PubMed · 9540596
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M C Miller. 1995. Expanding dental practices with computer technology.. https://pubmed.ncbi.nlm.nih.gov/9540596/
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A contoured elastic-membrane microvalve is presented that enables integrated microfluidic processing at the network level. This method takes advantage of two ideas to improve performance: flexible elastic membranes (which enable high-performance shutoff and reduced footprint), and three-dimensionally contoured valve geometries (which reduce dead volume, improve fluidic priming, and reduce susceptibility to cavitation at high fluid velocities). We describe the use of laser-induced etching for microfluidic manifold fabrication, discuss the nonlinear load-deflection behavior of elastic membranes that can occur below 30 psi, and present flow-rate data for microvalves under inlet pressures of 0-20 psi with zero applied membrane pressure. Valve-closure data for inlet pressures of 0-30 psi are presented for fully assembled microvalve structures. The microvalve structures under test were capable of turning off flows of > 20 microL/s. These flow rates were shown to be limited by inlet and outlet flow resistances and not by the valve structure itself, so that higher maximum flow rate capabilities should be readily achieved.
X-ray diffraction studies as well as structure-activity relationships indicate that the central part of class I major histocompatibility complex (MHC)-binding nonapeptides represents the main interaction site for a T cell receptor. In order to rationally manipulate T cell epitopes, three nonpeptidic spacers have been designed from the x-ray structure of a MHC-peptide complex and substituted for the T cell receptor-binding part of several antigenic peptides. The binding of the modified epitopes to the human leukocyte antigen-B*2705 protein was studied by an in vitro stabilization assay, and the thermal stability of all complexes was examined by circular dichroism spectroscopy. Depending on their chemical nature and length, the introduced spacers may be classified into two categories. Monofunctional spacers (11-amino undecanoate, (R)-3-hydroxybutyrate trimer) simply link two anchoring peptide positions (P3 and P9) but loosely contact the MHC binding groove and thus decrease more or less the affinity of the altered epitopes to human leukocyte antigen-B*2705. A bifunctional spacer ((R)-3-hydroxybutyrate tetramer) not only bridges the two distant anchoring amino acids but also strongly interacts with the binding cleft and leads to a 5-fold increase in binding to the MHC protein. To our knowledge, this is the first report of a nonpeptidic modification of T-cell receptor binding residues that significantly enhances the binding of altered peptide ligands to their host MHC protein. The presented modified ligands constitute interesting tools for perturbing the T cell response to the parent antigenic peptide.
BACKGROUND: Recent technologic innovations have created possibilities for restorative dentistry, such as computer-aided design and computer-aided manufacturing (CAD/CAM). PURPOSE: This article presents a new CAD/CAM process that has been developed for the fabrication of dental restorations. METHODS: This process uses an improved imaging technique, successfully applied in other industries. Imaging is accomplished with 2-dimensional line grids projected onto an object, which allows for a mathematical reproduction of prepared and unprepared tooth surfaces, including those that are outside the direct line of light. The relative position of the sensor to the surface of the object is controlled automatically. CONCLUSIONS: This system, which is undergoing clinical testing, allows the generation of various types of highly accurate dental restorations (inlays, onlays, crown, and fixed partial dentures) from a number of different materials. Acquired digitized data points are directly translated from the sensor to the electronic controls of the milling machine to provide various manufacturing possibilities, including copy milling and accurate reproduction of occlusal tooth surfaces in various materials.