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        Our problems and observations in 3D facial implant planning

        Gianmarco Saponaro,Chiara Paolantonio,Giorgio Barbera,Enrico Foresta,Giulio Gasparini,Alessandro Moro 대한악안면성형재건외과학회 2022 Maxillofacial Plastic Reconstructive Surgery Vol.44 No.-

        Background: Three-dimensional renderings of two-dimensional computed tomography data have allowed for more precise analysis in the craniofacial field. Design, engineering, architecture, and other industries have paved the way for the manipulation and printing of three-dimensional objects. The usual planning is only carried out based on the bony structures, often without taking into consideration the presence of soft tissues and soft structures. During our practice, we have found ourselves facing the challenge posed by these structures; the aim of this article is to discuss our experience in designing implants presenting our tips and tricks for a better planning leading to an easy and reliable positioning. Case presentation: We have retrieved all patients in 5 years among those who underwent computer-aided design/ computer-aided manufacturing implant placement in the last 5 years in order to review the eventual problems and the solutions found. A total number of 25 patients were retrieved and, among them, 10 patients were selected, in which planning inaccuracy caused difficulties during implant placement and which then led to induced changes during the planning of similar cases or in which the problems were noted before or during the planning which led to changes in the plan to address those problems. Six of the selected cases were polyetheretherketone facial implants for the correction of residual deformities in malformed or deformed patients. One case was a delayed orbital reconstruction with a titanium implant. Two cases were titanium functional and anatomical reconstruction of the mandible in patients with failed post-oncological reconstructions. There was 1 case with a mandibular ramus complex and hard-to-treat fracture. Conclusions: The planning of the implant mostly relies on hard tissue three-dimensional reconstruction, but it should not be limited at what is immediately evident. A surgeon’s clinical experience should always guide the process, with knowledge of the patient’s anatomy and evaluation of the quality and of the soft tissue response being taken into consideration. The implant should always be tailored not only based on the bone defect and evaluations but also using the patient’s previewed and actual anatomy, evaluating eventual interferences and pitfalls.

      • SCISCIESCOPUS

        The Human F-Box DNA Helicase FBH1 Faces Saccharomyces cerevisiae Srs2 and Postreplication Repair Pathway Roles

        Chiolo, Irene,Saponaro, Marco,Baryshnikova, Anastasia,Kim, Jeong-Hoon,Seo, Yeon-Soo,Liberi, Giordano American Society for Microbiology 2007 Molecular and cellular biology Vol.27 No.21

        <B>ABSTRACT</B><P>The<I>Saccharomyces cerevisiae</I>Srs2 UvrD DNA helicase controls genome integrity by preventing unscheduled recombination events. While Srs2 orthologues have been identified in prokaryotic and lower eukaryotic organisms, human orthologues of Srs2 have not been described so far. We found that the human F-box DNA helicase hFBH1 suppresses specific recombination defects of<I>S. cerevisiae srs2</I>mutants, consistent with the finding that the helicase domain of hFBH1 is highly conserved with that of Srs2. Surprisingly, hFBH1 in the absence of<I>SRS2</I>also suppresses the DNA damage sensitivity caused by inactivation of postreplication repair-dependent functions leading to PCNA ubiquitylation. The F-box domain of hFBH1, which is not present in Srs2, is crucial for hFBH1 functions in substituting for Srs2 and postreplication repair factors. Furthermore, our findings indicate that an intact F-box domain, acting as an SCF ubiquitin ligase, is required for the DNA damage-induced degradation of hFBH1 itself. Overall, our findings suggest that the hFBH1 helicase is a functional human orthologue of budding yeast Srs2 that also possesses self-regulation properties necessary to execute its recombination functions.</P>

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