Evolutionary and Functional Analysis of Monoamine Oxidase F (MAO F): A Novel Member of the MAO Gene Family.

The monoamine oxidase (MAO) gene family encodes for enzymes that perform the oxidative deamination of monoamines, a process required to degrade norepinephrine, serotonin, dopamine, and other amines. While mammalian MAO enzymes, MAO A and MAO B, have been extensively studied, the molecular properties of the other family members are only partly uncovered. This study aims to explore the evolution of monoamine oxidases, emphasizing understanding the MAO gene repertoire among vertebrates.

Spinal Dumbbell Meningiomas: A Systematic Review.

Aim: This systematic review aims to synthesize the epidemiology, clinical presentation, diagnostic approaches, treatment strategies, and outcomes of spinal dumbbell meningiomas to enhance understanding and improve patient management.

Methods: Following Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) guidelines, four major databases (PubMed, Scopus, Web of Science, and Cochrane Library) were searched until June 2024. Studies included patients diagnosed with spinal dumbbell intradural-extradural meningiomas, focusing on patient demographics, tumor characteristics, diagnostic methods, treatment modalities, and clinical outcomes.

Role of gliflozins on hepatocellular carcinoma progression: a systematic synthesis of preclinical and clinical evidence.

Introduction: The risk of HCC is twice as high in diabetic patients compared to non-diabetic ones, suggesting that diabetes advances carcinogenesis in the liver through a variety of mechanisms. Sodium-glucose cotransporter 2 inhibitors (SGLT2i) have been shown to improve liver outcomes, emerging as promising agents to treat hepatocellular carcinoma (HCC) in patients with type 2 diabetes mellitus (T2DM).

Methods: We searched PubMed and Scopus databases for articles presenting an association between SGLT2is and HCC to explore the putative mechanisms of action underlying the anti-proliferative activity of SGLT2is.

Altering substrate specificity of a thermostable bacterial monoamine oxidase by structure-based mutagenesis.

Bacterial monoamine oxidases (MAOs) are FAD-dependent proteins catalyzing a relevant reaction for many industrial biocatalytic applications, ranging from production of enantiomerically pure building blocks for pharmaceutical synthesis to biosensors for monitoring food and beverage quality. The thermostable MAO enzyme from Thermoanaerobacterales bacterium (MAO) is about 36 % identical to both putrescine oxidase and human MAOs and can be efficiently produced in Escherichia coli. MAO preferentially acts on n-alkyl monoamines but shows detectable activity also on polyamines and aromatic monoamines.