Assays using recombinant HIF prolyl hydroxylases did not support hydroxylation of more than 20 reported non-HIF substrates under conditions where robust HIF hydroxylation was observed.

Cells rely on prolyl hydroxylase enzymes to sense low levels of oxygen, but they might act on fewer targets than previously thought.

The prolyl hydroxylase domain 2 regulates the Treg development and function in a hypoxia-inducible factor 2α-dependent manner.

The protein uS12/Rps23 functions extra-ribosomally to control oxygen homeostasis in fission yeast.

The subcellular localization of the prolyl hydroxylase oxygen sensor in C. elegans neurons is regulated by p38 MAP kinase signaling.

Cysteine dioxygenase, a conserved and critical enzyme in sulfur amino acid metabolism, is activated by the hypoxia-inducible transcription factor.

An unbiased genome-wide human forward genetic screen identifies the vacuolar ATPase complex and assembly factors as regulators of HIF stability through their actions on intracellular iron metabolism.

Multi-omics reveals that Alkb homolog 7 (ALKBH7), α mitochondrial alpha-ketoglutarate dioxygenase of unclear function, regulates glyoxal metabolism, which may explain its role in necrosis and heart attack.

A survey of oxygen-dependent enzymes suggests new candidates for oxygen sensors, expanding potential mechanisms underlying hypoxia-related adaptations or diseases in humans.

Previous studies and emerging data on pseudohypoxic diseases suggest that the complex phenotypic spectrum of VHL disease is due to the extent of HIF pathway deregulation in susceptible cell types and not by other purported substrates or functions of pVHL.