Is JmjC oxygenase catalysis limited to demethylation?

Is JmjC oxygenase catalysis limited to demethylation?

Jobs on the side: Substrate selectivity studies indicate that members of the biomedically important JmjC demethylase family of histone N(ε)-methyllysine demethylases are capable of catalyzing the de-N-alkylation of groups other than N-methyl and can catalyze reactions that form stable hydroxylated p...

Bibliográfalaš dieđut
Váldodahkkit:	Hopkinson, R, Walport, L, Münzel, M, Rose, N, Smart, T, Kawamura, A, Claridge, T, Schofield, C
Materiálatiipa:	Journal article
Giella:	English
Almmustuhtton:	2013

Geahča maid

Analysis of JmjC Demethylase-Catalyzed Demethylation Using Geometrically-Constrained Lysine Analogues
Dahkki: Langley, G, et al.
Almmustuhtton: (2015)

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases.
Dahkki: Walport, L, et al.
Almmustuhtton: (2016)

JmjC-domain-containing proteins and histone demethylation.
Dahkki: Klose, R, et al.
Almmustuhtton: (2006)

Inhibitors of both the N-methyl lysyl- and arginyl- demethylase activities of the JmjC oxygenases
Dahkki: Bonnici, J, et al.
Almmustuhtton: (2018)

In vitro enzyme assays for JmjC-domain-containing lysine histone demethylases (JmjC-KDMs)
Dahkki: Tarhonskaya, H, et al.
Almmustuhtton: (2018)

Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases
Dahkki: Markolovic, S, et al.
Almmustuhtton: (2016)

The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.
Dahkki: Bonnici, J, et al.
Almmustuhtton: (2023)

Inhibitors of JmjC-containing histone demethylases
Dahkki: Wright, M, et al.
Almmustuhtton: (2020)

JmjC ‐domain‐containing histone demethylases
Dahkki: Højrup, C, et al.
Almmustuhtton: (2019)

JmjC catalysed histone H2a N -methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships
Dahkki: Bonnici, J, et al.
Almmustuhtton: (2024)

Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.
Dahkki: Woon, E, et al.
Almmustuhtton: (2012)

Investigating the inhibitor and substrate diversity of the JmjC histone demethylases
Dahkki: Shamo Schiller, R
Almmustuhtton: (2016)

Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66.
Dahkki: Türkmen, VA, et al.
Almmustuhtton: (2023)

Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control
Dahkki: Ramanan, R, et al.
Almmustuhtton: (2020)

Kinetic and inhibition studies on human Jumonji-C (JmjC) domain-containing protein 5
Dahkki: Tumber, A, et al.
Almmustuhtton: (2023)

A cell-permeable ester derivative of the JmjC histone demethylase inhibitor IOX1.
Dahkki: Schiller, R, et al.
Almmustuhtton: (2014)

The activity of JmjC histone lysine demethylase KDM4A is highly sensitive to oxygen concentrations
Dahkki: Hancock, R, et al.
Almmustuhtton: (2017)

JmjC catalysed histone H2a N-methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships
Dahkki: Bonnici, J
Almmustuhtton: (2024)

Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
Dahkki: Chowdhury, R, et al.
Almmustuhtton: (2022)

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

JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
Dahkki: Yeo, K.S., et al.
Almmustuhtton: (2017)

Investigating the effect of hypoxia on the JmjC histone lysine demethylase KDM4A
Dahkki: Hancock, R
Almmustuhtton: (2016)

JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.
Dahkki: Clissold, P, et al.
Almmustuhtton: (2001)

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

Host resistance to a gastrointestinal parasite regulated by Mina, an immunoregulatory member of the JmjC protein family
Dahkki: Pillai, MR, et al.
Almmustuhtton: (2013)

Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases.
Dahkki: Loenarz, C, et al.
Almmustuhtton: (2011)

Investigating the substrate selectivity and the inhibitor of the human KDM7 sub-family of JmjC histone lysine demethylases
Dahkki: Zhang, Y
Almmustuhtton: (2019)

Mechanistic and structural studies of KDM‐catalysed demethylation of histone 1 isotype 4 at lysine 26
Dahkki: Walport, L, et al.
Almmustuhtton: (2018)

Adventures in defining roles of oxygenases in the regulation of protein biosynthesis
Dahkki: Walport, L, et al.
Almmustuhtton: (2018)

Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation
Dahkki: Hancock, R, et al.
Almmustuhtton: (2018)

Inhibition of 2-oxoglutarate dependent oxygenases.
Dahkki: Rose, N, et al.
Almmustuhtton: (2011)

Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.
Dahkki: Leung, I, et al.
Almmustuhtton: (2013)

2-oxoglutarate-dependent oxygenases
Dahkki: Islam, M, et al.
Almmustuhtton: (2018)

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

Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling.
Dahkki: Hewitson, K, et al.
Almmustuhtton: (2005)

Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition
Dahkki: Belle, R, et al.
Almmustuhtton: (2017)

Human histone demethylase KDM6B can catalyse sequential oxidations
Dahkki: Hopkinson, R, et al.
Almmustuhtton: (2018)

Small-molecule-based inhibition of histone demethylation in cells assessed by quantitative mass spectrometry.
Dahkki: Mackeen, M, et al.
Almmustuhtton: (2010)

Reducing agent-mediated nonenzymatic conversion of 2‐oxoglutarate to succinate: implications for oxygenase assays
Dahkki: Khan, A, et al.
Almmustuhtton: (2020)

Oxygenases for oxygen sensing
Dahkki: Loenarz, C, et al.
Almmustuhtton: (2008)