Ask about this productRelated genes to: NANS antibody
- Gene:
- NANS NIH gene
- Name:
- N-acetylneuraminate synthase
- Previous symbol:
- -
- Synonyms:
- SAS
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-12-16
- Date modifiied:
- 2018-07-06
Related products to: NANS antibody
Related articles to: NANS antibody
- Despite increasing representation of women in medicine overall, significant gender disparities persist in procedural specialties such as interventional pain medicine. Women remain underrepresented as speakers at national pain conferences and in leadership roles. Additionally, a pay gap between female and male pain physicians remains. This study aims to objectively demonstrate the above-mentioned inequities. - Source: PubMed
Catalanotto MarissaKim Serena JiyeonJaved Saba - Bone loss-related disorders, driven by impaired osteoblast activity, pose a growing global health challenge, yet current anabolic therapies remain limited due to an incomplete understanding of osteoblast dysfunction. Emerging evidence suggests that lactate-derived lysine lactylation-a glycolysis-linked PTM-may regulate osteoblast differentiation and bone homeostasis, though its landscape and functional impact in osteoblasts are largely unknown. Here, we integrated multi-omics profiling, Mendelian randomization (MR), and computational modeling to investigate lactylation-mediated osteogenic regulation. Using osteoblast models, we mapped dynamic proteomic and lactylome changes during differentiation, identifying 43 key proteins with concurrent alterations in expression and lactylation. Integrated MR analysis of human genetic data identified NANS and SPTLC1 as causal regulators of bone mineral density. Molecular dynamics simulations revealed lactylation-driven functional remodeling of these proteins, and network pharmacology suggested FDA-approved compounds (e.g., Suramin sodium and Paritaprevir) as potential osteogenic agents. This study advances mechanistic understanding of osteogenesis and provides a framework for discovering small molecules that mimic lactylation-induced conformational changes for drug repurposing in clinical applications. - Source: PubMed
Publication date: 2026/02/06
Chen RuijingGe SiliangChang FeifanChen MingLi YiLi YihuiYou DeshengTang PeifuYin Pengbin - HIV-1 integrase (IN) promotes encapsulation of viral genomic RNA into mature viral cores, and this function is a target for ongoing antiretroviral drug development efforts. Here we determined the cryogenic electron microscopy (cryo-EM) structure of a primate lentiviral IN in a complex with RNA, revealing a linear filament made of IN octamer repeat units, each comprising a pair of asymmetric homotetramers. The assembly is stabilized through IN-RNA interactions involving mainly the IN C-terminal domains and RNA backbone. The spacing and orientation of the IN filament repeat units closely matched those of consecutive capsid (CA) hexamers within the mature CA lattice. Using cryo-EM images of native purified HIV-1 cores, we refined the structure of the IN filament as it propagates along the luminal side of the CA lattice. Each IN tetramer within the filament nestled in a CA hexamer, engaging closely with the major homology regions. Substitutions of residues involved in IN-CA contacts yielded eccentric virions with RNA nucleoids located outside of the cores. Collectively, our results establish the structural basis for the HIV-1 IN-RNA interaction and reveal that IN forms an RNA-binding module on the luminal side of the mature CA lattice. - Source: PubMed
Publication date: 2026/02/18
Singer Matthew RLi ZhenRey Juan SHope JoshuaChenavier FlorianCook Nicola JPunch EmmaSmith JamieZhou ZhiyuMaslen SarahMasino LauraNans AndreaSkehel MarkTaylor Ian AZanetti GiuliaZhang PeijunPerilla Juan REngelman Alan NCherepanov Peter - : The global population is ageing rapidly, with projections indicating that there will be over two billion individuals aged ≥60 years by 2050. Sarcopenia and frailty are major age-related syndromes associated with loss of muscle mass, reduced strength, and increased vulnerability, for which adequate protein and amino acid intake are key preventive factors. However, nationally representative data on dietary amino acid intakes and sources among older adults are lacking, particularly in Europe. : This study aimed to address this gap by updating the Irish Food Composition Database (IFCD) (2011) with amino acid composition data and estimating amino acid intakes and dietary sources in older adults in Ireland (≥65 years) using data from the National Adult Nutrition Survey (2008-2010; n = 226). : Mean total amino acid intake was 76.2 g/day (1.0 g/kg body weight/day). Intakes of all essential amino acids were above the US Institute of Medicine (IOM) recommendations, with no significant differences observed between sexes or age groups (65-74 y, 75+ y). 'Meat and meat dishes' were the principal contributors to amino acid intake (28-47%), followed by 'breads and rolls', 'milk and yoghurt', and 'fish and fish dishes'. : This study provides the first nationally representative estimates of amino acid intakes in older adults in Europe, establishing a baseline for future dietary surveillance and informing protein quality assessment amid dietary transitions toward plant-based foods. - Source: PubMed
Publication date: 2026/02/02
Burke AoifeO' Sullivan EmmaGiblin LindaNugent Anne PFlynn AlbertMcNulty Breige AKehoe LauraCallanan MichaelWalton Janette - Sialic acid (Sia) is essential for human physiology and health, as emphasized by the range of human diseases that is linked to abnormalities in the Sia pathway. Sias are typically found at the outermost part of glycoconjugates that are involved in several biological processes, including cell adhesion and signaling. Sia metabolism is key to the production of CMP-Sia, the building block for sialylation, and is targeted as a therapeutic strategy to ameliorate the effects of abnormal sialylation in disease. Interestingly, patients with different genetic defects in Sia metabolism show contrasting clinical symptoms affecting different tissues. For example, neurological symptoms are dominant in some congenital disorders of glycosylation (CDGs) like NANS-CDG, while the brain is unaffected in GNE myopathy which presents with isolated muscle symptoms. This suggests that more complex tissue-specific regulatory mechanisms may exist. In this review, we discuss the biosynthetic and genetic pathways in Sia metabolism with a specific focus on its role in brain, muscle, and platelets in health and genetic disease. Moreover, this review presents an overview of the clinical symptoms and genetic spectrum for each genetic disease. Overall, the molecular an biochemical profiles are not fully understood in these patients and effective therapies are limited. Therefore, additional research should focus on unravelling metabolic mechanisms that could be targeted to develop novel therapeutic strategies. - Source: PubMed
Publication date: 2026/02/06
Huang Sjanievan de Ven Eline G PTee TrishaLefeber Dirk J