Methods. A FE model of intact C2-C7 segments was developed and validated. Fixed-core (Prodisc-C, Synthes) and mobile-core (Mobi-C, LDR Spine) artificial disc prostheses were integrated at the C5-C6 segment into the validated FE model. All models were subjected to a follower load of 50 N and a moment of 1 Nm in flexion-extension, lateral bending, and axial torsion. The range

of segmental motion (ROM), facet joint force, tension on major ligaments, and stress on the polyethylene (PE) cores were analyzed.

Results. The ROM in the intact segments after ADR was not significantly different from those of the normal cervical spine model. The ROM in the implanted segment (C5-C6) increased during flexion (19% for fixed and 33% for mobile core), extension (48% for fixed and 56% for mobile core), lateral bending (28% for fixed and 35% for mobile core) and axial torsion (45% for fixed and 105% for mobile core). The facet joint force increased see more by 210% in both fixed and mobile core models during extension and the tension increased (range, 66%-166%) in all ligaments during flexion. The peak stress on a PE core was greater than the yield stress (51 MPa for fixed and 36 MPa for mobile core).

Conclusion. The results

of our study presented an increase in ROM, facet joint force, and ligament tension at the ADR segments. The mobile-core model showed a higher increase Selleckchem Cl-amidine in segmental motion, facet force, and ligament tension, but lower stress on the PE core than the fixed-core model.”
“Point mutations resulting in the substitution of a single amino acid can

cause severe functional consequences, but can also be completely harmless. Understanding what determines the phenotypical this website impact is important both for planning targeted mutation experiments in the laboratory and for analyzing naturally occurring mutations found in patients. Common wisdom suggests using the extent of evolutionary conservation of a residue or a sequence motif as an indicator of its functional importance and thus vulnerability in case of mutation. In this work, we put forward the hypothesis that in addition to conservation, co-evolution of residues in a protein influences the likelihood of a residue to be functionally important and thus associated with disease. While the basic idea of a relation between co-evolution and functional sites has been explored before, we have conducted the first systematic and comprehensive analysis of point mutations causing disease in humans with respect to correlated mutations. We included 14,211 distinct positions with known disease-causing point mutations in 1,153 human proteins in our analysis. Our data show that (1) correlated positions are significantly more likely to be disease-associated than expected by chance, and that (2) this signal cannot be explained by conservation patterns of individual sequence positions.