71 research outputs found

    The Effect of Kinesio Tape® on Lower Extremity Functional Movement Screen™ Scores

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    International Journal of Exercise Science 5(3) : 196-204, 2012. The purpose was to determine if application of Kinesio Tape (KT®) improves lower extremity scores on the Functional Movement Screen (FMS™). Individual FMS™ score assessments of 32 college students were obtained. The subjects were then randomized into treatment and control groups. The treatment group had a second FMS™ score after application of KT® to the lower extremity while the control group had a second FMS™ score with no intervention. 16 varsity women’s basketball players and 16 non-varsity female students (Tegner Scale: 6.84 ±1.25, Age: 19±1.2, Height: 165.1±15.1cm, Weight: 68.1±10.9kg) at a NCAA Division II institution participated. FMS™ scores were collected and recorded by the principal investigator. Data was analyzed through two way analysis of variance (ANOVA). Post hoc analysis indicated the treatment group significantly improved in comparison to the control group (Left: P\u3c.001, 95% CI: .283 - .467; Right P\u3c.001, 95% CI: .327 - .523) for both sides of the Hurdle Step. There were no interactions with Deep Squat (P=0.667) or either side of In-Line Lunge (Left: P=0.291, and Right: P=0.530). There were no interactions with either group in Deep Squat and In-Line Lunge of FMS™. However, there was a significant interaction with both groups in the Hurdle Step of FMS™. Findings from this research suggest that KT® may improve movement that incorporates a non-weight-bearing segment

    USC South Campus: A Last Look at Modernism

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    This is a class project from ARTH 542: American Architecture taught at the University of South Carolina by Lydia Mattice Brandt in Spring 2016. With more Americans attending college than ever before; urban renewal; racial integration; the expansion of coeducation; and the architecture community’s advocacy for holistic relationship between planning, architecture, and landscape architecture, the American college campus developed rapidly and dramatically in the mid twentieth century. Using the University of South Carolina’s Columbia Campus as a case study, this project explores the history of American architecture in the mid-twentieth century

    Paraoxonase 1 (PON1) Polymorphisms, Haplotypes and Activity in Predicting CAD Risk in North-West Indian Punjabis

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    Human serum paraoxonase-1 (PON1) prevents oxidation of low density lipoprotein cholesterol (LDL-C) and hydrolyzes the oxidized form, therefore preventing the development of atherosclerosis. The polymorphisms of PON1 gene are known to affect the PON1 activity and thereby coronary artery disease (CAD) risk. As studies are lacking in North-West Indian Punjabi's, a distinct ethnic group with high incidence of CAD, we determined PON1 activity, genotypes and haplotypes in this population and correlated them with the risk of CAD.350 angiographically proven (≥ 70% stenosis) CAD patients and 300 healthy controls were investigated. PON1 activity was determined towards paraoxon (Paraoxonase; PONase) and phenylacetate (Arylesterase; AREase) substrates. In addition, genotyping was carried out by using multiplex PCR, allele specific oligonucleotide -PCR and PCR-RFLP methods and haplotyping was determined by PHASE software. The serum PONase and AREase activities were significantly lower in CAD patients as compared to the controls. All studied polymorphisms except L55M had significant effect on PONase activity. However AREase activity was not affected by them. In a logistic regression model, after adjustment for the conventional risk factors for CAD, QR (OR: 2.73 (1.57-4.72)) and RR (OR, 16.24 (6.41-41.14)) genotypes of Q192R polymorphism and GG (OR: 2.07 (1.02-4.21)) genotype of -162A/G polymorphism had significantly higher CAD risk. Haplotypes L-T-G-Q-C (OR: 3.25 (1.72-6.16)) and L-T-G-R-G (OR: 2.82 (1.01-7.80)) were also significantly associated with CAD.In conclusion this study shows that CAD patients had lower PONase and AREase activities as compared to the controls. The coding Q192R polymorphism, promoter -162A/G polymorphism and L-T-G-Q-C and L-T-G-R-G haplotypes are all independently associated with CAD

    Prediction of the interacting surfaces in a trimolecular complex formed between the major dust mite allergen Der p 1, a mouse monoclonal anti-Der p 1 antibody, and its anti-idiotype

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    Background—Two mouse monoclonal antibodies (mAbs) have been described recently; namely, mAb 2C7 (IgG2bκ), which is directed against the major house dust mite allergen Der p 1, and mAb 2G10 (IgG1κ), which is an anti-idiotypic antibody raised against mAb 2C7. The anti-idiotype mAb 2G10 does not block the binding of mAb 2C7 to Der p 1, which means that mAb 2C7 can simultaneously bind to Der p 1 and to mAb 2G10, thereby generating a trimolecular complex consisting of antigen–idiotype–anti-idiotype. Aims—To sequence and model the V region of the anti-idiotypic antibody mAb 2G10 to enable the prediction of the interacting surfaces in the trimolecular complex consisting of Der p 1–mAb 2C7–mAb 2G10. Methods—DNA sequencing of mAb 2G10 was carried out and the Swiss Model and Swiss PDB-Viewer programs were used to build a three dimensional model of the trimolecular complex. Results—Complementarity of shape and charge was revealed when comparing the protrusion of the previously determined Der p 1 epitope (Leu147–Gln160) with the cavity formed by the complementarity determining regions (CDRs) of mAb 2C7. Such complementarity was also observed between the mAb 2C7 epitope predicted to be recognised by mAb 2G10 (residues Lys19 from framework region 1 (FRW1) and Ser74–Gln81 from FRW3) and residues from the CDRs of mAb 2G10 (a negatively charged patch flanked by the residues Asp55H/Glu58H and Glu27L/Glu27cL). As expected, the location of the mAb 2C7 epitope recognised by mAb 2G10 does not appear to interfere with the binding of Der p 1 to mAb 2C7. Conclusion—Although the results obtained represent only an approximation, they nevertheless provide a rare insight into how an antigen (Der p 1) might bind to its antibody (mAb 2C7) while in complex with an anti-idiotype (mAb 2G10)
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