Linked Life Data

21459576

Source:http://linkedlifedata.com/resource/pubmed/id/21459576

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2011-5-2
pubmed:abstractText
Purple acid phosphatases (PAPs) are binuclear metallohydrolases that have been isolated from various mammals, plants, fungi and bacteria. In mammals PAP activity is associated with bone resorption and can lead to bone metabolic disorders such as osteoporosis; thus human PAP is an attractive target to develop anti-osteoporotic drugs. Based on a previous lead compound and rational drug design, acyl derivatives of ?-aminonaphthylmethylphosphonic acid were synthesised and tested as PAP inhibitors. Kinetic analysis showed that they are good PAP inhibitors whose potencies improve with increasing acyl chain length. Maximum potency is reached when the number of carbons in the acyl chain is between 12 and 14. The most potent inhibitor of red kidney bean PAP is the dodecyl-derivative with K(ic)=5 ?M, while the most potent pig PAP inhibitor is the tetradecyl-derivative with K(ic)=8 ?M, the most potent inhibitor of a mammalian PAP yet reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1464-3405
pubmed:author
pubmed:copyrightInfo
Crown Copyright © 2011. Published by Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3092-4
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Synthesis, modelling and kinetic assays of potent inhibitors of purple acid phosphatase.
pubmed:affiliation
The University of Queensland, School of Chemistry and Molecular Biosciences, Brisbane, Qld 4072, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't