ABSTRACT
This clinical report describes a treatment protocol for completely edentulous patients using digital implant planning for an all-on-4 treatment of both the maxilla and mandible as well as the use of a shape-memory alloy retention system to secure a complete-arch restoration to the mandible.
Subject(s)
Dental Implants , Jaw, Edentulous , Dental Prosthesis, Implant-Supported , Dental Restoration Failure , Follow-Up Studies , Humans , Mandible , Maxilla , Shape Memory AlloysABSTRACT
A new hybrid particle swarm optimization (PSO) that incorporates a wavelet-theory-based mutation operation is proposed. It applies the wavelet theory to enhance the PSO in exploring the solution space more effectively for a better solution. A suite of benchmark test functions and three industrial applications (solving the load flow problems, modeling the development of fluid dispensing for electronic packaging, and designing a neural-network-based controller) are employed to evaluate the performance and the applicability of the proposed method. Experimental results empirically show that the proposed method significantly outperforms the existing methods in terms of convergence speed, solution quality, and solution stability.
Subject(s)
Algorithms , Behavior, Animal , Biomimetics/methods , Industry/methods , Models, Theoretical , Neural Networks, Computer , Signal Processing, Computer-Assisted , Animals , Computer SimulationABSTRACT
WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs and phosphorylated serine/threonine-proline sites. To pursue the functional properties of WW domains, we employed mass spectrometry to identify 148 proteins that associate with 10 human WW domains. Many of these proteins represent novel WW domain-binding partners and are components of multiprotein complexes involved in molecular processes, such as transcription, RNA processing, and cytoskeletal regulation. We validated one complex in detail, showing that WW domains of the AIP4 E3 protein-ubiquitin ligase bind directly to a PPXY motif in the p68 subunit of pre-mRNA cleavage and polyadenylation factor Im in a manner that promotes p68 ubiquitylation. The tested WW domains fall into three broad groups on the basis of hierarchical clustering with respect to their associated proteins; each such cluster of bound proteins displayed a distinct set of WW domain-binding motifs. We also found that separate WW domains from the same protein or closely related proteins can have different specificities for protein ligands and also demonstrated that a single polypeptide can bind multiple classes of WW domains through separate proline-rich motifs. These data suggest that WW domains provide a versatile platform to link individual proteins into physiologically important networks.