ReviewCritical reviews in biochemistry and molecular biology2010
Prolyl 4-hydroxylase.
Review in Critical reviews in biochemistry and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 298 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
298 citing papers in PubMed, 1 synthesis or guideline pooled it, 601 citations in OpenAlex.
- Pooled it
- Collagen Prolyl 4-Hydroxylase: An Emerging Key Player in Cardiac Fibrosis.Journal of cardiovascular translational research · 2026Review
- Selective Hydroxylation of Collagen Model Peptides by Metal Catalysis.Chemistry & biodiversity · 2026Article
- Threonine Phosphorylation Is a Bioreversible Surrogate of Proline Hydroxylation in a Collagen Triple Helix.Journal of the American Chemical Society · 2026Article
- Plasma 4-Hydroxyproline Levels Are Associated with Diabetes in Chinese Adults: A Cross-Sectional Analysis.Metabolites · 2026Article
- Clinically approved HIF-PHIs modulate redox metabolism, cell growth, and angiogenesis independent of HIF-1α/HIF-2α.Redox biology · 2026Article
- Glutamine-dependent changes in fibroblast-derived extracellular matrix dictate cancer cell behavior.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Targeting collagen biosynthesis by small molecules inhibiting the function of the peptide-substrate-binding domain of collagen prolyl 4-hydroxylases.Scientific reports · 2026Article
- The Fusarium sacchari Effector FsP4H1 Targets the Transcription Factor DPb to Disrupt Catalase-Mediated HMolecular plant pathology · 2026Article
- Salvianolic Acid B Inhibited LH2 Expression to Reduce Collagen Synthesis in Pulmonary Fibrosis.Journal of cellular and molecular medicine · 2026Article
- Review
- Prolyl hydroxylase-dependent proteolysis enables the orthogonal hypoxia responses in plants.Nature communications · 2026Article
- Functions of prolyl hydroxylation in elastin.The Journal of biological chemistry · 2026Article
- Relevance and Safe Utilization of Amino Acids in Supplements for Human Nutrition: Lessons from Clinical and Preclinical Studies.Nutrients · 2026Review
- Recombinant humanized type VII collagen for skin repair and regeneration: prospects for reconstructing the dermal-epidermal junction.Frontiers in medicine · 2026Review
- Photodynamic Action of Hypocrellin A and Hypocrellin B against Cancer-A Review.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Mechanistic Divergence in Sulfur-Ligated Iron(III)-Alkylperoxo Reactivity: Aldehyde Oxidation Prevails over Deformylation.Angewandte Chemie (International ed. in English) · 2025Article
- Proline Metabolism in Cancer: Emerging Roles in Redox Homeostasis and Therapeutic Opportunities.Cancers · 2025Review
- Morphological and histopathological study of edible bird's nest on wound healing in mice.Journal of molecular histology · 2025Article
- Enhanced Collagen Prolyl 4-Hydroxylase Activity and Expression Promote Cancer Progression via Both Canonical and Non-Canonical Mechanisms.International journal of molecular sciences · 2025Review
238 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Posttranslational modifications can cause profound changes in protein function. Typically, these modifications are reversible, and thus provide a biochemical on-off switch. In contrast, proline residues are the substrates for an irreversible reaction that is the most common posttranslational modification in humans. This reaction, which is catalyzed by prolyl 4-hydroxylase (P4H), yields (2S,4R)-4-hydroxyproline (Hyp). The protein substrates for P4Hs are diverse. Likewise, the biological consequences of prolyl hydroxylation vary widely, and include altering protein conformation and protein-protein interactions, and enabling further modification. The best known role for Hyp is in stabilizing the collagen triple helix. Hyp is also found in proteins with collagen-like domains, as well as elastin, conotoxins, and argonaute 2. A prolyl hydroxylase domain protein acts on the hypoxia inducible factor alpha, which plays a key role in sensing molecular oxygen, and could act on inhibitory kappaB kinase and RNA polymerase II. P4Hs are not unique to animals, being found in plants and microbes as well. Here, we review the enzymic catalysts of prolyl hydroxylation, along with the chemical and biochemical consequences of this subtle but abundant posttranslational modification.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.