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- Biochemistry_of_Alzheimer's_disease abstract "The biochemistry of Alzheimer's disease (AD), one of the most common causes of adult dementia, is as yet not well understood. AD has been identified as a protein misfolding disease due to the accumulation of abnormally folded amyloid beta protein in the brains of Alzheimer's patients. Amyloid beta, also written Aβ, is a short peptide that is an abnormal proteolytic byproduct of the transmembrane protein amyloid precursor protein (APP), whose function is unclear but thought to be involved in neuronal development. The presenilins are components of proteolytic complex involved in APP processing and degradation.Amyloid beta monomers are soluble and contain short regions of beta sheet and polyproline II helix secondary structures in solution, though they are largely alpha helical in membranes; however, at sufficiently high concentration, they undergo a dramatic conformational change to form a beta sheet-rich tertiary structure that aggregates to form amyloid fibrils. These fibrils deposit outside neurons in dense formations known as senile plaques or neuritic plaques, in less dense aggregates as diffuse plaques, and sometimes in the walls of small blood vessels in the brain in a process called amyloid angiopathy or congophilic angiopathy.AD is also considered a tauopathy due to abnormal aggregation of the tau protein, a microtubule-associated protein expressed in neurons that normally acts to stabilize microtubules in the cell cytoskeleton. Like most microtubule-associated proteins, tau is normally regulated by phosphorylation; however, in AD patients, hyperphosphorylated tau accumulates as paired helical filaments that in turn aggregate into masses inside nerve cell bodies known as neurofibrillary tangles and as dystrophic neurites associated with amyloid plaques. Although little is known about the process of filament assembly, it has recently been shown that a depletion of a prolyl isomerase protein in the parvulin family accelerates the accumulation of abnormal tau.Neuroinflammation is also involved in the complex cascade leading to AD pathology and symptoms. Considerable pathological and clinical evidence documents immunological changes associated with AD, including increased pro-inflammatory cytokine concentrations in the blood and cerebrospinal fluid. Whether these changes may be a cause or consequence of AD remains to be fully understood, but inflammation within the brain, including increased reactivity of the resident microglia towards amyloid deposits, has been implicated in the pathogenesis and progression of AD.".
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- Biochemistry_of_Alzheimer's_disease subject Category:Alzheimer's_disease.
- Biochemistry_of_Alzheimer's_disease subject Category:Neurology.
- Biochemistry_of_Alzheimer's_disease subject Category:Pathology.
- Biochemistry_of_Alzheimer's_disease subject Category:Unsolved_problems_in_neuroscience.
- Biochemistry_of_Alzheimer's_disease type Abstraction100002137.
- Biochemistry_of_Alzheimer's_disease type Attribute100024264.
- Biochemistry_of_Alzheimer's_disease type Condition113920835.
- Biochemistry_of_Alzheimer's_disease type Difficulty114408086.
- Biochemistry_of_Alzheimer's_disease type Problem114410605.
- Biochemistry_of_Alzheimer's_disease type State100024720.
- Biochemistry_of_Alzheimer's_disease type UnsolvedProblemsInNeuroscience.
- Biochemistry_of_Alzheimer's_disease comment "The biochemistry of Alzheimer's disease (AD), one of the most common causes of adult dementia, is as yet not well understood. AD has been identified as a protein misfolding disease due to the accumulation of abnormally folded amyloid beta protein in the brains of Alzheimer's patients.".
- Biochemistry_of_Alzheimer's_disease label "Biochemistry of Alzheimer's disease".
- Biochemistry_of_Alzheimer's_disease label "アルツハイマー型認知症の生化学".
- Biochemistry_of_Alzheimer's_disease sameAs アルツハイマー型認知症の生化学.
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