The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin.
Hypoxia-inducible factor-1 (HIF) is regulated by oxygen-dependent prolyl hydroxylation. Of the three HIF prolyl hydroxylases (PHD1, 2 and 3) identified, PHD3 exhibits restricted substrate specificity in vitro and is induced in different cell types by diverse stimuli. PHD3 may therefore provide an in...
Main Authors: | Masson, N, Appelhoff, R, Tuckerman, JR, Tian, Y, Demol, H, Puype, M, Vandekerckhove, J, Ratcliffe, P, Pugh, C |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2004
|
Similar Items
-
The use of dioxygen by HIF prolyl hydroxylase (PHD1).
by: McNeill, L, et al.
Published: (2002) -
Determination and comparison of specific activity of the HIF-prolyl hydroxylases.
by: Tuckerman, JR, et al.
Published: (2004) -
Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor.
by: Appelhoff, R, et al.
Published: (2004) -
Regulation of HIF: prolyl hydroxylases.
by: Stolze, I, et al.
Published: (2006) -
Assembly and substrate recognition properties of human CCT subunits of the TRiC chaperonin
by: Sergeeva, Oksana A
Published: (2015)