Linked Life Data

20221654

Source:http://linkedlifedata.com/resource/pubmed/id/20221654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-10-28
pubmed:abstractText
Assessing the difficulty of inhibiting a specific protein by a small molecule can be highly valuable in risk-assessment and prioritization of a new target. In particular, when the disease linkage for a number of targets is broadly similar, being able to identify the most tractable can have a significant impact on informing target selection. With an increasing focus against new and novel protein classes, being able to assess the most likely targets to yield lead-like chemical start points can guide the selection and the lead-generation strategy implemented. This study exploits protein-ligand docking studies on published protein x-ray crystal structures to provide guidance on the feasibility of identifying small molecule inhibitors against a range of targets.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0948-5023
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1833-43
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Using protein-ligand docking to assess the chemical tractability of inhibiting a protein target.
pubmed:affiliation
Cancer & Infection Discovery, AstraZeneca, Alderley Park, Macclesfield SK104TG, UK. richard.a.ward@astrazeneca.com
pubmed:publicationType
Journal Article