Identification of catechols as histone-lysine demethylase inhibitors
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Identification of catechols as histone-lysine demethylase inhibitors. / Nielsen, Anders L; Kristensen, Line H; Stephansen, Karen B; Kristensen, Jan B L; Helgstrand, Charlotte; Lees, Michael; Cloos, Paul; Helin, Kristian; Gajhede, Michael; Olsen, Lars.
In: F E B S Letters, Vol. 586, No. 8, 2012, p. 1190-4.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Identification of catechols as histone-lysine demethylase inhibitors
AU - Nielsen, Anders L
AU - Kristensen, Line H
AU - Stephansen, Karen B
AU - Kristensen, Jan B L
AU - Helgstrand, Charlotte
AU - Lees, Michael
AU - Cloos, Paul
AU - Helin, Kristian
AU - Gajhede, Michael
AU - Olsen, Lars
N1 - Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
PY - 2012
Y1 - 2012
N2 - Identification of inhibitors of histone-lysine demethylase (HDM) enzymes is important because of their involvement in the development of cancer. An ELISA-based assay was developed for identification of inhibitors of the HDM KDM4C in a natural products library. Based on one of the hits with affinity in the low µM range (1, a catechol), a subset of structurally related compounds was selected and tested against a panel of HDMs. In this subset, two inhibitors (2 and 10) had comparable affinities towards KDM4C and KDM6A but no effect on PHF8. One inhibitor restored H3K9me3 levels in KDM4C transfected U2-OS cells.
AB - Identification of inhibitors of histone-lysine demethylase (HDM) enzymes is important because of their involvement in the development of cancer. An ELISA-based assay was developed for identification of inhibitors of the HDM KDM4C in a natural products library. Based on one of the hits with affinity in the low µM range (1, a catechol), a subset of structurally related compounds was selected and tested against a panel of HDMs. In this subset, two inhibitors (2 and 10) had comparable affinities towards KDM4C and KDM6A but no effect on PHF8. One inhibitor restored H3K9me3 levels in KDM4C transfected U2-OS cells.
U2 - 10.1016/j.febslet.2012.03.001
DO - 10.1016/j.febslet.2012.03.001
M3 - Journal article
C2 - 22575654
VL - 586
SP - 1190
EP - 1194
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 8
ER -
ID: 38187819