Linked Life Data

20166961

Source:http://linkedlifedata.com/resource/pubmed/id/20166961

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-4-8
pubmed:abstractText
Intra- and extracellular protein misfolding and aggregation is likely to contribute to a number of age-related central nervous system diseases ("proteinopathies"). Therefore, molecular chaperones, such as heat shock proteins (HSPs), that regulate protein folding, misfolding and adaption to cellular stress are emerging as therapeutic targets. Here we review the current knowledge of HSP-modulating drugs and discuss the opportunities and difficulties of their therapeutic use to treat proteinopathies such as Alzheimer's- and Parkinson's disease, the polyglutamine- and prion disorders and Amyotrophic Lateral Sclerosis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1873-4316
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
198-215
pubmed:dateRevised
2010-8-31
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Heat shock proteins: therapeutic drug targets for chronic neurodegeneration?
pubmed:affiliation
Southampton Neuroscience Group, School of Biological Sciences, University of Southampton, Boldrewood Campus, Basset Crescent East, Southampton SO16 7PX, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't