Publications by authors named "A Brevet"
Article Synopsis
- Postoperative pain after hip fractures can lead to longer hospital stays and increased risk of complications, making effective pain management crucial, especially in older adults who are more sensitive to opioids.
- A study was conducted where an audit and feedback intervention was implemented in an orthogeriatric unit to improve the use of acetaminophen as a first-line pain relief method compared to a conventional orthopedic unit that didn't use this intervention.
- Results showed a significant increase in patients receiving the optimal dose of acetaminophen after the intervention, which also led to better functional outcomes and shorter hospital stays for those patients.
The highly conserved aspartyl-, asparaginyl-, and lysyl-tRNA synthetases compose one subclass of aminoacyl-tRNA synthetases, called IIb. The three enzymes possess an OB-folded extension at their N terminus. The function of this extension is to specifically recognize the anticodon triplet of the tRNA.
View Article and Find Full Text PDFLysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate.
View Article and Find Full Text PDFThe putative human tumor suppressor gene FHIT (fragile histidine triad) (M. Ohta et al., Cell 84:587-597, 1996) encodes a protein behaving in vitro as a dinucleoside 5',5"'-P1,P3-triphosphate (Ap3A) hydrolase.
View Article and Find Full Text PDFIn Escherichia coli, lysyl-tRNA synthetase activity is encoded by either a constitutive lysS gene or an inducible one, lysU. The two corresponding enzymes could be purified at homogeneity from a delta lysU and a delta lysS strain, respectively. Comparison of the pure enzymes, LysS and LysU, indicates that, in the presence of saturating substrates, LysS is about twice more active than LysU in the ATP-PPi exchange as well as in the tRNALys aminoacylation reaction.
View Article and Find Full Text PDF