Global collaborations to change the paradigm of oral health education and care: 2024 ADEA Annual Session Chair of the Board Symposium, Proceedings.

The 2024 ADEA Annual Session Chair of the Board Symposium titled, Global Collaborations to Change the Paradigm in Oral Health Education and Care, aimed to highlight innovative global education models in oral health. The symposium sought to identify and explore opportunities for collaboration with international partners to ensure sustainable healthcare education to improve the oral health workforce. Additionally, it focused on discovering and adapting innovative solutions and best practices to enhance access to oral health services worldwide.

Clinical impact of UV mutational signatures in Veterans with cancer.

Background: UV-related DNA damage signature (UVsig) is highly specific for cutaneous cancers. The prevalence of UVsig among tumors without a primary site and tumors of extracutaneous origin were previously reported, suggesting potential misclassification of cancers. Our study aims to assess if the knowledge of UVsig at diagnosis would change first-line treatment recommendation.

Physiological and transcriptomic response to methyl-coenzyme M reductase limitation in .

Unlabelled: Methyl-coenzyme M reductase (MCR) catalyzes the final step of methanogenesis, the microbial metabolism responsible for nearly all biological methane emissions to the atmosphere. Decades of biochemical and structural research studies have generated detailed insights into MCR function , yet very little is known about the interplay between MCR and methanogen physiology. For instance, while it is routinely stated that MCR catalyzes the rate-limiting step of methanogenesis, this has not been categorically tested.

Identification of two archaeal GDGT lipid-modifying proteins reveals diverse microbes capable of GMGT biosynthesis and modification.

Archaea produce unique membrane-spanning lipids (MSLs), termed glycerol dialkyl glycerol tetraethers (GDGTs), which aid in adaptive responses to various environmental challenges. GDGTs can be modified through cyclization, cross-linking, methylation, hydroxylation, and desaturation, resulting in structurally distinct GDGT lipids. Here, we report the identification of radical SAM proteins responsible for two of these modifications-a glycerol monoalkyl glycerol tetraether (GMGT) synthase (Gms), responsible for covalently cross-linking the two hydrocarbon tails of a GDGT to produce GMGTs, and a GMGT methylase (Gmm), capable of methylating the core hydrocarbon tail.