Toxic proteins in neurodegenerative disease.
A broad range of neurodegenerative disorders is characterized by neuronal damage that may be caused by toxic, aggregation-prone proteins. As genes are identified for these disorders and cell culture and animal models are developed, it has become clear that a major effect of mutations in these genes is the abnormal processing and accumulation of misfolded protein in neuronal inclusions and plaques. Increased understanding of the cellular mechanisms for disposal of abnormal proteins and of the effects of toxic protein accumulation on neuronal survival may allow the development of rational, effective treatment for these disorders.
Taylor
J Paul
JP
Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, Laboratory of Neurogenetics, National Institute on Aging, National Institutes of Health, Bethesda, MD 20892, USA. taylorjp@ninds.nih.gov
Hardy
John
J
Fischbeck
Kenneth H
KH
D000544:Alzheimer Disease / Q000235:genetics / Q000378:metabolism / Q000473:pathology / Q000628:therapy; D000690:Amyotrophic Lateral Sclerosis / Q000235:genetics / Q000378:metabolism / Q000473:pathology / Q000628:therapy; D000818:Animals; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism; D009154:Mutation; D019636:Neurodegenerative Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology / Q000628:therapy; D009474:Neurons / Q000378:metabolism* / Q000473:pathology; D010300:Parkinson Disease / Q000235:genetics / Q000378:metabolism / Q000473:pathology / Q000628:therapy; D010455:Peptides / Q000235:genetics / Q000378:metabolism; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology / Q000628:therapy; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D024801:Tauopathies / Q000378:metabolism / Q000473:pathology / Q000628:therapy; D019680:Trinucleotide Repeat Expansion
D010455:Peptides; D011506:Proteins; C097188:polyglutamine