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Related Experiment Video

Updated: Jun 20, 2026

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

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Prolyl hydroxylases and therapeutics.

Thomas G Smith, Nick P Talbot

Antioxidants & Redox Signaling

|September 19, 2009

Summary

Prolyl hydroxylase domain enzymes (PHDs) regulate hypoxia-inducible factors, offering therapeutic potential for diseases like anemia and cancer. Inhibitors targeting PHDs are advancing in clinical trials for various conditions.

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Prolyl hydroxylases are iron- and 2-oxoglutarate-dependent dioxygenases.
Collagen prolyl hydroxylase deficiency causes scurvy.
HIF prolyl hydroxylases (PHDs) regulate hypoxia-inducible factors (HIFs).

Discussion:

PHDs are central to cellular hypoxia response.
PHDs are investigated as therapeutic targets for anemia, ischemic heart disease, stroke, cancer, and pulmonary hypertension.
PHD inhibitors are in clinical trials.

Key Insights:

PHDs hydroxylate and regulate HIF transcription factors.
Targeting PHDs offers therapeutic avenues for oxygen homeostasis-related diseases.
Recent advances cover PHD biochemistry, therapeutic manipulation, neuroprotection, and iron homeostasis interplay.

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Outlook:

Novel PHD-based pharmaceuticals are progressing through clinical trials.
Further research into PHD inhibitors may yield new treatments.
Understanding PHD roles in oxygen and iron homeostasis is crucial for future therapies.