Debonding of LDSVs utilising Er,Cr:YSGG laser irradiation with fractional technique: an in vitro study.

Background: The removal of porcelain laminate veneers with rotary instruments could be accompanied by microfractures because differentiation of the veneer from the dental structure and resin cement is not a highly selective procedure. This can lead to scratches and overheating of the enamel and patient discomfort. Therefore, this in vitro research aimed to examine the effectiveness of the 2790 nm Er,Cr:YSGG laser utilizing a fractional technique to debond lithium disilicate veneer.

The influence of pulse duration and exposure time of Er,Cr:YSGG laser on lithium disilicate laminate debonding, an study.

Problem Statement: Grinding restorations, such as veneers, with rotary instruments, is the conventional removal approach. It may be accompanied by micro-fractures that affect the adjacent healthy dental structures. Differentiation of the veneer from the dental structure, as well as the resin cement, is not a highly selective procedure when rotary instruments are used.

Crystal structure of DNA polymerase I from Thermus phage G20c.

This study describes the structure of DNA polymerase I from Thermus phage G20c, termed PolI_G20c. This is the first structure of a DNA polymerase originating from a group of related thermophilic bacteriophages infecting Thermus thermophilus, including phages G20c, TSP4, P74-26, P23-45 and phiFA and the novel phage Tth15-6. Sequence and structural analysis of PolI_G20c revealed a 3'-5' exonuclease domain and a DNA polymerase domain, and activity screening confirmed that both domains were functional.

Targeting Acute Myelogenous Leukemia Using Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on the 2-Hydroxypyrazolo[1,5-]pyridine Scaffold: SAR of the Aryloxyaryl Moiety.

In recent years, human dihydroorotate dehydrogenase inhibitors have been associated with acute myelogenous leukemia as well as studied as potent host targeting antivirals. Starting from MEDS433 (IC 1.2 nM), we kept improving the structure-activity relationship of this class of compounds characterized by 2-hydroxypyrazolo[1,5-]pyridine scaffold.

Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6.

This study describes the production, characterization and structure determination of a novel Holliday junction-resolving enzyme. The enzyme, termed Hjc_15-6, is encoded in the genome of phage Tth15-6, which infects Thermus thermophilus. Hjc_15-6 was heterologously produced in Escherichia coli and high yields of soluble and biologically active recombinant enzyme were obtained in both complex and defined media.