the purpose of this study was to investigate the validity of the modified ashworth scale (mas) by using both the conventional (hmax/mmax ratio) and the new indicators (hslp/mslp) of motoneuron excitability. this research was a correlational study on twenty post-stroke patients. main outcome measures were the mas and electrophysiologic assessments. the latter was performed using both conventiona...

In polarized T cells, HIV-1 Gag localizes to a rear-end protrusion known as the uropod in a multimerization-dependent manner. Gag-laden uropods participate in formation of virological synapses, intercellular contact structures that play a key role in cell-to-cell HIV-1 transmission. Our previous observations suggest that Gag associates with uropod-directed microdomains (UDMs) that eventually co...

Rous sarcoma virus (RSV) budding requires an interaction of the L domain within the p2b region of Gag with cellular Nedd4-family E3 ubiquitin protein ligases. Members of our laboratories previously demonstrated that overexpression of a fragment of the chicken Nedd4-like protein (LDI-1 WW) inhibits Gag release in a dominant-negative manner (A. Kikonyogo, F. Bouamr, M. L. Vana, Y. Xiang, A. Aiyar...

RNA appears to be required for the assembly of retroviruses. This is likely due to binding of RNA by multiple Gags, which in turn organizes and stabilizes the Gag-Gag interactions that form the virion. While the nucleocapsid (NC) domain is the most conspicuous RNA-binding region of the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein, we have previously shown that NC is not strictly ...

29 In polarized T cells, HIV-1 Gag localizes to a rear end protrusion known as the uropod in 30 a multimerization-dependent manner. Gag-laden uropods participate in formation of virological 31 synapses, an intercellular contact structure that plays a key role in cell-to-cell HIV-1 32 transmission. Our previous observations suggest that Gag associates with uropod-directed 33 microdomains (UDMs) ...

HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with target cell membrane, forms a cell junction known as the virological synapse. While Gag associatio...

HIV-1 Gag selects and packages a dimeric, unspliced viral RNA in the context of a large excess of cytosolic human RNAs. As Gag assembles on the plasma membrane, the HIV-1 genome is enriched relative to cellular RNAs by an unknown mechanism. We used a minimal system consisting of purified RNAs, recombinant HIV-1 Gag and giant unilamellar vesicles to recapitulate the selective packaging of the 5'...

Urinary glycosaminoglycan (GAG) excretion was measured in 24 patients with active rheumatoid arthritis (RA) before and after treatment with conventional second-line agents. Urinary GAG excretion was also measured in normal controls, patients with osteoarthritis (OA), and patients with acute myocardial infarction (MI). Total GAG excretion was increased in the RA group and fell after second-line ...

The genomic retroviral RNA is the messenger for the translation of the gag and pol genes encoding the precursors to the major structural proteins and enzymes, respectively, of the virion core. The long 5' untranslated region, the leader, is formed of independent well-structured domains involved in key steps of the viral life cycle such as the initiation of proviral DNA synthesis, genomic RNA di...

The nucleocapsid (NC) domain of the retrovirus Gag protein plays several important roles in the viral life cycle, including virus assembly, viral genomic RNA encapsidation, primer tRNA placement, and enhancement of viral reverse transcription. In this study, deletion of NC domain of human immunodeficiency virus type 1 (HIV-1) Gag was found to drastically reduce virus particle production in CD4(...