A fluorescent benzo[g]isoquinoline-based HIF prolyl hydroxylase inhibitor for cellular imaging
Prolyl hydroxylation domain (PHD) enzymes catalyze the hydroxylation of the transcription factor hypoxia‐inducible factor (HIF) and serve as cellular oxygen sensors. HIF and the PHD enzymes regulate numerous potentially tissue‐protective target genes which can adapt cells to metabolic and ischemic s...
Autors principals: | Mayer, M, Fey, K, Heinze, E, Rainer Wick, C, Abboud, M, Yeh, T, Tumber, A, Orth, N, Schley, G, Buchholz, B, Clark, T, Schofield, C, Willam, C, Burzlaff, N |
---|---|
Format: | Journal article |
Publicat: |
Wiley
2018
|
Ítems similars
-
No benefit of HIF prolyl hydroxylase inhibition for hypertensive renal damage in renovascular hypertensive rats
per: Andrea Hartner, et al.
Publicat: (2023-06-01) -
Tuning the transcriptional response to hypoxia by inhibiting HIF prolyl- and asparaginyl-hydroxylases
per: Chan, M, et al.
Publicat: (2016) -
Molecular and Cellular Mechanisms of HIF Prolyl Hydroxylase inhibitors in Clinical Trials
per: Yeh, TL, et al.
Publicat: (2017) -
The use of dioxygen by HIF prolyl hydroxylase (PHD1).
per: McNeill, L, et al.
Publicat: (2002) -
2-oxoglutarate analogue inhibitors of HIF prolyl hydroxylase.
per: Mole, D, et al.
Publicat: (2003)