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Structural Study of Membrane Glycoprotein-Precursor of β-Amyloid and Proteins Involved in Its Proteolysis

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CRYSTALLOGRAPHY REPORTS
卷 66, 期 5, 页码 737-750

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PLEIADES PUBLISHING INC
DOI: 10.1134/S1063774521050229

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  1. Russian Science Foundation [20-64-46027, 19-15-00427]
  2. Russian Science Foundation [20-64-46027, 19-15-00427] Funding Source: Russian Science Foundation

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Alzheimer's disease is a common neurodegenerative disease characterized by the degeneration of neurons in the cerebral cortex, leading to impaired cognitive perception and memory. Accumulation of amyloid peptide in the brain forms ordered strands known as amyloid plaques, which are key pathological features of the disease. These plaques are formed from the aggregation of beta-amyloid or Aβ peptides produced by the cleavage of membrane glycoprotein precursor by beta- and gamma-secretases in neurons' plasma membrane.
Alzheimer's disease is the most widespread form of neurodegenerative disease in the world. Its clinical manifestations are explained by selective degeneration of neurons in the portions of cerebral cortex responsible for cognitive perception and memory. Amyloid peptide is accumulated beyond nerve cells at neuron contact sites into ordered strands (fibrils), forming the so-called amyloid plaques. It is found that amyloid peptide (beta-amyloid or A beta(1-38)-A beta(1-43)), which aggregates and forms amyloid plaques in brain, is a product of successive cleavage of membrane glycoprotein-precursor of beta-amyloid by beta- and gamma-secretases in the plasmatic membrane of neurons. The results of structural studies of this process and the main proteins involved in it are considered.

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