Cargando…

Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control

The N(ε)-methyl lysine status of histones is important in the regulation of eukaryotic transcription. The Fe(ii) and 2-oxoglutarate (2OG) -dependent JmjC domain enzymes are the largest family of histone N(ε)-methyl lysine demethylases (KDMs). The human KDM4 subfamily of JmjC KDMs is linked with mult...

Descripción completa

Detalles Bibliográficos
Autores principales:	Ramanan, Rajeev, Chaturvedi, Shobhit S., Lehnert, Nicolai, Schofield, Christopher J., Karabencheva-Christova, Tatyana G., Christov, Christo Z.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	The Royal Society of Chemistry 2020
Materias:	Chemistry
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8162366/ https://www.ncbi.nlm.nih.gov/pubmed/34094257 http://dx.doi.org/10.1039/d0sc03713c

Ejemplares similares

Catalysis by the Non-Heme Iron(II) Histone Demethylase PHF8 Involves Iron Center Rearrangement and Conformational Modulation of Substrate Orientation
por: Chaturvedi, Shobhit S., et al.
Publicado: (2019)

Role of Structural Dynamics in Selectivity and Mechanism of Non-heme Fe(II) and 2-Oxoglutarate-Dependent Oxygenases Involved in DNA Repair
por: Waheed, Sodiq O., et al.
Publicado: (2020)

Is JmjC Oxygenase Catalysis Limited to Demethylation?**
por: Hopkinson, Richard J, et al.
Publicado: (2013)

The Activity of JmjC Histone Lysine Demethylase KDM4A is Highly Sensitive to Oxygen Concentrations
por: Hancock, Rebecca L, et al.
Publicado: (2017)

Characterization of Drosophila melanogaster JmjC+N histone demethylases
por: Lloret-Llinares, Marta, et al.
Publicado: (2008)

Chromatin and oxygen sensing in the context of JmjC histone demethylases
por: Shmakova, Alena, et al.
Publicado: (2014)

JmjC histone demethylases act as chromatin oxygen sensors
por: Batie, Michael, et al.
Publicado: (2019)

JmjC Family of Histone Demethylases Form Nuclear Condensates
por: Vicioso-Mantis, Marta, et al.
Publicado: (2022)

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases
por: Walport, Louise J., et al.
Publicado: (2016)

Inhibitors of both the N-methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases
por: Bonnici, Joanna, et al.
Publicado: (2018)

A Cell-Permeable Ester Derivative of the JmjC Histone Demethylase Inhibitor IOX1
por: Schiller, Rachel, et al.
Publicado: (2014)

Can Second Coordination Sphere and Long-Range Interactions Modulate Hydrogen Atom Transfer in a Non-Heme Fe(II)-Dependent Histone Demethylase?
por: Chaturvedi, Shobhit S., et al.
Publicado: (2022)

Evolutionary History and Functional Diversification of the JmjC Domain-Containing Histone Demethylase Gene Family in Plants
por: Ma, Shifeng, et al.
Publicado: (2022)

Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: involvement in the proliferation of cancer cells through the E2F/RB pathway
por: Hayami, Shinya, et al.
Publicado: (2010)

MoJMJ1, Encoding a Histone Demethylase Containing JmjC Domain, Is Required for Pathogenic Development of the Rice Blast Fungus, Magnaporthe oryzae
por: Huh, Aram, et al.
Publicado: (2017)

Clioquinol as an inhibitor of JmjC-histone demethylase exhibits common and unique histone methylome and transcriptome between clioquinol and hypoxia
por: Moon, Yunwon, et al.
Publicado: (2022)

Genome-wide Characterization of the JmjC Domain-Containing Histone Demethylase Gene Family Reveals GhJMJ24 and GhJMJ49 Involving in Somatic Embryogenesis Process in Cotton
por: Li, Yan, et al.
Publicado: (2022)

Investigations on small molecule inhibitors targeting the histone H3K4 tri-methyllysine binding PHD-finger of JmjC histone demethylases
por: Bhushan, Bhaskar, et al.
Publicado: (2018)

Genome-wide identification, classification and expression analysis of the JmjC domain-containing histone demethylase gene family in maize
por: Qian, Yexiong, et al.
Publicado: (2019)

Genome-wide identification, classification, and expression analysis of the JmjC domain-containing histone demethylase gene family in birch
por: Chen, Bowei, et al.
Publicado: (2021)

Characterization and Stress Response of the JmjC Domain-Containing Histone Demethylase Gene Family in the Allotetraploid Cotton Species Gossypium hirsutum
por: Zhang, Jie, et al.
Publicado: (2020)

JmjC-KDMs KDM3A and KDM6B modulate radioresistance under hypoxic conditions in esophageal squamous cell carcinoma
por: Macedo-Silva, Catarina, et al.
Publicado: (2020)

Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates
por: Williams, Sophie T, et al.
Publicado: (2015)

Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66
por: Türkmen, Vildan A., et al.
Publicado: (2023)

Systematic analysis of JmjC gene family and stress-response expression of KDM5 subfamily genes in Brassica napus
por: He, Xinghui, et al.
Publicado: (2021)

Genome-wide identification, classification and expression analysis of the JmjC domain-containing histone demethylase gene family in Jatropha curcas L.
por: Wang, Jie, et al.
Publicado: (2022)

Kinetic and inhibition studies on human Jumonji-C (JmjC) domain-containing protein 5
por: Tumber, Anthony, et al.
Publicado: (2023)

Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
por: Chowdhury, Rasheduzzaman, et al.
Publicado: (2022)

JmjC domain proteins modulate circadian behaviors and sleep in Drosophila
por: Shalaby, Nevine A., et al.
Publicado: (2018)

Noncatalytic Function of a JmjC Domain Protein Disrupts Heterochromatin
por: Bao, Kehan, et al.
Publicado: (2019)

The JmjN domain as a dimerization interface and a targeted inhibitor of KDM4 demethylase activity
por: Levin, May, et al.
Publicado: (2018)

The JmjC domain protein Epe1 prevents unregulated assembly and disassembly of heterochromatin
por: Trewick, Sarah C, et al.
Publicado: (2007)

JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
por: Yeo, Kok Siong, et al.
Publicado: (2017)

Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions
por: Kwok, Janice, et al.
Publicado: (2017)

Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8
por: Wang, Chengliang, et al.
Publicado: (2015)

Regulation of ectopic heterochromatin-mediated epigenetic diversification by the JmjC family protein Epe1
por: Sorida, Masato, et al.
Publicado: (2019)

The Cross Marks the Spot: The Emerging Role of JmjC Domain-Containing Proteins in Myeloid Malignancies
por: Staehle, Hans Felix, et al.
Publicado: (2021)

Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1
por: Singh, Warispreet, et al.
Publicado: (2016)

IBM1, a JmjC domain-containing histone demethylase, is involved in the regulation of RNA-directed DNA methylation through the epigenetic control of RDR2 and DCL3 expression in Arabidopsis
por: Fan, Di, et al.
Publicado: (2012)

An Arabidopsis jmjC domain protein protects transcribed genes from DNA methylation at CHG sites
por: Miura, Asuka, et al.
Publicado: (2009)

Cannot write session to /tmp/vufind_sessions/sess_ijeh1v0ef95ksc5e8dlh6c6lio