Background: No study has reported the differences between sides in the net muscular moment of lower limbs of subjects with hemiparesis during sit-to-stand and stand-to-sit tasks in various foot positions. Moreover, the asymmetry of lower-joint moments has not yet been related to muscular weakness of the lower limbs in this population.
Methods: A convenience sample of 12 individuals (mean age (standard deviation): 49.
Background: The asymmetrical motor pattern of persons with hemiparesis influences the performance of activities that require interactions between the two sides of the body.
Methods: Twelve subjects with a chronic hemiparesis were asked to stand up and sit down at their natural speed in the following foot positions: (1) spontaneous; (2) symmetrical; (3) asymmetrical with the affected foot placed backward; and (4) asymmetrical with the unaffected foot placed backward. Forces were recorded under each foot using two force plates and under each thigh with an instrumented chair.
Objective: The purpose of this study was to measure the effect of repeated distension arthrographies combined with a home exercise program on impairments and disability of the upper limb in subjects with adhesive capsulitis of the shoulder.
Design: A total of 15 subjects with idiopathic adhesive capsulitis participated in the study. Intervention consisted of three distension arthrographies with steroid, done at 3-wk intervals, and a home exercise program.
The 3' poly(A) tail of eukaryotic mRNAs and the poly(A) binding protein (PABP) play important roles in the regulation of translation. Recently, a human PABP-interacting protein, Paip2, which disrupts the PABP-poly(A) interaction and consequently inhibits translation, was described. To gain insight into the biological role of Paip2, we studied the Drosophila melanogaster Paip2 (dPaip2).
View Article and Find Full Text PDFThe 3' poly(A) tail of eukaryotic mRNAs plays an important role in the regulation of translation. The poly(A) binding protein (PABP) interacts with eukaryotic initiation factor 4G (eIF4G), a component of the eIF4F complex, which binds to the 5' cap structure. The PABP-eIF4G interaction brings about the circularization of the mRNA by joining its 5' and 3' termini, thereby stimulating mRNA translation.
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