Relevant bibliographies by topics / JmjC KDMs

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Academic literature on the topic 'JmjC KDMs'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "JmjC KDMs"

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Bonnici, Joanna, Anthony Tumber, Akane Kawamura, and Christopher J. Schofield. "Inhibitors of both the N -methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1748 (2018): 20170071. http://dx.doi.org/10.1098/rstb.2017.0071.

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The Jumonji C (JmjC) family of 2-oxoglutarate (2OG)-dependent oxygenases have established roles in the regulation of transcription via the catalysis of demethylation of N ε - methylated lysine residues in histone tails, especially the N - terminal tail of histone H3. Most human JmjC N ɛ -methyl lysine demethylases (KDMs) are complex enzymes, with ‘reader domains’ in addition to their catalytic domains. Recent biochemical evidence has shown that some, but not all, JmjC KDMs also have N ω - methyl arginyl demethylase (RDM) activity. JmjC KDM activity has been linked to multiple cancers and some
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Nanduri, Jayasri, Ning Wang, Benjamin L. Wang та Nanduri R. Prabhakar. "Lysine demethylase KDM6B regulates HIF-1α-mediated systemic and cellular responses to intermittent hypoxia". Physiological Genomics 53, № 9 (2021): 385–94. http://dx.doi.org/10.1152/physiolgenomics.00045.2021.

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Intermittent hypoxia (IH) is a hallmark manifestation of obstructive sleep apnea (OSA). Rodents treated with IH exhibit hypertension. Hypoxia-inducible factor (HIF)-1-dependent transcriptional activation of NADPH oxidases ( Nox) and the resulting increase in reactive oxygen species (ROS) levels is a major molecular mechanism underlying IH/OSA-induced hypertension. Jumanji C (JmjC)-containing histone lysine demethylases (JmjC-KDMs) are coactivators of HIF-1-dependent transcriptional activation. In the present study, we tested the hypothesis that JmjC-KDMs are required for IH-evoked HIF-1 transc
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Tarhonskaya, Hanna, Anthony Tumber, Akane Kawamura, and Christopher J. Schofield. "In Vitro Enzyme Assays for JmjC-Domain-Containing Lysine Histone Demethylases (JmjC-KDMs)." Current Protocols in Pharmacology 80, no. 1 (2018): 3.15.1–3.15.12. http://dx.doi.org/10.1002/cpph.34.

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Benedetti, Rosaria, Carmela Dell’Aversana, Tommaso De Marchi та ін. "Inhibition of Histone Demethylases LSD1 and UTX Regulates ERα Signaling in Breast Cancer". Cancers 11, № 12 (2019): 2027. http://dx.doi.org/10.3390/cancers11122027.

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In breast cancer, Lysine-specific demethylase-1 (LSD1) and other lysine demethylases (KDMs), such as Lysine-specific demethylase 6A also known as Ubiquitously transcribed tetratricopeptide repeat, X chromosome (UTX), are co-expressed and co-localize with estrogen receptors (ERs), suggesting the potential use of hybrid (epi)molecules to target histone methylation and therefore regulate/redirect hormone receptor signaling. Here, we report on the biological activity of a dual-KDM inhibitor (MC3324), obtained by coupling the chemical properties of tranylcypromine, a known LSD1 inhibitor, with the
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Konduri, Purna Chaitanya, Tianyuan Wang, Narges Salamat, and Li Zhang. "Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins." Cells 9, no. 3 (2020): 773. http://dx.doi.org/10.3390/cells9030773.

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The KDM4 histone demethylase subfamily is constituted of yeast JmjC domain-containing proteins, such as Gis1, and human Gis1 orthologues, such as KDM4A/B/C. KDM4 proteins have important functions in regulating chromatin structure and gene expression in response to metabolic and nutritional stimuli. Heme acts as a versatile signaling molecule to regulate important cellular functions in diverse organisms ranging from bacteria to humans. Here, using purified KDM4 proteins containing the JmjN/C domain, we showed that heme stimulates the histone demethylase activity of the JmjN/C domains of KDM4A a
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He, Xinghui, Qianwen Wang, Jiao Pan, Boyu Liu, Ying Ruan, and Yong Huang. "Systematic analysis of JmjC gene family and stress­-response expression of KDM5 subfamily genes in Brassica napus." PeerJ 9 (March 31, 2021): e11137. http://dx.doi.org/10.7717/peerj.11137.

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Background Jumonji C (JmjC) proteins exert critical roles in plant development and stress response through the removal of lysine methylation from histones. Brassica napus, which originated from spontaneous hybridization by Brassica rapa and Brassica oleracea, is the most important oilseed crop after soybean. In JmjC proteins of Brassica species, the structure and function and its relationship with the parents and model plant Arabidopsis thaliana remain uncharacterized. Systematic identification and analysis for JmjC family in Brassica crops can facilitate the future functional characterization
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Jin, Fengyan, Shaji K. Kumar, and Yun Dai. "The Lysine-Specific Demethylase KDM4A/JMJD2A Acts As a Tumor Suppressor in Multiple Myeloma." Blood 132, Supplement 1 (2018): 191. http://dx.doi.org/10.1182/blood-2018-191.

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Abstract Introduction: Histone lysine methylation, a reversible event dynamically and reciprocally regulated by lysine methyltransferases (KMTs) and demethylases (KDMs), represents one of the major epigenetic mechanisms for regulation of chromatin remodeling and gene expression re-programming. The KDM4 family, which belongs to the Jumonji C (JmjC)-domain-containing proteins (JMJDs), consists of five members, including KDM4A-E that demethylate H3K9me2/3 and/or H3K36me2/3 in a Fe2+- and α-ketoglutarate-dependent manner. KDM4 proteins are involved in various cellular processes such as gene transc
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8

Yoo, Jung, Yu Hyun Jeon, Ha Young Cho, et al. "Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target." Cancers 12, no. 5 (2020): 1098. http://dx.doi.org/10.3390/cancers12051098.

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Lysine-specific histone demethylase 3 (KDM3) subfamily proteins are H3K9me2/me1 histone demethylases that promote gene expression. The KDM3 subfamily primarily consists of four proteins (KDM3A−D). All four proteins contain the catalytic Jumonji C domain (JmjC) at their C-termini, but whether KDM3C has demethylase activity is under debate. In addition, KDM3 proteins contain a zinc-finger domain for DNA binding and an LXXLL motif for interacting with nuclear receptors. Of the KDM3 proteins, KDM3A is especially deregulated or overexpressed in multiple cancers, making it a potential cancer therape
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Walters, Denise K., Renee C. Tschumper, Dominique B. Hoelzinger, et al. "CRISPR-Mediated Loss of Immunoglobulin Heavy Chain in Multiple Myeloma Cell Line Results in Metabolic Pathway Alterations." Blood 132, Supplement 1 (2018): 1885. http://dx.doi.org/10.1182/blood-2018-99-114943.

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Abstract Aberrant over production of monoclonal immunoglobulin is a classic feature of the plasma cell (PC) malignancy multiple myeloma (MM). At diagnosis and more frequently upon relapse, some MM patients present with increased production of monoclonal free light chain (FLC) without a corresponding increase in intact immunoglobulin. This phenomenon is commonly referred to as light chain escape (LCE). As previously described (Walters et al. 2018, Experimental Hematology, Vol 57 p42-49), we have established a monoclonal IgA kappa MM cell line, designated as MC-B11/14, from the bone marrow (BM)
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10

Levin, May, Michal Stark, and Yehuda G. Assaraf. "The JmjN domain as a dimerization interface and a targeted inhibitor of KDM4 demethylase activity." Oncotarget 9, no. 24 (2018): 16861–82. http://dx.doi.org/10.18632/oncotarget.24717.

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Dissertations / Theses on the topic "JmjC KDMs"

1

Schiller, Rachel Shamo. "Investigating the inhibitor and substrate diversity of the JmjC histone demethylases." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:1e7fd2a1-a9c3-48f7-8fa7-a041299d42f9.

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Epigenetic control of gene expression by histone post-translational modifications (PTMs) is a complex process regulated by proteins that can 'read', 'write' or 'erase' these PTMs. The histone lysine demethylase (KDM) family of epigenetic enzymes remove methyl modifications from lysines on histone tails. The Jumonji C domain (JmjC) family is the largest family of KDMs. Investigating the scope and mechanisms of the JmjC KDMs is of interest for understanding the diverse functions of the JmjC KDMs in vivo, as well as for the application of the basic science to medicinal chemistry design. The work
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