Linked Life Data

21269829

Source:http://linkedlifedata.com/resource/pubmed/id/21269829

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-2-7
pubmed:abstractText
Ero1p, using molecular oxygen as its preferred terminal electron acceptor, promotes disulfide bond formation by interaction with protein disulfide isomerase. Dysfunction of Ero1p leads to strong activation of the unfolded protein response and marked loss of cell viability. However, modest attenuation of Ero1p improves the fitness of yeast challenged with high levels of protein misfolding in their endoplasmic reticulum stress. Partial inhibition of Ero1p is hence of great significance. In the present paper, a docking-based virtual screening method was performed to identify inhibitors of Ero1p and 12 hits were successfully obtained from 81 purchased compounds with micromolar inhibition against Ero1p. Particularly, six of the hits demonstrated remarkable potency with IC(50)<30?M and held the prospect of becoming lead compounds. Then the interaction modes were analyzed for further lead optimization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1464-3405
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1118-21
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Identification of small molecular inhibitors for Ero1p by structure-based virtual screening.
pubmed:affiliation
Department of Pharmaceutical Sciences, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't