Linked Life Data

18386295

Source:http://linkedlifedata.com/resource/pubmed/id/18386295

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-4-8
pubmed:abstractText
Human beta2-microglobulin (beta2-m) is a small amyloidogenic protein responsible for dialysis-related amyloidosis, which represents a severe complication of long-term hemodialysis. A therapeutic approach for this amyloidosis could be based on the stabilization of beta2-m through the binding to a small molecule, to possibly inhibit protein misfolding and amyloid fibril formation. The search of a strong ligand of this protein is extremely challenging: by using CE in affinity and refolding experiments we study the effect that previously selected sulfonated molecules have on the equilibrium between the native form and an ensemble of conformers populating the slow phase of beta2-m folding. These data are correlated with the effect that the same molecules exert on in vitro fibrillogenesis experiments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0173-0835
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1502-10
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Sulfonated molecules that bind a partially structured species of beta2-microglobulin also influence refolding and fibrillogenesis.
pubmed:affiliation
Department of Pharmaceutical Chemistry, School of Pharmacy, University of Pavia, Pavia, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't