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Reduced Bone Mass in Collagen Prolyl 4-Hydroxylase <em>P4ha1</em> ^+/-; <em>P4ha2</em> ^-/- Compound Mutant Mice

Pharmaceuticals, Vol. 15, Pages 786: Will We Unlock the Benefit of Metformin for Patients with Lung Cancer? Lessons from Current Evidence and New Hypotheses

HIF-PH Encoded by <em>EGLN1</em> Is a Potential Therapeutic Target for Chronic Lymphocytic Leukemia

Prolyl-4-hydroxylase 3 maintains β cell glucose metabolism during fatty acid excess in mice

Prolyl hydroxylase inhibitor treatment confers whole-animal hypoxia tolerance

Prolyl 4-hydroxylation regulates Argonaute 2 stability.

Prolyl Hydroxylase PHD3 Enhances the Hypoxic Survival and G1 to S Transition of Carcinoma Cells.

Prolyl 4-hydroxylases, master regulators of the hypoxia response.

Proline hydroxylation in collagen supports integrin binding by two distinct mechanisms.

Proline hydroxylation in collagen supports integrin binding by two distinct mechanisms.

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls.

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls.

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls.

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls.

Prolyl hydroxylase domain 2 reduction enhances skeletal muscle tissue regeneration after soft tissue trauma in mice.

Prolyl hydroxylase domain 2 reduction enhances skeletal muscle tissue regeneration after soft tissue trauma in mice.

Prolyl Hydroxylase Domain Inhibitor Protects against Metabolic Disorders and Associated Kidney Disease in Obese Type 2 Diabetic Mice.

Prolyl hydroxylase PHD3 enhances the hypoxic survival and G1 to S transition of carcinoma cells

Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas, and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls

Prolyl hydroxylase domain 2 reduction enhances skeletal muscle tissue regeneration after soft tissue trauma in mice

Proline hydroxylation in collagen supports integrin binding by two distinct mechanisms

Prolyl 4-hydroxylases, master regulators of the hypoxia response

Prolyl 4-hydroxylase subunit alpha 1 (P4HA1) is a biomarker of poor prognosis in primary melanomas, and its depletion inhibits melanoma cell invasion and disrupts tumor blood vessel walls

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains

Co-expression of recombinant human collagen α1(III) chain with viral prolyl 4-Hydroxylase in P. pastoris GS115

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): high affinity peptides have a PxGP sequence motif.

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): high affinity peptides have a PxGP sequence motif.

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif

The Structural Motifs for Substrate Binding and Dimerization of theα Subunit of Collagen Prolyl 4-Hydroxylase.

The Structural Motifs for Substrate Binding and Dimerization of theα Subunit of Collagen Prolyl 4-Hydroxylase.

The Structural Motifs for Substrate Binding and Dimerization of theα Subunit of Collagen Prolyl 4-Hydroxylase.

Assembly of the elongated collagen prolyl 4-hydroxylase α2β2 heterotetramer around a central α2 dimer.

Assembly of the elongated collagen prolyl 4-hydroxylase α2β2 heterotetramer around a central α2 dimer.

Assembly of the elongated collagen prolyl 4-hydroxylase α2β2 heterotetramer around a central α2 dimer.

An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on HIF-alpha.

An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on HIF-alpha.

Assembly of the elongated collagen prolyl 4-hydroxylaseα₂β₂ heterotetramer around a central α₂ dimer

The structural motifs for substrate binding and dimerization of theα subunit of collagen prolyl 4-hydroxylase

Assembly of the elongated collagen prolyl 4-hydroxylaseα₂β₂ heterotetramer around a central α₂ dimer

The structural motifs for substrate binding and dimerization of theα subunit of collagen prolyl 4-hydroxylase

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains

Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains

Type I and type V procollagen triple helix use different subsets of the molecular ensemble for lysine post-translational modifications in the rER

Improved production of human type II procollagen in the yeast Pichia pastoris in shake flasks by a wireless-controlled fed-batch system.

Improved production of human type II procollagen in the yeast Pichia pastoris in shake flasks by a wireless-controlled fed-batch system.