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Inhibitors of Jumonji-C domain-containing histone demethylases
2023Agencia Estatal de Investigación | Ref.
Sian, Veronica +5 more
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BioEssays, 2023
AbstractAscorbic acid is a redox regulator in many physiological processes. Besides its antioxidant activity, many intriguing functions of ascorbic acid in the expression of immunoregulatory genes have been suggested. Ascorbic acid acts as a co‐factor for the Fe+2‐containing α‐ketoglutarate‐dependent Jumonji‐C domain‐containing histone demethylases ...
Jeet Maity +4 more
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AbstractAscorbic acid is a redox regulator in many physiological processes. Besides its antioxidant activity, many intriguing functions of ascorbic acid in the expression of immunoregulatory genes have been suggested. Ascorbic acid acts as a co‐factor for the Fe+2‐containing α‐ketoglutarate‐dependent Jumonji‐C domain‐containing histone demethylases ...
Jeet Maity +4 more
openaire +2 more sources
4.3 Pulmonary Circulation and Pulmonary Vascular Diseases, 2016
Pulmonary hypertension (PH) is characterized by increased proliferation and apoptosis resistance of pulmonary vascular cells. Jumonji C domain-containing histone demethylases (JMJDs) are a novel class of epigenetic regulators, implicated in chromatin regulation and often possess the ability to demethylate lysine residues on histones.
Christian Muecke +3 more
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Pulmonary hypertension (PH) is characterized by increased proliferation and apoptosis resistance of pulmonary vascular cells. Jumonji C domain-containing histone demethylases (JMJDs) are a novel class of epigenetic regulators, implicated in chromatin regulation and often possess the ability to demethylate lysine residues on histones.
Christian Muecke +3 more
openaire +1 more source
Bioorganic & Medicinal Chemistry Letters, 2009
N-Oxalylglycine (NOG) derivatives were synthesized, and their inhibitory effect on histone lysine demethylase activity was evaluated. NOG and compound 1 inhibited histone lysine demethylases JMJD2A, 2C and 2D in enzyme assays, and their dimethyl ester prodrugs DMOG and 21 exerted histone lysine methylating activity in cellular assays.
Shohei, Hamada +7 more
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N-Oxalylglycine (NOG) derivatives were synthesized, and their inhibitory effect on histone lysine demethylase activity was evaluated. NOG and compound 1 inhibited histone lysine demethylases JMJD2A, 2C and 2D in enzyme assays, and their dimethyl ester prodrugs DMOG and 21 exerted histone lysine methylating activity in cellular assays.
Shohei, Hamada +7 more
openaire +2 more sources
Journal of Medicinal Chemistry, 2010
Selective inhibitors of Jumonji domain-containing protein (JMJD) histone demethylases are candidate anticancer agents as well as potential tools for elucidating the biological functions of JMJDs. On the basis of the crystal structure of JMJD2A and a homology model of JMJD2C, we designed and prepared a series of hydroxamate analogues bearing a tertiary ...
Shohei, Hamada +16 more
openaire +2 more sources
Selective inhibitors of Jumonji domain-containing protein (JMJD) histone demethylases are candidate anticancer agents as well as potential tools for elucidating the biological functions of JMJDs. On the basis of the crystal structure of JMJD2A and a homology model of JMJD2C, we designed and prepared a series of hydroxamate analogues bearing a tertiary ...
Shohei, Hamada +16 more
openaire +2 more sources
Role and Regulation of Jumonji C domain-containing histone demethylases in Pulmonary Hypertension
Pneumologie, 2016C Mücke, S Dabral, S Savai Pullamsetti
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PP-074 INHIBITION OF JUMONJI C DOMAIN CONTAINING HISTONE DEMETHYLASES IN ACUTE MYELOID LEUKEMIA
Leukemia Research, 2014N. Hastar, D. Koca, Y. Baran
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