File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Conference Paper: Identification of a polyoxometalate inhibitor of the DNA binding activity of sox2

TitleIdentification of a polyoxometalate inhibitor of the DNA binding activity of sox2
Authors
Issue Date2011
Citation
ACS Chemical Biology, 2011, v. 6, n. 6, p. 573-581 How to Cite?
AbstractAberrant expression of transcription factors is a frequent cause of disease, yet drugs that modulate transcription factor protein-DNA interactions are presently unavailable. To this end, the chemical tractability of the DNA binding domain of the stem cell inducer and oncogene Sox2 was explored in a high-throughput fluorescence anisotropy screen. The screening revealed a Dawson polyoxometalate (K 6 [P 2 Mo 18 O 62 ]) as a direct and nanomolar inhibitor of the DNA binding activity of Sox2. The Dawson polyoxometalate (Dawson-POM) was found to be selective for Sox2 and related Sox-HMG family members when compared to unrelated paired and zinc finger DNA binding domains. [ 15 N, 1 H]-Transverse relaxation optimized spectroscopy (TROSY) experiments coupled with docking studies suggest an interaction site of the POM on the Sox2 surface that enabled the rationalization of its inhibitory activity. The unconventional molecular scaffold of the Dawson-POM and its inhibitory mode provides strategies for the development of drugs that modulate transcription factors. © 2011 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/253145
ISSN
2023 Impact Factor: 3.5
2023 SCImago Journal Rankings: 1.344
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorNarasimhan, Kamesh-
dc.contributor.authorPillay, Shubhadra-
dc.contributor.authorBin Ahmad, Nor Rizal-
dc.contributor.authorBikadi, Zsolt-
dc.contributor.authorHazai, Eszter-
dc.contributor.authorYan, Li-
dc.contributor.authorKolatkar, Prasanna R.-
dc.contributor.authorPervushin, Konstantin-
dc.contributor.authorJauch, Ralf-
dc.date.accessioned2018-05-11T05:38:43Z-
dc.date.available2018-05-11T05:38:43Z-
dc.date.issued2011-
dc.identifier.citationACS Chemical Biology, 2011, v. 6, n. 6, p. 573-581-
dc.identifier.issn1554-8929-
dc.identifier.urihttp://hdl.handle.net/10722/253145-
dc.description.abstractAberrant expression of transcription factors is a frequent cause of disease, yet drugs that modulate transcription factor protein-DNA interactions are presently unavailable. To this end, the chemical tractability of the DNA binding domain of the stem cell inducer and oncogene Sox2 was explored in a high-throughput fluorescence anisotropy screen. The screening revealed a Dawson polyoxometalate (K 6 [P 2 Mo 18 O 62 ]) as a direct and nanomolar inhibitor of the DNA binding activity of Sox2. The Dawson polyoxometalate (Dawson-POM) was found to be selective for Sox2 and related Sox-HMG family members when compared to unrelated paired and zinc finger DNA binding domains. [ 15 N, 1 H]-Transverse relaxation optimized spectroscopy (TROSY) experiments coupled with docking studies suggest an interaction site of the POM on the Sox2 surface that enabled the rationalization of its inhibitory activity. The unconventional molecular scaffold of the Dawson-POM and its inhibitory mode provides strategies for the development of drugs that modulate transcription factors. © 2011 American Chemical Society.-
dc.languageeng-
dc.relation.ispartofACS Chemical Biology-
dc.titleIdentification of a polyoxometalate inhibitor of the DNA binding activity of sox2-
dc.typeConference_Paper-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/cb100432x-
dc.identifier.pmid21344919-
dc.identifier.scopuseid_2-s2.0-79961094533-
dc.identifier.volume6-
dc.identifier.issue6-
dc.identifier.spage573-
dc.identifier.epage581-
dc.identifier.eissn1554-8937-
dc.identifier.isiWOS:000291896400007-
dc.identifier.issnl1554-8929-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats