Abstract
Alzheimer's disease (AD) is one of the most common neurological disorders with vast reaching worldwide prevalence. Research attempts to decipher what's happening to the human mind have shown that pathogenesis of AD is associated with misfolded protein intermediates displaying tertiary structure conformational changes eventually leading to forming large polymers of unwanted aggregates. The two hallmarks of AD pathological protein aggregates are extraneuronal β-amyloid (Aβ) based senile plaques and intraneuronal neurofibrillary tangles (NFTs). As such, AD is categorized as a protein misfolding neurodegenerative disease (PMND) . Therapeutic interventions interfering with the formation of these protein aggregates have been widely explored as potential pathways for thwarting AD progression. One such tactic is modulating the function of enzymes involved in the metabolic pathways leading to formation of these misfolded protein aggregates. Much evidence has shown that glycogen synthase kinase-3β (GSK-3β) plays a key role in hyperphosphorylation of tau protein leading eventually to its aggregation to form NFTs. Data presented hereby will display a plethora of information as to how to interfere with progression of AD through the route of GSK-3β activity control.
TY - JOUR
T1 - Personalized Medicine and Resurrected Hopes for the Management of Alzheimer's Disease: A Modular Approach Based on GSK-3β Inhibitors.
AU - Arafa,Reem K,
AU - Elghazawy,Nehal H,
PY - 2017/8/26/entrez
PY - 2017/8/26/pubmed
PY - 2018/4/24/medline
KW - Alzheimer’s disease
KW - Extraneuronal senile plaques
KW - GSK-3β inhibitors
KW - Intraneuronal neurofibrillary tangles
KW - Protein misfolding neurodegenerative disease
KW - Tau-hyperphosphorylation
SP - 199
EP - 224
JF - Advances in experimental medicine and biology
JO - Adv Exp Med Biol
VL - 1007
N2 - Alzheimer's disease (AD) is one of the most common neurological disorders with vast reaching worldwide prevalence. Research attempts to decipher what's happening to the human mind have shown that pathogenesis of AD is associated with misfolded protein intermediates displaying tertiary structure conformational changes eventually leading to forming large polymers of unwanted aggregates. The two hallmarks of AD pathological protein aggregates are extraneuronal β-amyloid (Aβ) based senile plaques and intraneuronal neurofibrillary tangles (NFTs). As such, AD is categorized as a protein misfolding neurodegenerative disease (PMND) . Therapeutic interventions interfering with the formation of these protein aggregates have been widely explored as potential pathways for thwarting AD progression. One such tactic is modulating the function of enzymes involved in the metabolic pathways leading to formation of these misfolded protein aggregates. Much evidence has shown that glycogen synthase kinase-3β (GSK-3β) plays a key role in hyperphosphorylation of tau protein leading eventually to its aggregation to form NFTs. Data presented hereby will display a plethora of information as to how to interfere with progression of AD through the route of GSK-3β activity control.
SN - 0065-2598
UR - https://www.unboundmedicine.com/medline/citation/28840559/Personalized_Medicine_and_Resurrected_Hopes_for_the_Management_of_Alzheimer's_Disease:_A_Modular_Approach_Based_on_GSK_3β_Inhibitors_
L2 - https://dx.doi.org/10.1007/978-3-319-60733-7_11
DB - PRIME
DP - Unbound Medicine
ER -
