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Although standardization has been shown to improve patient safety and improve the efficiency of workflows, implementation of standards can take considerable effort and requires the engagement of all clinical stakeholders. Engaging team members includes increasing awareness of the proposed benefit of the standard, a clear implementation plan, monitoring for improvements, and open communication to support successful implementation. The benefits of standardization often focus on large institutions to improve research endeavors, yet all clinics can benefit from standardization to increase quality and implement more efficient or automated workflow. The benefits of nomenclature standardization for all team members and institution sizes, including success stories, are discussed with practical implementation guides to facilitate the adoption of standardized nomenclature in radiation oncology., Competing Interests: Disclosures Susan L. Richardson is Deputy Editor for the Journal of Applied Clinical Medical Physics. Walter R. Bosch reports grant from National Cancer Institute (NCI) (U24 CA 189893); Charles S. Mayo if Chair of American Association of Physicists in Medicine (AAPM) SC-263 and the Big Data Subcommittee. Todd R. McNutt is Chairman of the board of Oncospace and holds founder shares of Common Stock. Jean M. Moran reports software licensed to Fuse Oncology and grants or contracts from the National Institutes of Health (NIH), NCI, and Blue Cross Blue Shield of Michigan. Richard A. Popple reports honoraria and research support from Varian Medical Systems and also receives royalties for the University of Alabama at Birmingham Research Foundation. Ying Xiao reports no conflicts. Elizabeth L. Covington is the Chair of AAPM Task Group TG-263U1., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

The ability to introduce non-canonical amino acids into peptides and proteins is facilitated by working within in vitro translation systems. Non-canonical amino acids can be introduced into these systems using sense codon reprogramming, stop codon suppression, and by breaking codon degeneracy. Here, we review how these techniques have been used to create proteins with novel properties and how they facilitate sophisticated studies of protein function. We also discuss how researchers are using in vitro translation experiments with non-canonical amino acids to explore the tolerance of the translation apparatus to artificial building blocks. Finally, we give several examples of how non-canonical amino acids can be combined with mRNA-displayed peptide libraries for the creation of protease-stable, macrocyclic peptide libraries for ligand discovery., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Protein methylation and acetylation play important roles in biological processes, and misregulation of these modifications is involved in various diseases. Therefore, it is critical to understand the activities of the enzymes responsible for these modifications. Herein we describe a sensitive method for ratiometric quantification of methylated and acetylated peptides via MALDI-MS by direct spotting of enzymatic methylation and acetylation reaction mixtures without tedious purification procedures. The quantifiable detection limit for peptides with our method is approximately 10 fmol. This is achieved by increasing the signal-to-noise ratio through the addition of NH4H2PO4 to the matrix solution and reduction of the matrix α-cyanohydroxycinnamic acid concentration to 2 mg/ml. We have demonstrated the application of this method in enzyme kinetic analysis and inhibition studies. The unique feature of this method is the simultaneous quantification of multiple peptide species for investigation of processivity mechanisms. Its wide buffer compatibility makes it possible to be adapted to investigate the activity of any protein methyltransferase or acetyltransferase., (Copyright © 2015 Elsevier Inc. All rights reserved.)

Many different proteins associated with the cell cycle, including cyclins, cyclin-dependent kinases, and proto-oncogenes such as c-MYC (MYC), are increased in degenerating neurons. Consequently, an ectopic activation of the cell cycle machinery in neurons has emerged as a potential pathogenic mechanism of neuronal dysfunction and death in many neurodegenerative diseases, including Alzheimer's disease. However, the exact role of cell cycle re-entry during disease pathogenesis is unclear, primarily because of the lack of relevant research models to study the effects of cell cycle re-entry on mature neurons in vivo. To address this issue, we developed a new transgenic mouse model in which forebrain neurons (CaMKII-MYC) can be induced to enter the cell cycle using the physiologically relevant proto-oncogene MYC to drive cell cycle re-entry. We show that such cell cycle re-entry results in neuronal cell death, gliosis, and cognitive deficits. These findings provide compelling evidence that dysregulation of cell cycle re-entry results in neurodegeneration in vivo. Our current findings, coupled with those of previous reports, strengthen the hypothesis that neurodegeneration in Alzheimer's disease, similar to cellular proliferation in cancer, is a disease that results from inappropriate cell cycle control.