Human UTY(KDM6C) is a male-specific Nϵ-methyl lysyl demethylase.

Human UTY(KDM6C) is a male-specific Nϵ-methyl lysyl demethylase.

The Jumonji C lysine demethylases (KDMs) are 2-oxoglutarate- and Fe(II)-dependent oxygenases. KDM6A (UTX) and KDM6B (JMJD3) are KDM6 subfamily members that catalyze demethylation of N(ϵ)-methylated histone 3 lysine 27 (H3K27), a mark important for transcriptional repression. Despite reports stating...

Бүрэн тодорхойлолт

Номзүйн дэлгэрэнгүй
Үндсэн зохиолчид:	Walport, L, Hopkinson, R, Vollmar, M, Madden, S, Gileadi, C, Oppermann, U, Schofield, C, Johansson, C
Формат:	Journal article
Хэл сонгох:	English
Хэвлэсэн:	2014

Ижил төстэй зүйлс

Inhibitors of both the N-methyl lysyl- and arginyl- demethylase activities of the JmjC oxygenases
-н: Bonnici, J, зэрэг
Хэвлэсэн: (2018)

Human histone demethylase KDM6B can catalyse sequential oxidations
-н: Hopkinson, R, зэрэг
Хэвлэсэн: (2018)

Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.
-н: Hillringhaus, L, зэрэг
Хэвлэсэн: (2011)

Mechanisms of human histone and nucleic acid demethylases
-н: Walport, L, зэрэг
Хэвлэсэн: (2012)

Mechanisms of human histone and nucleic acid demethylases.
-н: Walport, L, зэрэг
Хэвлэсэн: (2012)

The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.
-н: Bonnici, J, зэрэг
Хэвлэсэн: (2023)

Studies on the interaction of the histone demethylase KDM5B with tricarboxylic acid cycle intermediates
-н: Tarhonskaya, H, зэрэг
Хэвлэсэн: (2017)

Structural analysis of human KDM5B guides histone demethylase inhibitor development.
-н: Johansson, C, зэрэг
Хэвлэсэн: (2016)

Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases.
-н: Rose, N, зэрэг
Хэвлэсэн: (2012)

The role of the lysine demethylases KDM5 and KDM6 in bone malignancies
-н: Hookway, E
Хэвлэсэн: (2016)

Conformational dynamics underlies different functions of human KDM7 histone demethylases
-н: Chaturvedi, S, зэрэг
Хэвлэсэн: (2019)

Identification of the KDM2/7 histone lysine demethylase subfamily inhibitor and its antiproliferative activity.
-н: Suzuki, T, зэрэг
Хэвлэсэн: (2013)

Analysis of JmjC Demethylase-Catalyzed Demethylation Using Geometrically-Constrained Lysine Analogues
-н: Langley, G, зэрэг
Хэвлэсэн: (2015)

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases.
-н: Walport, L, зэрэг
Хэвлэсэн: (2016)

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase
-н: Yue, W, зэрэг
Хэвлэсэн: (2010)

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.
-н: Yue, W, зэрэг
Хэвлэсэн: (2010)

Mechanistic and structural studies of KDM‐catalysed demethylation of histone 1 isotype 4 at lysine 26
-н: Walport, L, зэрэг
Хэвлэсэн: (2018)

Targeting lysine demethylase 5 (KDM5) in mantle cell lymphoma
-н: Danmei Xu, зэрэг
Хэвлэсэн: (2024-02-01)

8-substituted pyrido[3,4-d]pyrimidin-4(3H)-one derivatives as potent, cell permeable, KDM4 (JMJD2) and KDM5 (JARID1) histone lysine demethylase inhibitors
-н: Bavetsias, V, зэрэг
Хэвлэсэн: (2016)

Refractory testicular germ cell tumors are highly sensitive to the targeting of polycomb pathway demethylases KDM6A and KDM6B
-н: Doha Shokry, зэрэг
Хэвлэсэн: (2024-10-01)

The histone demethylase Kdm5 controls Hid-induced cell death in Drosophila
-н: Hans-Martin Herz, зэрэг
Хэвлэсэн: (2024-11-01)

The Lysine Demethylase KDM5B Regulates Islet Function and Glucose Homeostasis
-н: Marie Balslev Backe, зэрэг
Хэвлэсэн: (2019-01-01)

Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
-н: Kawamura, A, зэрэг
Хэвлэсэн: (2017)

Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
-н: Mantri, M, зэрэг
Хэвлэсэн: (2010)

Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6.
-н: Mantri, M, зэрэг
Хэвлэсэн: (2010)

Targeting histone lysine demethylases - Progress, challenges, and the future.
-н: Thinnes, C, зэрэг
Хэвлэсэн: (2014)

Advances and challenges in understanding histone demethylase biology
-н: Nowak, R, зэрэг
Хэвлэсэн: (2016)

Hypoxia and hormone-mediated pathways converge at the histone demethylase KDM4B in cancer.
-н: Yang, J, зэрэг
Хэвлэсэн: (2018)

Investigating the effect of hypoxia on the JmjC histone lysine demethylase KDM4A
-н: Hancock, R
Хэвлэсэн: (2016)

Histone Demethylase KDM4C Is Required for Ovarian Cancer Stem Cell Maintenance
-н: Guo-Qing Chen, зэрэг
Хэвлэсэн: (2020-01-01)

Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control
-н: Ramanan, R, зэрэг
Хэвлэсэн: (2020)

Recent progress in histone demethylase inhibitors
-н: McAllister, T, зэрэг
Хэвлэсэн: (2016)

Discovery of a highly selective cell‐active inhibitor of the histone lysine demethylases KDM2/7
-н: Gerken, P, зэрэг
Хэвлэсэн: (2017)

Discovery of a highly selective cell-active inhibitor of the histone lysine demethylases KDM2/7
-н: Gerken, PA, зэрэг
Хэвлэсэн: (2017)

Lysine Demethylase JMJD2D (KDM4D); A Targeting Enabling Package
-н: Brennan, P
Хэвлэсэн: (2018)

Lysine Demethylase JMJD1B (KDM3B); A Target Enabling Package
-н: Brennan, P
Хэвлэсэн: (2018)

Lysine Demethylase JMJD2D (KDM4D); A Targeting Enabling Package
-н: Savitsky, P
Хэвлэсэн: (2018)

Lysine Demethylase JMJD1B (KDM3B); A Target Enabling Package
-н: Brennan, P
Хэвлэсэн: (2018)

Lysine Demethylase JMJD2D (KDM4D); A Targeting Enabling Package
-н: Brennan, P
Хэвлэсэн: (2018)

Biochemical and cellular studies of the KDM6 sub-family of JmjC histone lysine demethylases
-н: Dunne, K
Хэвлэсэн: (2018)