The etiology of Alzheimer's dementia is, at best multifactorial. Before the emergence of cognitive impairment, symptoms such as thinning of the cortex, accumulation of β-amyloid, and decreased hippocampal volume are common. Hence, the accumulation of β-amyloid and hyperphosphorylated tau fibrillary tangles are two pathological hallmarks in Alzheimer's disease brains, but antibody therapy aimed to decrease β-amyloid has been a failure and, in most optimistic opinions, may delay somewhat disease progression. However, 31-38 % of subjects develop cerebral micro-hemorrhages in aducanumab therapy, an antibody to the amyloid beta plaque by Biogen. Genetics such as Apo E3/E3 have demonstrated defects in the blood-brain barrier in early-onset dementia. Late Onset Alzheimer’s Dementia, has implicated microbe cerebral infections and numerous genetic single nucleotide polymorphisms. However, several cellular biological signatures of Alzheimer's disease have been identified, such as synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies which are related to the actin cytoskeleton. Cofilin is one of the most affluent and common actin-binding proteins and plays a role in cell motility, migration, shape, and metabolism. They also play an important role in severing actin filament, nucleating, depolymerizing, and bundling activities. This review summarizes the structure of cofilins appearing after ATP interruptions and deficits in mitochondrial and microtubules and their functional and regulating roles, focusing on the synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies of Alzheimer's disease. These findings strengthen our hypothesis that Alzheimer’s dementia is characterized by “Quantum Decoherence” resulting from mitochondrial and microtubular deterioration and responding to near-infrared transcranial photobiomodulation to support mitochondrial and microtubule repair, regrowth and neuronal synaptic renormalization.