The neonatal Fc receptor (FcRn) is a heterodimeric protein encoded by the FCGRTgene, consisting of a heavy chain and a light chain (β₂-microglobulin) associated non-covalently. Its heavy chain, structurally similar to MHC class I molecules, comprises a cytoplasmic tail, a transmembrane domain, and three extracellular functional segments (α₁, α₂, α₃). Together with the light chain, these segments form the ligand-binding site for FcRn. FcRn is widely expressed in the body, found in various cell types (e.g., epithelial cells), secondary lymphoid organs (e.g., spleen), and tissues like the placenta.

In recent years, the role of RNA-binding proteins in gene expression regulation has become increasingly prominent. The CPEB (cytoplasmic polyadenylation element binding protein) family, as core proteins regulating mRNA translation, localization, and stability, is emerging as a hotspot in neuroscience and translational medicine research due to its critical roles in synaptic plasticity, long-term memory formation, and various neuropsychiatric disorders. CPEB family members, especially their unique prion-like domains, provide a novel perspective for understanding the mechanisms of memory persistence and treating related diseases. This article will systematically elaborate on the functional mechanisms of the CPEB family and their central roles in the nervous system, from development and functional maintenance to the pathogenesis of diseases.

In drug development and clinical practice, the rate at which a drug is eliminated from the human body directly determines its therapeutic efficacy and safety profile. A key group of proteins governing this process is the CYP3A family of drug-metabolizing enzymes. Among these, CYP3A4 is the most highly expressed enzyme in the human liver and mediates the oxidative metabolism of a large percentage of widely prescribed medications. Consequently, drug exposure levels, treatment duration, and the risk of drug–drug interactions (DDIs) are all strongly associated with CYP3A4 functional activity

What is Cystic Fibrosis? Introduction to CFTR and Disease Association​ Cystic fibrosis (CF) is a rare autosomal recessive disorder caused by mutations in the CFTR gene located on chromosome 7 (7q31.1). The CFTR protein functions as a chloride channel critical for maintaining fluid balance across epithelial surfaces. Defects in CFTR lead to abnormal ion transport, resulting in thickened mucus in multiple organs. Pulmonary manifestations—such as chronic airway obstruction and recurrent infections—are the most life-threatening features of CF and directly stem from CFTR dysfunction.

In 2024, Biogen announced that its antisense oligonucleotide drug Tofersen met the primary endpoint in a Phase III clinical trial for SOD1-mutated amyotrophic lateral sclerosis (ALS). This achievement, published in the New England Journal of Medicine, marks the entry of SOD1-targeted therapeutic strategies into a new clinical stage, demonstrating that reducing mutant SOD1 protein levels via intrathecal administration can significantly delay disease progression.