Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
By Robert P. Hausinger. 2004
800 citations recorded by the source corpus.
Subfields: Inorganic Chemistry, Materials Chemistry, Renewable Energy, Sustainability and the Environment
View Paper: https://www.semanticscholar.org/paper/0bc1d2d4c9a6994909965f3c3f745e9cac6f4a55
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- B. Weinert
- M. Mullowney
- J. Navarro-Muñoz
- Chunaram Choudhary
- Sebastian A. Wagner
- S. Kautsar
- Nelly Sélem-Mojica
- Shenghong Ma
Citations in the corpus
- A computational framework to explore large-scale biosynthetic diversity (2019, positive): “The product of the tauD gene belongs to the Fe(II)/ α -ketoglutarate-dependent hydroxylase enzyme superfamily and is named for the commonly encoded α -ketoglutarate-dependent taurine dioxygenase involved in the assimilation of sulphite by oxygenolytic release from the amino acid taurine 44 .”
- Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. (2012, background): “The DNA amount used for dot blot analysis was determined by methylene blue staining (Supplemental Fig.”
- Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. (2013, background): “However, succinate can traverse the mitochondrial membrane and can be formed in the cytoplasm as a side product from a-ketoglutarate-dependent enzymes (Hausinger, 2004).”