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Small-molecules that covalently react with a human prolyl hydroxylase-towards activity modulation and substrate capture

Autor: Bush, J, Lesniak, R, Yeh, T, Belle, R, Kramer, H, Tumber, A, Chowdhury, R, Flashman, E, Mecinovic, J, Schofield, C

Publikováno v: Bush, J T, Leśniak, R K, Yeh, T L, Belle, R, Kramer, H, Tumber, A, Chowdhury, R, Flashman, E, Mecinović, J & Schofield, C J 2019, ' Small-molecules that covalently react with a human prolyl hydroxylase-towards activity modulation and substrate capture ', Chemical Communications, vol. 55, no. 8, pp. 1020-1023 . https://doi.org/10.1039/c8cc07706a

We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbseq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::c51852a308e76e7b3e7f5727fcc6d0bd
https://findresearcher.sdu.dk:8443/ws/files/145976068/c8cc07706a.pdf

Oxygen-dependent proteolysis regulates the stability of angiosperm polycomb repressive complex 2 subunit VERNALIZATION 2

Autor: Gibbs, D, Tedds, H, Labandara, A, Bailey, M, White, M, Hartman, S, Sprigg, C, Mogg, S, Osborne, R, Dambire, C, Boeckx, T, Paling, Z, Voesenek, L, Flashman, E, Holdsworth, M

Publikováno v: Nature Communications. 9

The polycomb repressive complex 2 (PRC2) regulates epigenetic gene repression in eukaryotes. Mechanisms controlling its developmental specificity and signal-responsiveness are poorly understood. Here, we identify an oxygen-sensitive N-terminal (N-) d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b6089490b02f2b95c93254f2faf0e592
http://ora.ox.ac.uk/objects/uuid:

The activity of JmjC histone lysine demethylase KDM4A is highly sensitive to oxygen concentrations

Autor: Hancock, R, Masson, N, Dunne, K, Flashman, E, Kawamura, A

Publikováno v: ACS Chemical Biology. 12(4)

The JmjC histone lysine demethylases (KDMs) are epigenetic regulators involved in the removal of methyl groups from post-translationally modified lysyl residues within histone tails, modulating gene transcription. These enzymes require molecular oxyg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::15e57775fbb6f22d62c8edaa7f70efb0
http://ora.ox.ac.uk/objects/uuid:

Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen

Autor: Flashman, E, Hoffart, LM, Hamed, RB, Bollinger, JM, Krebs, C, Schofield, CJ

The response of animals to hypoxia is mediated by the hypoxia-inducible transcription factor. Human hypoxia-inducible factor is regulated by four Fe(II)- and 2-oxoglutarate-dependent oxygenases: prolyl hydroxylase domain enzymes 1-3 catalyse hydroxyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::18d7273aea32aee53ba16817c3d89046
https://doi.org/10.1111/j.1742-4658.2010.07804.x