Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors
Abstract The human 2-oxoglutarate dependent oxygenase aspartate/asparagine-β-hydroxylase (AspH) catalyses the hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains (EGFDs). AspH is upregulated on the surface of malign cancer cells; increased AspH levels correlate with tumour inva...
Saved in:
Main Authors: | Lennart Brewitz, Anthony Tumber, Inga Pfeffer, Michael A. McDonough, Christopher J. Schofield |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2020
|
Subjects: | |
Online Access: | https://doaj.org/article/86f4a7c44ed5487c8df924d7752ecc2e |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Author Correction: Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors
by: Lennart Brewitz, et al.
Published: (2020) -
Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
by: Inga Pfeffer, et al.
Published: (2019) -
p53-mediated control of aspartate-asparagine homeostasis dictates LKB1 activity and modulates cell survival
by: Longfei Deng, et al.
Published: (2020) -
2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases
by: Yu Nakashima, et al.
Published: (2021) -
Precision multidimensional assay for high-throughput microRNA drug discovery
by: Benjamin Haefliger, et al.
Published: (2016)