Linked Life Data

18038971

Source:http://linkedlifedata.com/resource/pubmed/id/18038971

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
2007-12-20
pubmed:abstractText
Peptidyl-prolyl cis-trans isomerases are a group of cytosolic enzymes initially characterized by their ability to catalyze the cis-trans isomerization of peptidyl-prolyl bonds. This represents a significant event for protein folding because cis-proline introduces critical bends within the protein conformation. FK506-binding proteins (FKBPs) represent one of the three families of enzymes sharing peptidyl-prolyl cis-trans isomerase activity. Inhibitors of FKBP12, in particular, have potent neurotrophic properties both in vivo and in vitro. Here, we describe a fragment-based unbiased nuclear magnetic resonance drug discovery approach for the identification of novel classes of chemical inhibitors against FKBP12. Compared to FK506, the fragment-based FKBP12 inhibitors developed herein possess significant advantages as drug candidates.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6607-17
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Nuclear magnetic resonance fragment-based identification of novel FKBP12 inhibitors.
pubmed:affiliation
Infectious and Inflammatory Disease Center, Burnham Institute for Medical Research, and University of California at San Diego, Division of Biological Sciences, 9500 Gilman Drive, La Jolla, California 92093, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, N.I.H., Extramural