Enzyme kinetic studies of histone demethylases KDM4C and KDM6A: Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases

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Standard

Enzyme kinetic studies of histone demethylases KDM4C and KDM6A : Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases. / Kristensen, Jan B L; Nielsen, Anders L; Jørgensen, Lars; Kristensen, Line Hyltoft; Helgstrand, Charlotte; Juknaite, Lina; Kristensen, Jesper Langgaard; Kastrup, Jette Sandholm; Clausen, Rasmus Prætorius; Olsen, Lars; Gajhede, Michael.

I: F E B S Letters, Bind 585, Nr. 12, 23.06.2011, s. 1951-1956.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Kristensen, JBL, Nielsen, AL, Jørgensen, L, Kristensen, LH, Helgstrand, C, Juknaite, L, Kristensen, JL, Kastrup, JS, Clausen, RP, Olsen, L & Gajhede, M 2011, 'Enzyme kinetic studies of histone demethylases KDM4C and KDM6A: Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases', F E B S Letters, bind 585, nr. 12, s. 1951-1956. https://doi.org/10.1016/j.febslet.2011.05.023

APA

Kristensen, J. B. L., Nielsen, A. L., Jørgensen, L., Kristensen, L. H., Helgstrand, C., Juknaite, L., Kristensen, J. L., Kastrup, J. S., Clausen, R. P., Olsen, L., & Gajhede, M. (2011). Enzyme kinetic studies of histone demethylases KDM4C and KDM6A: Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases. F E B S Letters, 585(12), 1951-1956. https://doi.org/10.1016/j.febslet.2011.05.023

Vancouver

Kristensen JBL, Nielsen AL, Jørgensen L, Kristensen LH, Helgstrand C, Juknaite L o.a. Enzyme kinetic studies of histone demethylases KDM4C and KDM6A: Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases. F E B S Letters. 2011 jun. 23;585(12):1951-1956. https://doi.org/10.1016/j.febslet.2011.05.023

Author

Kristensen, Jan B L ; Nielsen, Anders L ; Jørgensen, Lars ; Kristensen, Line Hyltoft ; Helgstrand, Charlotte ; Juknaite, Lina ; Kristensen, Jesper Langgaard ; Kastrup, Jette Sandholm ; Clausen, Rasmus Prætorius ; Olsen, Lars ; Gajhede, Michael. / Enzyme kinetic studies of histone demethylases KDM4C and KDM6A : Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases. I: F E B S Letters. 2011 ; Bind 585, Nr. 12. s. 1951-1956.

Bibtex

@article{f3fcd570a221461ca8c7f0981738b173,
title = "Enzyme kinetic studies of histone demethylases KDM4C and KDM6A: Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases",
abstract = "To investigate ligand selectivity between the oncogenic KDM4C and tumor repressor protein KDM6A histone demethylases, KDM4C and KDM6A were enzymatically characterized, and subsequently, four compounds were tested for inhibitory effects. 2,4-dicarboxypyridine and (R)-N-oxalyl-O-benzyltyrosine (3) are both known to bind to a close KDM4C homolog and 3 binds in the part of the cavity that accommodates the side chain in position 11 of histone 3. The inhibition measurements showed significant selectivity between KDM4C and KDM6A. This demonstrates that despite very similar active site topologies, selectivity between Jumonji family histone demethylases can be obtained even with small molecule ligands.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Kristensen, {Jan B L} and Nielsen, {Anders L} and Lars J{\o}rgensen and Kristensen, {Line Hyltoft} and Charlotte Helgstrand and Lina Juknaite and Kristensen, {Jesper Langgaard} and Kastrup, {Jette Sandholm} and Clausen, {Rasmus Pr{\ae}torius} and Lars Olsen and Michael Gajhede",
note = "Keywords: histone lysine demethylases, oncogenic, tumor repressor, enzyme kinetics, ligand selectivity",
year = "2011",
month = jun,
day = "23",
doi = "10.1016/j.febslet.2011.05.023",
language = "English",
volume = "585",
pages = "1951--1956",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "12",

}

RIS

TY - JOUR

T1 - Enzyme kinetic studies of histone demethylases KDM4C and KDM6A

T2 - Towards understanding selectivity of inhibitors targeting oncogenic histone demethylases

AU - Kristensen, Jan B L

AU - Nielsen, Anders L

AU - Jørgensen, Lars

AU - Kristensen, Line Hyltoft

AU - Helgstrand, Charlotte

AU - Juknaite, Lina

AU - Kristensen, Jesper Langgaard

AU - Kastrup, Jette Sandholm

AU - Clausen, Rasmus Prætorius

AU - Olsen, Lars

AU - Gajhede, Michael

N1 - Keywords: histone lysine demethylases, oncogenic, tumor repressor, enzyme kinetics, ligand selectivity

PY - 2011/6/23

Y1 - 2011/6/23

N2 - To investigate ligand selectivity between the oncogenic KDM4C and tumor repressor protein KDM6A histone demethylases, KDM4C and KDM6A were enzymatically characterized, and subsequently, four compounds were tested for inhibitory effects. 2,4-dicarboxypyridine and (R)-N-oxalyl-O-benzyltyrosine (3) are both known to bind to a close KDM4C homolog and 3 binds in the part of the cavity that accommodates the side chain in position 11 of histone 3. The inhibition measurements showed significant selectivity between KDM4C and KDM6A. This demonstrates that despite very similar active site topologies, selectivity between Jumonji family histone demethylases can be obtained even with small molecule ligands.

AB - To investigate ligand selectivity between the oncogenic KDM4C and tumor repressor protein KDM6A histone demethylases, KDM4C and KDM6A were enzymatically characterized, and subsequently, four compounds were tested for inhibitory effects. 2,4-dicarboxypyridine and (R)-N-oxalyl-O-benzyltyrosine (3) are both known to bind to a close KDM4C homolog and 3 binds in the part of the cavity that accommodates the side chain in position 11 of histone 3. The inhibition measurements showed significant selectivity between KDM4C and KDM6A. This demonstrates that despite very similar active site topologies, selectivity between Jumonji family histone demethylases can be obtained even with small molecule ligands.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.febslet.2011.05.023

DO - 10.1016/j.febslet.2011.05.023

M3 - Journal article

C2 - 21575637

VL - 585

SP - 1951

EP - 1956

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 12

ER -

ID: 33688211