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2. Evaluating determinants of rider performance in high-level dressage riders

Author

Hobbs, Sarah Jane, Serra Braganca, F. M., Rhodin, M., Hernlund, E., Peterson, M. L., Clayton, H. M., Hobbs, Sarah Jane, Serra Braganca, F. M., Rhodin, M., Hernlund, E., Peterson, M. L., and Clayton, H. M.

Abstract

Many factors influence the overall score for a dressage test, which makes it challenging and complex to establish key performance determinants. The aim was to identify an objective locomotory measure to quantify overall rider performance in dressage. The chosen variable should be both easy to collect and useful in a practical context. Twenty dressage horse/ rider combinations (Int1-GP) were equipped with inertial measurement units (IMU’s, 200 Hz) attached to the rider’s sacrum and thorax. Transverse dynamic trunk symmetry and pelvis symmetry (symmetry measures) and trunk-to-pelvis 3-dimensional coordination variability (within rider coordination measure) were collected from the IMU’s during straight line walk, trot and canter on left and right reins with ≥9 strides/condition. Sixteen United States Dressage Federation senior judges evaluated the movements of interest from video footage with 2-3 judges scoring each rider’s performance in the movements of interest and awarding collective scores to represent the overall impression of each rider’s performance. Stepwise linear regression was used to seek associations between objective measurements from the IMUs and subjective scores awarded by the judges. The variable dynamic trunk symmetry was the strongest predictor of collective scores, specifically the score for rider position (R=0.357, P=0.001). The rider’s dynamic pelvic symmetry was a strong predictor of the judged score for the walk (R=0.607, P=0.010), but no relationships were found between objective and judged scores for trot or canter. The overall impression of trunk posture may be influential in judges’ collective scores. Symmetrical pelvic motion appears to be a key factor in producing a high-quality walk.

Published
2023

21. High Throughput Solid Phase Parallel Synthesis of Macrocyclic Peptidomimetics

Author

Marsault, E., Hoveyda, H. R., Peterson, M. L., Gagnon, R., Vézina, M., Pinault, J.F., Landry, A., Saint-Louis, C., Ouellet, L. G., Beauchemin, S., Benakli, K., Beaubien, S., Brassard, M., Wang, Z., Champagne, M., Galaud, F., Fortin, N., Fortin, D., Plourde, V., Ramaseshan, M., Bhat, S., Bilodeau, F., Lonergan, D., Lan, R., Li, S., Berthiaume, G., Foucher, L., Peng, X., Dory, Y., Deslongchamps, P., Valle, Susan Del, editor, Escher, Emanuel, editor, and Lubell, William D., editor

Published
2009
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37. Extensively drug-resistant tuberculosis ‘hotspots' and sociodemographic associations in Durban, South Africa

Author

Peterson, M. L., primary, Gandhi, N. R., additional, Clennon, J., additional, Nelson, K. N., additional, Morris, N., additional, Ismail, N., additional, Allana, S., additional, Campbell, A., additional, Brust, J. C. M., additional, Auld, S. C., additional, Mathema, B., additional, Mlisana, K., additional, Moodley, P., additional, and Shah, N. S., additional

Published
2019
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40. Rider preferences for arena characteristics in showjumping

Author

Hernlund, E, Hobbs, Sarah Jane, Roepstorff, L, Peterson, M, L, Tranquille, C, Murray, R, Bergh, A, and Egenvall, A

Subjects
genetic structures, behavior and behavior mechanisms, D422, humanities, health care economics and organizations, psychological phenomena and processes
Published
2016

41. Novel Compstatin Family Peptides Inhibit Complement Activation by Drusen-Like Deposits in Human Retinal Pigmented Epithelial Cell Cultures

Author

Gorham, R. D., Forest, D. L., Tamamis, Phanourios, López de Victoria, A., Kraszni, M., Kieslich, C. A., Banna, C. D., Bellows-Peterson, M. L., Larive, C. K., Floudas, C. A., Archontis, Georgios Z., Johnson, L. V., Morikis, D., Tamamis, Phanourios [0000-0002-3342-2651], and Archontis, Georgios Z. [0000-0002-7750-8641]

Subjects
Cell, Peptide, arginine, protein binding, Retinal Pigment Epithelium, AMD, C3b, C3c, chemistry.chemical_compound, 0302 clinical medicine, lipophilicity, retina macula age related degeneration, protein data bank, Complement Activation, Compstatin family peptides, Cells, Cultured, apolipoprotein E, chemistry.chemical_classification, 0303 health sciences, C5b-9, article, Sensory Systems, peptide, 3. Good health, unclassified drug, pigment cell, fetus, medicine.anatomical_structure, Biochemistry, priority journal, immunohistochemistry, ELISA, RPE, reversed phase high performance liquid chromatography, Complement inhibitors, drug potency, ApoE, FB, PDB, in vitro study, Complement system, high performance liquid chromatography, Retinal Drusen, Drusen, Biology, Molecular dynamics, Complement factor B, Peptides, Cyclic, Article, complement component C3, 03 medical and health sciences, Cellular and Molecular Neuroscience, peptide synthesis, factor B, medicine, Humans, controlled study, human, protein structure, C3, the c-fragment of C3, age-related macular degeneration, alternative pathway of complement activation, 030304 developmental biology, nuclear magnetic resonance spectroscopy, hydrophobicity, complement activation, cell culture, Retinal pigment epithelium, human cell, Macular degeneration, MD, compstatin, Retinal, IC 50, the b-fragment of C3, medicine.disease, biogenesis, pigment epithelium, eye diseases, enzyme linked immunosorbent assay, Ophthalmology, complement system protein 3, the membrane attack complex consisting of complement proteins C5b, C6, C7, C8, and C9(n), chemistry, concentration response, RP-HPLC, 030221 ophthalmology & optometry, drug solubility, pathology, enzyme-linked immunosorbent assay, Retinal pigmented epithelium, sense organs, AP
Abstract

We have used a novel human retinal pigmented epithelial (RPE) cell-based model that mimics drusen biogenesis and the pathobiology of age-related macular degeneration to evaluate the efficacy of newly designed peptide inhibitors of the complement system. The peptides belong to the compstatin family and, compared to existing compstatin analogs, have been optimized to promote binding to their target, complement protein C3, and to enhance solubility by improving their polarity/hydrophobicity ratios. Based on analysis of molecular dynamics simulation data of peptide-C3 complexes, novel binding features were designed by introducing intermolecular salt bridge-forming arginines at the N-terminus and at position-1 of N-terminal dipeptide extensions. Our study demonstrates that the RPE cell assay has discriminatory capability for measuring the efficacy and potency of inhibitory peptides in a macular disease environment.© 2013 Elsevier Ltd. 116 96 108 Cited By :15

Published
2013

43. British Diabetic Association Abstracts Medical and Scientific Section, Spring Meeting: Oxford, 5th and 6th April 1968

Author

Garratt, C. J., Jones, A. H., Miles, L. E. M., Hales, C. N., Manchester, K. L., Buchanan, K. D., Vance, J. E., Morgan, A., Williams, R. H., Track, Norman S., Caird, F. I., Kohner, E. M., Roth, J., Bulpitt, C. J., Dollery, C. T., Fraser, T. Russell, Weight, A. D., Oakley, N. W., Hartog, M., Joplin, G. F., Mayne, B. E., Weaver, J. A., Bridges, J. M., Butterfield, W. J. H., Keates, J. S., Devlin, James G., Stephenson, Nuala, Malherbe, C., Heller, F., de Gasparo, M., Hoet, J. J., Robertson, W. B., Robinson, D. S., Kingsbury, K. J., O'Sullivan, John B., Keen, H., Jarrett, R. J., Chlouverakis, C., Boyns, D. A., Pyke, D. A., Hardwick, G., Catterall, R. C. F., Kemball, Margaret, Nourse, Christopher, Sohiff, David, Tiernan, Ray, Bevan, A. T., Hockaday, T. D. R., Jelfs, R., Bewsher, P. D., Scott, R. D. M., Stowers, J. M., Adnitt, P. I., Oleesky, S., Schnieden, H., Rigas, A. N., Bittles, A., Hadden, D. R., Montgomery, D. A. D., Bingle, J. P., McKiddie, M. T., Albutt, E. C., Chance, G. W., Hirsch J., Farquhar, J. W., Ahrens, E. H., Peterson, M. L., Stoffel, W., Dayton S., Hashimoto, S., Pearce, M. L., Cohen, N. M., Alexander, D. Pauline, Britton, H. G., Nixon, D. A., Parker, R. A., Campbell, N., Oakley, W. G., Peel, J., Taylor, K. W., Boyns, A. R., Mahler, R., Pearce, N., Kaden, M., Field, J. B., Matty, A. J., and Qureshi, M. A.

Published
1968
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44. Molecular Dynamics in Drug Design: New Generations of Compstatin Analogs

Author

Tamamis, Phanourios, López de Victoria, A., Gorham, R. D., Bellows-Peterson, M. L., Pierou, P., Floudas, C. A., Morikis, D., Archontis, Georgios Z., Tamamis, Phanourios [0000-0002-3342-2651], and Archontis, Georgios Z. [0000-0002-7750-8641]

Subjects
crystal structure, drug design, Molecular Sequence Data, Molecular modeling, protein binding, Molecular Dynamics Simulation, Peptides, Cyclic, hydroxymethylglutaryl coenzyme A reductase inhibitor, Mice, binding affinity, physical chemistry, Humans, Animals, Animalia, rat, Mechanism-based drug design, human, mouse, hydrophobicity, Complement system, C3, hydrogen bond, nonhuman, Rattus, solubility, article, retina macula degeneration, X ray crystallography, molecular docking, Complement C3, molecular dynamics, amino acid sequence, unclassified drug, Rats, priority journal, protein stability, protein protein interaction, amino terminal sequence, Compstatin, protein secondary structure, Structure-based drug design, mutation
Abstract

We report the computational and rational design of new generations of potential peptide-based inhibitors of the complement protein C3 from the compstatin family. The binding efficacy of the peptides is tested by extensive molecular dynamics-based structural and physicochemical analysis, using 32 atomic detail trajectories in explicit water for 22 peptides bound to human, rat or mouse target protein C3, with a total of 257 ns. The criteria for the new design are: (i) optimization for C3 affinity and for the balance between hydrophobicity and polarity to improve solubility compared to known compstatin analogs and (ii) development of dual specificity, human-rat/mouse C3 inhibitors, which could be used in animal disease models. Three of the new analogs are analyzed in more detail as they possess strong and novel binding characteristics and are promising candidates for further optimization. This work paves the way for the development of an improved therapeutic for age-related macular degeneration, and other complement system-mediated diseases, compared to known compstatin variants. © 2012 John Wiley & Sons A/S. 79 5 703 718 Cited By :16

Published
2012

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