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Figure 1. Expression of two species of PHD1 protein in different cell lines. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
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Figure 9. Effect of Siah suppression or deficiency on PHD1 expression. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 5. Cycloheximide chase examining the protein stability of the two species of PHD1 (p43 and p40) under hypoxic and normoxic conditions. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 3. Pulse–chase study examining for a precursor–product relationship between the two species of PHD1. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 4. Expression of the two species of PHD1 in response to oestrogen, proteasomal inhibition, hypoxia and cellular confluence. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 6. Prolyl hydroxylase activity of wild-type, PHD1M1A and PHD1M34A enzymes. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 8. Effect of the Siah E3 ligase overexpression on PHD1 abundance. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 7. Effect of PHD1 expression on the activity of Gal4 fusion proteins bearing isolated HIF-α degradation domains. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
Figure 2. Endogenous expression of the two forms of PHD1 and comparison with IVTT syntheses of wild-type, PHD1M1A and PHD1M34A proteins. From: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation.
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