Source:http://linkedlifedata.com/resource/pubmed/id/15272267
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2004-7-23
|
pubmed:abstractText |
Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases are increasingly being realized to have common cellular and molecular mechanisms including protein aggregation and inclusion body formation. The aggregates usually consist of fibers containing misfolded protein with a beta-sheet conformation, termed amyloid. There is partial but not perfect overlap among the cells in which abnormal proteins are deposited and the cells that degenerate. The most likely explanation is that inclusions and other visible protein aggregates represent an end stage of a molecular cascade of several steps, and that earlier steps in the cascade may be more directly tied to pathogenesis than the inclusions themselves. For several diseases, genetic variants assist in explaining the pathogenesis of the more common sporadic forms and developing mouse and other models. There is now increased understanding of the pathways involved in protein aggregation, and some recent clues have emerged as to the molecular mechanisms of cellular toxicity. These are leading to approaches toward rational therapeutics.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/HD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hdh protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/polyglutamine
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1078-8956
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
10 Suppl
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
S10-7
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:15272267-Amyloid beta-Peptides,
pubmed-meshheading:15272267-Animals,
pubmed-meshheading:15272267-Humans,
pubmed-meshheading:15272267-Inclusion Bodies,
pubmed-meshheading:15272267-Mice,
pubmed-meshheading:15272267-Models, Biological,
pubmed-meshheading:15272267-Nerve Tissue Proteins,
pubmed-meshheading:15272267-Neurodegenerative Diseases,
pubmed-meshheading:15272267-Nuclear Proteins,
pubmed-meshheading:15272267-Peptides,
pubmed-meshheading:15272267-Protein Folding,
pubmed-meshheading:15272267-Protein Structure, Secondary,
pubmed-meshheading:15272267-Ubiquitin
|
pubmed:year |
2004
|
pubmed:articleTitle |
Protein aggregation and neurodegenerative disease.
|
pubmed:affiliation |
Division of Neurobiology, Department of Psychiatry, Johns Hopkins University School of Medicine, Ross Research Building, Room 618, 720 Rutland Avenue, Baltimore, Maryland 21205, USA. caross@jhu.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|