The relationship between structure and function is important in the judgement of the horse. Twenty sound riding horses walked and trotted on a treadmill. The movement of the backs of each of the horses was measured using a commercially available movement analysis system. Morphometric, spatiotemporal and kinematic information were correlated to investigate the effect of conformation on movement. Taller and heavier horses seem to have longer thoracic and lumbar backs, and are wider at the pelvis. Horses with longer strides extended and flexed their backs in the caudal saddle region to a greater extent at the walk, but not the trot. Horses with greater angle of L5 tend to extend and flex this region of the back more. At the walk and trot, a long thoracic back results in greater lumbar lateral bending. A negative relationship was found between the curvature of mid-thoracic back and the amount of lateral bending of L1 and L3 and axial rotation of the pelvis at the trot. There are clear relationships between back conformation and movement that may be important to the orthopaedic health of the horse. Further understanding of the relationships between conformation, movement and injury may provide an objective basis for the evaluation of future performance and soundness.
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http://dx.doi.org/10.1111/j.2042-3306.2002.tb05439.x | DOI Listing |
J Biomol Struct Dyn
January 2025
Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
Cancer sparks if the components of the cellular signaling network are aberrantly activated, leading to uncontrolled cell growth and proliferation. One of the most important players of this highly regulated network is the Wnt/β-catenin signaling, with a significant role in human health and disease. The critical co-receptor of this pathway, LRP6, is overexpressed in various cancer types and is a target for therapy.
View Article and Find Full Text PDFNat Commun
January 2025
Center for Life Sciences, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, School of Life Sciences, Yunnan University, Kunming, China.
Phosphorus in crucial for all living organisms. In vertebrate, cellular phosphate homeostasis is partly controlled by XPR1, a poorly characterized inositol pyrophosphate-dependent phosphate exporter. Here, we report the cryo-EM structure of human XPR1, which forms a loose dimer with 10 transmembrane helices (TM) in each protomer.
View Article and Find Full Text PDFJ Lipid Res
January 2025
Finsen Laboratory, Copenhagen University Hospital - Rigshospitalet, Copenhagen, Denmark; Biotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark. Electronic address:
Movement of lipoprotein lipase (LPL) from myocytes or adipocytes to the capillary lumen is essential for intravascular lipolysis and plasma triglyceride homeostasis-low LPL activity in the capillary lumen causes hypertriglyceridemia. The trans-endothelial transport of LPL depends on ionic interactions with GPIHBP1's intrinsically disordered N-terminal tail, which harbors two acidic clusters at positions 5-12 and 19-30. This polyanionic tail provides a molecular switch that controls LPL detachment from heparan sulfate proteoglycans (HSPGs) by competitive displacement.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Chemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia.
ORF2p (open reading frame 2 protein) is a multifunctional multidomain enzyme that demonstrates both reverse transcriptase and endonuclease activities and is associated with the pathophysiology of cancer. The 3D structure of the entire seven-domain ORF2p complex was revealed with the recent achievements in structural studies. The different arrangements of the CTD (carboxy-terminal domain) and tower domains were identified as the "closed-ring" and "open-ring" conformations, which differed by the hairpin position of the tower domain, but the structural diversity of these complexes has the potential to be more extensive.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Bioengineering, California Institute of Technology, Pasadena, CA 91125.
The diversity and heterogeneity of biomarkers has made the development of general methods for single-step quantification of analytes difficult. For individual biomarkers, electrochemical methods that detect a conformational change in an affinity binder upon analyte binding have shown promise. However, because the conformational change must operate within a nanometer-scale working distance, an entirely new sensor, with a unique conformational change, must be developed for each analyte.
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