstructure-Scale Growth from Corrosion Damage in Al-Zn-Mg-Cu
Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression of SSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers