<p>With 60–70% of all occurrences of dementia, Alzheimer’s disease (AD), an advancing neurological illness, is one of the most frequent causes of dementia. Even though the exact etiology of AD is still unidentified, persons who have the disease have been found to have a number of abnormalities in their brains. Apart from the buildup of amyloid-β plaques inside the brain tissue, it has been demonstrated that abnormal tau protein phosphorylation increases the risk of neuronal death. The discovery of dual-specificity tyrosine phosphorylation-regulated kinase 1A (<i>DYRK1A</i>) is becoming increasingly significant in the fight to create efficacious Alzheimer’s disease (AD) therapies. The pathophysiology of AD, which includes the creation of amyloid plaques and tau hyperphosphorylation, is intimately connected with the dysregulation of <i>DYRK1A</i>, which is essential for neurodevelopment and cognitive function. In addition to amyloid plaques, <i>DYRK1A</i> phosphorylates tau on 11 distinct Ser/Thr residues, forming aggregates known as “neurofibrillary tangles” that may be the cause of dementia, neuronal degeneration, and cell death. Therefore, targeting <i>DYRK1A</i> with small molecules may be a promising therapy strategy for Alzheimer’s and other neurodegenerative illnesses. This study examines the therapeutic potential of <i>DYRK1A</i> inhibitors in AD and offers a thorough explanation of the molecular pathways through which <i>DYRK1A</i> promotes the development of the illness.</p> Graphical Abstract <p><i>DYRK1A</i> antagonist against neuronal cell damage</p> <p></p>