Linked Life Data

17163671

Source:http://linkedlifedata.com/resource/pubmed/id/17163671

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-12-13
pubmed:abstractText
A growing number of diseases have been associated with protein misfolding. Thus, strategies that use small molecules to adjust folding tendencies have therapeutic potential. However, progress in this area has been hampered by an insufficient description of the molecular underpinnings of protein instability within the cell. In a recent report, a chemical approach was taken to probe the mechanism by which Gaucher disease associated mutations in glucocerebrosidase destabilize that enzyme and lead to its destruction. These studies provide a blueprint for the design of "chemical chaperones" for the exploration of cellular protein homeostasis and the treatment of misfolding diseases.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1554-8937
pubmed:author
pubmed:issnType
Electronic
pubmed:day
23
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Reclamation of proteins from the cellular scrap heap.
pubmed:affiliation
Department of Pathology and the Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, Michigan 48109-2216, USA. gestwick@umich.edu
pubmed:publicationType
Journal Article, Comment, Review