Alzheimer's disease is a progressive neurodegenerative disorder caused by abnormal accumulation and aggregation of amyloid-β peptide which results in various toxic effects such as neurofibrillary tangles of hyperphosphorilated tau protein, increased concentration of reactive oxygen species, chronic inflammation and ionic disequilibrium, all of which ultimately lead to neuronal apoptosis and loss of synapses, thus causing dementia. The most important element of this disease is a disruption of cell proteostasis which is why molecular chaperones have shown to be one of the main factors in its pathophisiology. Molecular chaperones are proteins that are involved in many cellular events such as folding of newly synthesized and/or unfolded proteins, membrane translocation of macromolecules, unfolding of protein aggregates and maintining the function of many enzymes and receptors. Recently, many functions of chaperones in prevention and amelioration of the aggregation of amyloid proteins have been found. Furthermore, their role has been recognized in modulating the immune system, in reducing the concentration of reactive oxygen species and in preventing cell apoptosis directly. This is why many of new strategies of treating Alzheimer's disease are based on modulating the chaperone systems which could be a big step in curing this and many other neurodegenerative diseases. For these strategies to succeed, intensive research regarding mechanisms of chaperone function in the context of the chaperone network will have to be conducted. This would reveal a detailed role of these systems in Alzheimer's and other neurodegenerative diseases.