[Proteinopathies--forms of neurodegenerative disorders with protein aggregation-based pathology].
A number of neurodegenerative disorders have recently been coalesced into a group of proteinopathies because of the similarity of molecular mechanisms underlying their pathogenesis. A key step in the development of proteinopathies is a structural change that triggers aggregation of proteins, which are intrinsically prone to form aggregates due to their physical and chemical properties. Present review is devoted to the recent progress in the field of proteinopathies with specific focus on properties of aggregate-prone proteins, main stages of the development of molecular pathology and the role of cellular clearance systems in progression of neurodegeneration. Recent modifications in the nomenclature of neurodegenerative diseases will also be addressed.
T A
TA
Shelkovnikova
A A
AA
Kulikova
F O
FO
Tsvetkov
O
O
Peters
S O
SO
Bachurin
V L
VL
Bukhman
N N
NN
Ninkina
D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000378:metabolism; D001343:Autophagy; D006801:Humans; D019636:Neurodegenerative Diseases / Q000145:classification / Q000378:metabolism* / Q000503:physiopathology; D018384:Oxidative Stress; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D057165:Proteostasis Deficiencies / Q000145:classification / Q000378:metabolism* / Q000503:physiopathology; D017382:Reactive Oxygen Species / Q000378:metabolism; D009626:Terminology as Topic; D013997:Time Factors; D025801:Ubiquitin / Q000378:metabolism
D058227:Amyloidogenic Proteins; D017382:Reactive Oxygen Species; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex